CC ----------------------------------------------------------------------- CC CC ENZYME nomenclature database CC CC ----------------------------------------------------------------------- CC Release 31 of June 2003 CC ----------------------------------------------------------------------- CC CC Amos Bairoch and Kristian Axelsen CC Swiss Institute of Bioinformatics (SIB) CC Centre Medical Universitaire (CMU) CC 1, rue Michel Servet CC 1211 Geneva 4 CC Switzerland CC CC Email: enzyme@isb-sib.ch CC Telephone: +41-22-379 50 50 CC Fax: +41-22-379 58 58 CC CC WWW server: http://www.expasy.org/enzyme/ CC CC ----------------------------------------------------------------------- CC This database is copyright from the Swiss Institute of Bioinformatics. CC There are no restrictions on its use by any institutions as long as CC its content is in no way modified. CC ----------------------------------------------------------------------- // ID 1.1.1.1 DE Alcohol dehydrogenase. AN Aldehyde reductase. CA An alcohol + NAD(+) = an aldehyde or ketone + NADH. CF Zinc or Iron. CC -!- Acts on primary or secondary alcohols or hemiacetals. CC -!- The animal, but not the yeast, enzyme acts also on cyclic secondary CC alcohols. PR PROSITE; PDOC00058; PR PROSITE; PDOC00059; PR PROSITE; PDOC00060; DR P80222, ADH1_ALLMI; P49645, ADH1_APTAU; P06525, ADH1_ARATH; DR P41747, ADH1_ASPFL; P12311, ADH1_BACST; Q17334, ADH1_CAEEL; DR P43067, ADH1_CANAL; P48814, ADH1_CERCA; P23991, ADH1_CHICK; DR P23236, ADH1_DROHY; P48586, ADH1_DROMN; P09370, ADH1_DROMO; DR P22246, ADH1_DROMT; P07161, ADH1_DROMU; P12854, ADH1_DRONA; DR P08843, ADH1_EMENI; P05336, ADH1_HORVU; P20369, ADH1_KLULA; DR Q07288, ADH1_KLUMA; P00333, ADH1_MAIZE; P80512, ADH1_NAJNA; DR Q9P6C8, ADH1_NEUCR; P20306, ADH1_ORYSA; P12886, ADH1_PEA ; DR P14219, ADH1_PENAM; P25141, ADH1_PETHY; O00097, ADH1_PICST; DR Q03505, ADH1_RABIT; P22797, ADH1_RANPE; P14673, ADH1_SOLTU; DR P80338, ADH1_STRCA; P13603, ADH1_TRIRP; P00330, ADH1_YEAST; DR Q07264, ADH1_ZEALU; P20368, ADH1_ZYMMO; P42327, ADH2_BACST; DR O45687, ADH2_CAEEL; O94038, ADH2_CANAL; P48815, ADH2_CERCA; DR P27581, ADH2_DROAR; P25720, ADH2_DROBU; P23237, ADH2_DROHY; DR P48587, ADH2_DROMN; P09369, ADH2_DROMO; P07160, ADH2_DROMU; DR P25721, ADH2_DROMY; P24267, ADH2_DROWH; P37686, ADH2_ECOLI; DR P54202, ADH2_EMENI; Q24803, ADH2_ENTHI; P10847, ADH2_HORVU; DR P49383, ADH2_KLULA; Q9P4C2, ADH2_KLUMA; P28032, ADH2_LYCES; DR P04707, ADH2_MAIZE; P18332, ADH2_ORYSA; P41681, ADH2_PERMA; DR O13309, ADH2_PICST; P14674, ADH2_SOLTU; P80468, ADH2_STRCA; DR P00331, ADH2_YEAST; P06758, ADH2_ZYMMO; P42328, ADH3_BACST; DR P19631, ADH3_COTJA; P25437, ADH3_ECOLI; P07754, ADH3_EMENI; DR P44557, ADH3_HAEIN; P10848, ADH3_HORVU; P49384, ADH3_KLULA; DR P39450, ADH3_PASPI; P14675, ADH3_SOLTU; P73138, ADH3_SYNY3; DR P07246, ADH3_YEAST; P49385, ADH4_KLULA; P10127, ADH4_YEAST; DR P38113, ADH5_YEAST; P28332, ADH6_HUMAN; P40394, ADH7_HUMAN; DR Q64437, ADH7_MOUSE; P41682, ADH7_RAT ; Q64413, ADHA_GEOBU; DR Q64415, ADHA_GEOKN; P07327, ADHA_HUMAN; P00329, ADHA_MOUSE; DR P41680, ADHA_PERMA; P06757, ADHA_RAT ; O31186, ADHA_RHIME; DR P25405, ADHA_UROHA; P00325, ADHB_HUMAN; P25406, ADHB_UROHA; DR P33744, ADHE_CLOAB; P17547, ADHE_ECOLI; P00327, ADHE_HORSE; DR Q09669, ADHF_SCHPO; P00326, ADHG_HUMAN; P81600, ADHH_GADMO; DR P72324, ADHI_RHOSH; P81601, ADHL_GADMO; P39451, ADHP_ECOLI; DR P08319, ADHP_HUMAN; O46649, ADHP_RABIT; O46650, ADHQ_RABIT; DR P00328, ADHS_HORSE; Q96533, ADHX_ARATH; Q17335, ADHX_CAEEL; DR P46415, ADHX_DROME; P19854, ADHX_HORSE; P11766, ADHX_HUMAN; DR P93629, ADHX_MAIZE; P28474, ADHX_MOUSE; P80360, ADHX_MYXGL; DR P81431, ADHX_OCTVU; P93436, ADHX_ORYSA; P80572, ADHX_PEA ; DR O19053, ADHX_RABIT; P12711, ADHX_RAT ; P79896, ADHX_SPAAU; DR P80467, ADHX_UROHA; P14940, ADH_ALCEU ; P30350, ADH_ANAPL ; DR Q9NAR7, ADH_BACOL ; Q00669, ADH_DROAD ; P21518, ADH_DROAF ; DR P25139, ADH_DROAM ; P48584, ADH_DROBO ; Q00670, ADH_DROCR ; DR P22245, ADH_DRODI ; P28483, ADH_DROER ; P48585, ADH_DROFL ; DR P51551, ADH_DROGR ; Q09009, ADH_DROGU ; P51549, ADH_DROHA ; DR P21898, ADH_DROHE ; Q07588, ADH_DROIM ; Q27404, ADH_DROLA ; DR P10807, ADH_DROLE ; P07162, ADH_DROMA ; Q09010, ADH_DROMD ; DR P00334, ADH_DROME ; Q00671, ADH_DROMM ; Q00672, ADH_DRONI ; DR P07159, ADH_DROOR ; P37473, ADH_DROPE ; P23361, ADH_DROPI ; DR P23277, ADH_DROPL ; P07158, ADH_DROPS ; P07163, ADH_DROSI ; DR P23278, ADH_DROSL ; Q03384, ADH_DROSU ; P28484, ADH_DROTE ; DR P51550, ADH_DROTS ; Q05114, ADH_DROWI ; P26719, ADH_DROYA ; DR P17648, ADH_FRAAN ; P26325, ADH_GADCA ; P28469, ADH_MACMU ; DR P48977, ADH_MALDO ; P14139, ADH_PAPHA ; P25988, ADH_SCAAL ; DR P00332, ADH_SCHPO ; P39462, ADH_SULSO ; P50381, ADH_SULSR ; DR P51552, ADH_ZAPTU ; P32771, FADH_YEAST; P71017, GBSB_BACSU; DR P33010, TERD_PSESP; // ID 1.1.1.2 DE Alcohol dehydrogenase (NADP+). AN Aldehyde reductase (NADPH). CA An alcohol + NADP(+) = an aldehyde + NADPH. CF Zinc. CC -!- Some members of this group oxidize only primary alcohols; others act CC also on secondary alcohols. CC -!- May be identical with EC 1.1.1.19, EC 1.1.1.33 and EC 1.1.1.55. CC -!- A-specific with respect to NADPH. PR PROSITE; PDOC00061; DR P35630, ADH1_ENTHI; Q24857, ADH3_ENTHI; O57380, ADH4_RANPE; DR P25984, ADH_CLOBE ; P75214, ADH_MYCPN ; P31975, ADH_MYCTU ; DR P14941, ADH_THEBR ; O70473, AKA1_CRIGR; P14550, AKA1_HUMAN; DR Q9JII6, AKA1_MOUSE; P50578, AKA1_PIG ; P51635, AKA1_RAT ; DR Q9UUN9, ALD2_SPOSA; P27800, ALDX_SPOSA; // ID 1.1.1.3 DE Homoserine dehydrogenase. CA L-homoserine + NAD(P)(+) = L-aspartate 4-semialdehyde + NAD(P)H. CC -!- The yeast enzyme acts most rapidly with NAD(+); Neurospora enzyme CC with NADP(+). Enzyme from E.coli is a multifunctional protein, which CC also catalyzes the reaction of EC 2.7.2.4. PR PROSITE; PDOC00800; DR P00561, AK1H_ECOLI; P27725, AK1H_SERMA; P00562, AK2H_ECOLI; DR P49079, AKH1_MAIZE; P49080, AKH2_MAIZE; P57290, AKH_BUCAI ; DR Q8K9U9, AKH_BUCAP ; P37142, AKH_DAUCA ; P44505, AKH_HAEIN ; DR P19582, DHOM_BACSU; P08499, DHOM_CORGL; Q9ZL20, DHOM_HELPJ; DR P56429, DHOM_HELPY; Q9CGD8, DHOM_LACLA; P52985, DHOM_LACLC; DR P37143, DHOM_METGL; P46806, DHOM_MYCLE; Q10601, DHOM_MYCTU; DR P29365, DHOM_PSEAE; O94671, DHOM_SCHPO; P52986, DHOM_SYNY3; DR P31116, DHOM_YEAST; P37144, DHON_METGL; // ID 1.1.1.4 DE (R,R)-butanediol dehydrogenase. AN Butyleneglycol dehydrogenase. AN D-butanediol dehydrogenase. AN D-(-)-butanediol dehydrogenase. AN Butylene glycol dehydrogenase. AN Diacetyl (acetoin) reductase. AN D-aminopropanol dehydrogenase. AN D-aminopropanol dehydrogenase. AN 1-amino-2-propanol dehydrogenase. AN 2,3-butanediol dehydrogenase. AN D-1-amino-2-propanol dehydrogenase. AN (R)-diacetyl reductase. AN (R)-2,3-butanediol dehydrogenase. AN D-1-amino-2-propanol:NAD(2) oxidoreductase. AN 1-amino-2-propanol oxidoreductase. AN Aminopropanol oxidoreductase. CA (R,R)-butane-2,3-diol + NAD(+) = (R)-acetoin + NADH. CC -!- Also converts diacetyl into acetoin with NADH as reductant. DR P39714, BDH1_YEAST; // ID 1.1.1.5 DE Acetoin dehydrogenase. AN Diacetyl reductase. CA Acetoin + NAD(+) = diacetyl + NADH. CC -!- NADP(+) also acts. PR PROSITE; PDOC00060; DR Q48436, BUDC_KLEPN; Q04520, BUDC_KLETE; // ID 1.1.1.6 DE Glycerol dehydrogenase. AN NAD-linked glycerol dehydrogenase. CA Glycerol + NAD(+) = glycerone + NADH. CC -!- Also acts on 1,2-propanediol. PR PROSITE; PDOC00059; DR P32816, GLDA_BACST; P45511, GLDA_CITFR; P32665, GLDA_ECOLI; DR P50173, GLDA_PSEPU; // ID 1.1.1.7 DE Propanediol-phosphate dehydrogenase. CA Propane-1,2-diol 1-phosphate + NAD(+) = hydroxyacetone phosphate + CA NADH. // ID 1.1.1.8 DE Glycerol-3-phosphate dehydrogenase (NAD+). AN Glycerophosphate dehydrogenase (NAD). AN NAD-dependent glycerol phosphate dehydrogenase. AN NAD-dependent glycerol-3-phosphate dehydrogenase. CA Sn-glycerol 3-phosphate + NAD(+) = glycerone phosphate + NADH. CC -!- Also acts on 1,2-propanediol phosphate and glycerone sulfate (but CC with a much lower affinity). PR PROSITE; PDOC00740; DR Q9UVF4, GPD1_YARLI; Q00055, GPD1_YEAST; Q9HGY2, GPD1_ZYGRO; DR P41911, GPD2_YEAST; Q9HGY1, GPD2_ZYGRO; P34517, GPDA_CAEEL; DR P52425, GPDA_CUPLA; Q27556, GPDA_DROAE; Q27567, GPDA_DROEZ; DR O97463, GPDA_DROKA; P13706, GPDA_DROME; Q27928, GPDA_DROPS; DR P07735, GPDA_DROVI; O57656, GPDA_FUGRU; P21695, GPDA_HUMAN; DR P13707, GPDA_MOUSE; P08507, GPDA_RABIT; O35077, GPDA_RAT ; DR P21696, GPDA_SCHPO; P90593, GPDA_TRYBB; Q26756, GPDA_TRYBR; DR Q09845, GPDB_SCHPO; // ID 1.1.1.9 DE D-xylulose reductase. AN Xylitol dehydrogenase. CA Xylitol + NAD(+) = D-xylulose + NADH. CC -!- Also acts as an L-erythrulose reductase. PR PROSITE; PDOC00058; DR P22144, XYL2_PICST; P83049, XYL2_PIG ; // ID 1.1.1.10 DE L-xylulose reductase. CA Xylitol + NADP(+) = L-xylulose + NADPH. DI Pentosuria; MIM:260800. // ID 1.1.1.11 DE D-arabinitol 4-dehydrogenase. CA D-arabinitol + NAD(+) = D-xylulose + NADH. DR O52720, DALD_KLEPN; P58708, DALD_RALSO; P58709, DALD_YERPE; // ID 1.1.1.12 DE L-arabinitol 4-dehydrogenase. CA L-arabinitol + NAD(+) = L-xylulose + NADH. // ID 1.1.1.13 DE L-arabinitol 2-dehydrogenase (ribulose forming). CA L-arabinitol + NAD(+) = L-ribulose + NADH. // ID 1.1.1.14 DE L-iditol 2-dehydrogenase. AN Polyol dehydrogenase. AN Sorbitol dehydrogenase. AN Glucitol dehydrogenase. CA L-iditol + NAD(+) = L-sorbose + NADH. CC -!- Also acts on D-glucitol (giving D-fructose) and other closely related CC sugar alcohols. DI Sorbitol dehydrogenase deficiency; MIM:182500. PR PROSITE; PDOC00058; DR Q9Z9U1, DHSO_BACHD; Q06004, DHSO_BACSU; Q02912, DHSO_BOMMO; DR Q00796, DHSO_HUMAN; Q64442, DHSO_MOUSE; P27867, DHSO_RAT ; DR Q59787, DHSO_RHOSH; P36624, DHSO_SCHPO; P07846, DHSO_SHEEP; DR P35497, DHSO_YEAST; // ID 1.1.1.15 DE D-iditol 2-dehydrogenase. CA D-iditol + NAD(+) = D-sorbose + NADH. CC -!- Also converts xylitol into L-xylulose and L-glucitol into L-fructose. // ID 1.1.1.16 DE Galactitol 2-dehydrogenase. CA Galactitol + NAD(+) = D-tagatose + NADH. CC -!- Also converts other alditols containing an L-threo-configuration CC adjacent to a primary alcohol group into the corresponding sugars. // ID 1.1.1.17 DE Mannitol-1-phosphate 5-dehydrogenase. CA D-mannitol 1-phosphate + NAD(+) = D-fructose 6-phosphate + NADH. PR PROSITE; PDOC00751; DR Q9K681, MTLD_BACHD; Q45421, MTLD_BACST; P42957, MTLD_BACSU; DR P57634, MTLD_BUCAI; Q8K912, MTLD_BUCAP; Q89A37, MTLD_BUCBP; DR O65992, MTLD_CLOAB; Q8XDG9, MTLD_ECO57; Q8FCB7, MTLD_ECOL6; DR P09424, MTLD_ECOLI; P27543, MTLD_ENTFA; Q9XBM6, MTLD_KLEPN; DR Q9CJH1, MTLD_LACLA; P55800, MTLD_MYCMY; P78008, MTLD_MYCPN; DR Q98PH2, MTLD_MYCPU; Q8EN87, MTLD_OCEIH; Q9CLY7, MTLD_PASMU; DR Q8Z2E0, MTLD_SALTI; Q8ZL67, MTLD_SALTY; Q99SA1, MTLD_STAAM; DR Q02418, MTLD_STRMU; Q97SH1, MTLD_STRPN; Q8DR31, MTLD_STRR6; DR Q8RCS0, MTLD_THETN; Q9KKQ6, MTLD_VIBCH; Q87SQ3, MTLD_VIBPA; DR Q8DEF5, MTLD_VIBVU; Q8Z9X0, MTLD_YERPE; // ID 1.1.1.18 DE Myo-inositol 2-dehydrogenase. CA Myo-inositol + NAD(+) = 2,4,6/3,5-pentahydroxycyclohexanone + NADH. DR P26935, MI2D_BACSU; O68965, MI2D_RHIME; // ID 1.1.1.19 DE Glucuronate reductase. AN Glucuronate dehydrogenase. CA L-gulonate + NADP(+) = D-glucuronate + NADPH. CC -!- Also reduces D-galacturonate. CC -!- May be identical with EC 1.1.1.2. // ID 1.1.1.20 DE Glucuronolactone reductase. CA L-gulono-1,4-lactone + NADP(+) = D-glucurono-3,6-lactone + NADPH. // ID 1.1.1.21 DE Aldehyde reductase. AN Aldose reductase. AN Polyol dehydrogenase (NADP+). CA Alditol + NAD(P)(+) = aldose + NAD(P)H. CC -!- Wide specificity. CC -!- Formerly EC 1.1.1.139. PR PROSITE; PDOC00061; DR P21300, ALD1_MOUSE; P45377, ALD2_MOUSE; P16116, ALDR_BOVIN; DR P23901, ALDR_HORVU; P15121, ALDR_HUMAN; P45376, ALDR_MOUSE; DR P80276, ALDR_PIG ; P15122, ALDR_RABIT; P07943, ALDR_RAT ; // ID 1.1.1.22 DE UDP-glucose 6-dehydrogenase. CA UDP-glucose + 2 NAD(+) + H(2)O = UDP-glucuronate + 2 NADH. CC -!- Also acts on UDP-2-deoxyglucose. DR Q47329, UDG5_ECOLI; O33952, UDG8_ECOLI; Q04872, UDG_ECO11 ; DR P76373, UDG_ECOLI ; O86422, UDG_PSEAE ; O54068, UDG_RHIME ; DR Q92GB1, UDG_RICCN ; O05973, UDG_RICPR ; Q04873, UDG_SALTY ; DR P37791, UDG_SHIFL ; Q57346, UDG_STRPN ; Q07172, UDG_STRPY ; DR P12378, UGDH_BOVIN; Q19905, UGDH_CAEEL; O02373, UGDH_DROME; DR O60701, UGDH_HUMAN; O70475, UGDH_MOUSE; O70199, UGDH_RAT ; DR Q96558, UGDH_SOYBN; // ID 1.1.1.23 DE Histidinol dehydrogenase. CA L-histidinol + 2 NAD(+) + H(2)O = L-histidine + 2 NADH. CC -!- Also oxidizes L-histidinal. CC -!- The Neurospora enzyme also catalyzes the reactions of EC 3.5.4.19 CC and EC 3.6.1.31. PR PROSITE; PDOC00534; DR O74712, HIS2_CANAL; O13471, HIS2_KLULA; P07685, HIS2_NEUCR; DR P45353, HIS2_PICPA; Q12670, HIS2_SACBA; P00815, HIS2_YEAST; DR Q8UHX1, HISX_AGRT5; O66976, HISX_AQUAE; Q9C5U8, HISX_ARATH; DR O30027, HISX_ARCFU; P18786, HISX_AZOBR; Q9K6Z2, HISX_BACHD; DR O34651, HISX_BACSU; Q8ABA9, HISX_BACTN; Q8G4S9, HISX_BIFLO; DR P59397, HISX_BRAJA; P24226, HISX_BRAOC; Q8YF59, HISX_BRUME; DR Q8G2R2, HISX_BRUSU; P57201, HISX_BUCAI; Q9ZHE6, HISX_BUCAP; DR P59398, HISX_BUCBP; Q9RQ88, HISX_BUCDN; Q9RQ82, HISX_BUCMH; DR Q9RQ85, HISX_BUCSC; Q9PM77, HISX_CAMJE; Q9A5V1, HISX_CAUCR; DR Q8KEY6, HISX_CHLTE; Q97KI2, HISX_CLOAB; Q8FNZ0, HISX_COREF; DR Q8NNT5, HISX_CORGL; Q9RSI4, HISX_DEIRA; Q8X8T3, HISX_ECO57; DR Q8FG52, HISX_ECOL6; P06988, HISX_ECOLI; P44001, HISX_HAEIN; DR Q9HPW5, HISX_HALN1; Q8GDP4, HISX_HELMO; Q02136, HISX_LACLA; DR P59399, HISX_LACPL; Q8F393, HISX_LEPIN; Q92E84, HISX_LISIN; DR Q8Y9G1, HISX_LISMO; Q8TL41, HISX_METAC; Q58851, HISX_METJA; DR Q8TXG3, HISX_METKA; Q8PZR8, HISX_METMA; O26327, HISX_METTH; DR Q9CC57, HISX_MYCLE; P28736, HISX_MYCSM; O08396, HISX_MYCTU; DR Q9JTH9, HISX_NEIMA; Q9JYH8, HISX_NEIMB; Q8ESR8, HISX_OCEIH; DR Q9CLM4, HISX_PASMU; Q9HVW9, HISX_PSEAE; P59400, HISX_PSEPK; DR Q87WV5, HISX_PSESM; Q8ZY17, HISX_PYRAE; O59626, HISX_PYRFU; DR Q8XV79, HISX_RALSO; Q8GKZ1, HISX_SALEN; Q8Z5K0, HISX_SALTI; DR P10370, HISX_SALTY; Q9P777, HISX_SCHPO; Q8EFB1, HISX_SHEON; DR P59401, HISX_SHIFL; Q99QW3, HISX_STAAM; Q8CQ95, HISX_STAEP; DR P16245, HISX_STRCO; Q8DTQ7, HISX_STRMU; O33775, HISX_SULSO; DR Q970Y9, HISX_SULTO; Q8DGR2, HISX_SYNEL; Q9X0D1, HISX_THEMA; DR Q8R882, HISX_THETN; Q9L6I1, HISX_THIRO; Q9F854, HISX_VIBCH; DR Q87QL1, HISX_VIBPA; Q8D8Q0, HISX_VIBVU; Q8PLG9, HISX_XANAC; DR Q8P9P2, HISX_XANCP; Q9PBC5, HISX_XYLFA; Q87C29, HISX_XYLFT; DR Q8ZFX5, HISX_YERPE; Q9RH05, HISX_ZYMMO; Q8YSM8, HIX1_ANASP; DR Q989E7, HIX1_RHILO; Q92S26, HIX1_RHIME; P73058, HIX1_SYNY3; DR Q8YWL4, HIX2_ANASP; Q988P7, HIX2_RHILO; Q930I4, HIX2_RHIME; DR P72946, HIX2_SYNY3; Q987C6, HIX3_RHILO; // ID 1.1.1.24 DE Quinate 5-dehydrogenase. CA Quinate + NAD(+) = 5-dehydroquinate + NADH. DR P25415, DHQA_EMENI; P11635, DHQA_NEUCR; // ID 1.1.1.25 DE Shikimate 5-dehydrogenase. AN 5-dehydroshikimate reductase. CA Shikimate + NADP(+) = 5-dehydroshikimate + NADPH. DR P56961, ARDE_CHLMU; Q9Z6M4, ARDE_CHLPN; O84375, ARDE_CHLTR; DR P07547, ARO1_EMENI; Q12659, ARO1_PNECA; Q9P7R0, ARO1_SCHPO; DR P08566, ARO1_YEAST; Q8UJC5, AROE_AGRT5; Q8YVC1, AROE_ANASP; DR O67049, AROE_AQUAE; O27957, AROE_ARCFU; Q9KD93, AROE_BACHD; DR P54374, AROE_BACSU; Q8YE20, AROE_BRUME; Q44607, AROE_BUCAI; DR P46240, AROE_BUCAP; P59414, AROE_BUCBP; Q9AC57, AROE_CAUCR; DR Q8XMI8, AROE_CLOPE; Q9X5C9, AROE_CORGL; Q8X8F9, AROE_ECO57; DR P15770, AROE_ECOLI; P43876, AROE_HAEIN; Q9HS68, AROE_HALN1; DR Q9ZJX8, AROE_HELPJ; P56119, AROE_HELPY; Q9CES7, AROE_LACLA; DR Q92EG7, AROE_LISIN; Q8THC3, AROE_METAC; Q58484, AROE_METJA; DR Q8TZ24, AROE_METKA; Q8PXE6, AROE_METMA; O26344, AROE_METTH; DR P95337, AROE_NEICI; P95340, AROE_NEIFL; P95361, AROE_NEIGO; DR P95368, AROE_NEILA; P56991, AROE_NEIMA; P56992, AROE_NEIMB; DR P95389, AROE_NEIMU; P95400, AROE_NEIPH; P95399, AROE_NEIPO; DR P57932, AROE_PASMU; P43904, AROE_PSEAE; Q9V1H7, AROE_PYRAB; DR Q8U0A6, AROE_PYRFU; Q98DY3, AROE_RHILO; Q92TF0, AROE_RHIME; DR Q8Z1W5, AROE_SALTI; Q8ZLN1, AROE_SALTY; Q99TQ3, AROE_STAAM; DR Q8NWA1, AROE_STAAW; Q8CP09, AROE_STAEP; Q8P031, AROE_STRP8; DR Q97Q55, AROE_STRPN; Q99YQ9, AROE_STRPY; P74591, AROE_SYNY3; DR Q9HLE4, AROE_THEAC; Q9WYI1, AROE_THEMA; Q8RAG2, AROE_THETN; DR Q9KVT3, AROE_VIBCH; Q87KE4, AROE_VIBPA; Q8DDD4, AROE_VIBVU; DR Q8PFE9, AROE_XANAC; Q8P3W6, AROE_XANCP; Q9PFN3, AROE_XYLFA; DR Q87BC5, AROE_XYLFT; Q8ZJ74, AROE_YERPE; Q8Y9N5, AROX_LISMO; // ID 1.1.1.26 DE Glycolate reductase. AN Glyoxylic acid reductase. AN NADH-dependent glyoxylate reductase. CA Glycolate + NAD(+) = glyoxylate + NADH. CC -!- Reduces glyoxylate to glycolate or hydroxypyruvate to D-glycerate. // ID 1.1.1.27 DE L-lactate dehydrogenase. AN L-lactic acid dehydrogenase. AN L-lactic dehydrogenase. CA (S)-lactate + NAD(+) = pyruvate + NADH. CC -!- Also oxidizes other (S)-2-hydroxymonocarboxylic acids. CC -!- NADP(+) acts, more slowly, with the animal, but not the CC bacterial, enzyme. DI Exertional myoglobinuria; MIM:150000. PR PROSITE; PDOC00062; DR P59050, LDH1_BIFLO; Q01462, LDH1_LACLA; P56512, LDH1_LACPL; DR Q27743, LDH1_PLAFD; Q99WY2, LDH1_STAAM; P19869, LDH2_BIFLO; DR Q9CII4, LDH2_LACLA; P59390, LDH2_LACPL; P13774, LDH2_PLAFA; DR Q99R35, LDH2_STAAM; Q8NUM9, LDH2_STAAW; Q9PW06, LDHA_ALLMI; DR Q9W7M6, LDHA_AMBME; Q9YGL2, LDHA_ANGRO; P19858, LDHA_BOVIN; DR Q9PVK5, LDHA_BRARE; Q98SL2, LDHA_CAICA; O93619, LDHA_CHAAC; DR O93541, LDHA_CHAGU; P00340, LDHA_CHICK; Q9PW07, LDHA_COLLI; DR O93401, LDHA_CORNI; Q9W7K5, LDHA_CYPCA; Q9PW61, LDHA_DISEL; DR O93544, LDHA_DISMA; O93542, LDHA_ELEMC; Q92055, LDHA_FUNHE; DR O93620, LDHA_GILMI; O93540, LDHA_GOBGI; O93537, LDHA_HARAN; DR P22988, LDHA_HORVU; P00338, LDHA_HUMAN; O93545, LDHA_LEPNU; DR Q9BE24, LDHA_MACFA; Q9XT87, LDHA_MONDO; P06151, LDHA_MOUSE; DR Q9PRH8, LDHA_NOTAN; O93539, LDHA_NOTCO; O93538, LDHA_PARCR; DR O93543, LDHA_PARMG; O93546, LDHA_PATTE; Q98SL0, LDHA_PELSJ; DR P00339, LDHA_PIG ; Q9W7L3, LDHA_PYTRG; P13491, LDHA_RABIT; DR P04642, LDHA_RAT ; Q9PW58, LDHA_RHIDE; Q9P4B6, LDHA_RHIOR; DR Q9W7L5, LDHA_SCEUN; P79912, LDHA_SCEWO; O13276, LDHA_SPHAG; DR O13277, LDHA_SPHID; O13278, LDHA_SPHLU; P00341, LDHA_SQUAC; DR Q9PT43, LDHA_TRASC; P42120, LDHA_XENLA; Q9PW05, LDHB_ALLMI; DR P13743, LDHB_ANAPL; Q9PVK4, LDHB_BRARE; Q98SL1, LDHB_CAICA; DR P00337, LDHB_CHICK; Q9PW04, LDHB_COLLI; P20373, LDHB_FUNHE; DR P42122, LDHB_FUNPA; P22989, LDHB_HORVU; P07195, LDHB_HUMAN; DR Q9XT86, LDHB_MONDO; P16125, LDHB_MOUSE; Q98SK9, LDHB_PELSJ; DR P00336, LDHB_PIG ; P13490, LDHB_RABIT; P42123, LDHB_RAT ; DR Q9P4B5, LDHB_RHIOR; Q9W7L4, LDHB_SCEUN; P79913, LDHB_SCEWO; DR Q9YI05, LDHB_SQUAC; Q9PT42, LDHB_TRASC; P42119, LDHB_XENLA; DR Q06176, LDHC_FUNHE; P07864, LDHC_HUMAN; P00342, LDHC_MOUSE; DR Q9TSX5, LDHC_PIG ; P19629, LDHC_RAT ; Q29563, LDHC_VULVU; DR P42121, LDHC_XENLA; Q9BYZ2, LDHL_HUMAN; P14561, LDHP_BACPS; DR P20619, LDHX_BACPS; Q07251, LDH_ALCEU ; P10655, LDH_BACCA ; DR Q59244, LDH_BACCL ; Q9K5Z8, LDH_BACHD ; P00345, LDH_BACME ; DR P00344, LDH_BACST ; P13714, LDH_BACSU ; O51114, LDH_BORBU ; DR P93052, LDH_BOTBR ; Q27888, LDH_CAEEL ; Q97MD1, LDH_CLOAB ; DR Q8XP62, LDH_CLOPE ; Q8NLN0, LDH_CORGL ; P50933, LDH_DEIRA ; DR Q95028, LDH_DROME ; P00343, LDH_LACCA ; O32765, LDH_LACHE ; DR P04034, LDH_LACLC ; P56511, LDH_LACPE ; P50934, LDH_LACSK ; DR Q92F65, LDH_LISIN ; P33380, LDH_LISMO ; P29038, LDH_MAIZE ; DR O52354, LDH_MYCGA ; P47698, LDH_MYCGE ; P33572, LDH_MYCHY ; DR P78007, LDH_MYCPN ; Q98PG4, LDH_MYCPU ; Q59645, LDH_PEDAC ; DR P33571, LDH_PETMA ; Q9P7P7, LDH_SCHPO ; Q59828, LDH_STRBO ; DR P26283, LDH_STRMU ; O33734, LDH_STRPN ; Q99ZN5, LDH_STRPY ; DR Q60009, LDH_STRTR ; P13715, LDH_THEAQ ; P06150, LDH_THECA ; DR P16115, LDH_THEMA ; Q27797, LDH_TOXGO ; // ID 1.1.1.28 DE D-lactate dehydrogenase. AN D-lactic acid dehydrogenase. AN D-lactic dehydrogenase. CA (R)-lactate + NAD(+) = pyruvate + NADH. PR PROSITE; PDOC00063; DR P06149, DLD_ECOLI ; P52643, LDHD_ECOLI; P45295, LDHD_HAEIN; DR P26297, LDHD_LACDE; P30901, LDHD_LACHE; P26298, LDHD_LACPE; DR P51011, LDHD_LEUMC; Q59642, LDHD_PEDAC; // ID 1.1.1.29 DE Glycerate dehydrogenase. AN Hydroxypyruvate reductase. AN Hydroxypyruvate dehydrogenase. CA (R)-glycerate + NAD(+) = hydroxypyruvate + NADH. DI Oxalosis II (glycericaciduria); MIM:260000. PR PROSITE; PDOC00063; DR P13443, DHGY_CUCSA; P36234, DHGY_HYPME; Q59516, DHGY_METEX; // ID 1.1.1.30 DE 3-hydroxybutyrate dehydrogenase. AN D-beta-hydroxybutyrate dehydrogenase. CA (R)-3-hydroxybutanoate + NAD(+) = acetoacetate + NADH. CC -!- Also oxidizes other 3-hydroxymonocarboxylic acids. PR PROSITE; PDOC00060; DR Q9X6U2, BDHA_ALCEU; O86034, BDHA_RHIME; Q02337, BDH_BOVIN ; DR Q02338, BDH_HUMAN ; P29147, BDH_RAT ; // ID 1.1.1.31 DE 3-hydroxyisobutyrate dehydrogenase. CA 3-hydroxy-2-methylpropanoate + NAD(+) = 2-methyl-3-oxopropanoate + CA NADH. DI 3-hydroxyisobutyricaciduria; MIM:236795. PR PROSITE; PDOC00697; DR Q9SUC0, D3HI_ARATH; Q9V8M5, D3HI_DROME; P31937, D3HI_HUMAN; DR P32185, D3HI_RABIT; P29266, D3HI_RAT ; Q9XTI0, DH3I_CAEEL; DR O53814, MMSB_MYCTU; P28811, MMSB_PSEAE; // ID 1.1.1.32 DE Mevaldate reductase. CA (R)-mevalonate + NAD(+) = mevaldate + NADH. // ID 1.1.1.33 DE Mevaldate reductase (NADPH). CA (R)-mevalonate + NADP(+) = mevaldate + NADPH. CC -!- May be identical with EC 1.1.1.2. // ID 1.1.1.34 DE Hydroxymethylglutaryl-CoA reductase (NADPH). AN 3-hydroxy-3-methylglutaryl-coenzyme A reductase. AN HMG-CoA reductase. CA (R)-mevalonate + CoA + 2 NADP(+) = (S)-3-hydroxy-3-methylglutaryl-CoA + CA 2 NADPH. CC -!- The enzyme is inactivated by EC 2.7.1.109 and reactivated by CC EC 3.1.3.47. PR PROSITE; PDOC00064; DR P14891, HMD1_ARATH; P34135, HMD1_DICDI; O64966, HMD1_GOSHI; DR P29057, HMD1_HEVBR; P48019, HMD1_ORYSA; P48020, HMD1_SOLTU; DR P12683, HMD1_YEAST; P43256, HMD2_ARATH; Q9XEL8, HMD2_CAPAN; DR P34136, HMD2_DICDI; O64967, HMD2_GOSHI; P29058, HMD2_HEVBR; DR P48022, HMD2_LYCES; Q41437, HMD2_SOLTU; P12684, HMD2_YEAST; DR Q00583, HMD3_HEVBR; Q9XHL5, HMD3_ORYSA; Q41438, HMD3_SOLTU; DR Q9YAS4, HMDH_AERPE; O76819, HMDH_AGRIP; O28538, HMDH_ARCFU; DR Q9Y7D2, HMDH_ASPTE; P54960, HMDH_BLAGE; P48021, HMDH_CAMAC; DR Q03163, HMDH_CATRO; P00347, HMDH_CRIGR; P14773, HMDH_DROME; DR Q12577, HMDH_GIBFU; Q59468, HMDH_HALVO; P04035, HMDH_HUMAN; DR O24594, HMDH_MAIZE; P09610, HMDH_MESAU; Q58116, HMDH_METJA; DR O26662, HMDH_METTH; Q01237, HMDH_MOUSE; Q01559, HMDH_NICSY; DR Q12649, HMDH_PHYBL; O74164, HMDH_PICJA; Q9V1R3, HMDH_PYRAB; DR O59469, HMDH_PYRHO; Q29512, HMDH_RABIT; P51639, HMDH_RAT ; DR P16237, HMDH_SCHMA; Q10283, HMDH_SCHPO; P16393, HMDH_STRPU; DR O08424, HMDH_SULSO; P20715, HMDH_XENLA; // ID 1.1.1.35 DE 3-hydroxyacyl-CoA dehydrogenase. AN Beta-hydroxyacyl dehydrogenase. AN Beta-keto-reductase. CA (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH. CC -!- Also oxidizes S-3-hydroxyacyl-N-acylthioethanolamine and CC S-3-hydroxyacylhydrolipoate. CC -!- Some enzymes act, more slowly, with NADP(+). CC -!- Broad specificity to acyl chain-length (cf. EC 1.1.1.211). DI Peroxisomal bifunctional enzyme deficiency; MIM:261515. PR PROSITE; PDOC00065; PR PROSITE; PDOC00060; DR P40939, ECHA_HUMAN; Q29554, ECHA_PIG ; Q64428, ECHA_RAT ; DR P55100, ECHP_CAVPO; Q08426, ECHP_HUMAN; Q9DBM2, ECHP_MOUSE; DR P07896, ECHP_RAT ; Q8X8I2, FADB_ECO57; P21177, FADB_ECOLI; DR Q8Z3C6, FADB_SALTI; Q9L6L5, FADB_SALTY; Q8ZAN0, FADB_YERPE; DR P28793, FAOB_PSEFR; P34439, HCD1_CAEEL; O02691, HCD2_BOVIN; DR P41938, HCD2_CAEEL; O18404, HCD2_DROME; Q99714, HCD2_HUMAN; DR O08756, HCD2_MOUSE; O70351, HCD2_RAT ; Q16836, HCDH_HUMAN; DR Q61425, HCDH_MOUSE; P00348, HCDH_PIG ; Q9WVK7, HCDH_RAT ; DR P77399, YFCX_ECOLI; // ID 1.1.1.36 DE Acetoacetyl-CoA reductase. CA (R)-3-hydroxyacyl-CoA + NADP(+) = 3-oxoacyl-CoA + NADPH. PR PROSITE; PDOC00060; DR P50203, PHAB_ACISP; P50204, PHAB_PARDE; P14697, PHBB_ALCEU; DR P45375, PHBB_CHRVI; P50205, PHBB_RHIME; P23238, PHBB_ZOORA; // ID 1.1.1.37 DE Malate dehydrogenase. AN Malic dehydrogenase. CA (S)-malate + NAD(+) = oxaloacetate + NADH. CC -!- Also oxidizes some other 2-hydroxydicarboxylic acids. PR PROSITE; PDOC00066; DR P93819, MDHC_ARATH; Q9SML8, MDHC_BETVU; Q04820, MDHC_ECHGR; DR P40925, MDHC_HUMAN; Q08062, MDHC_MAIZE; O48905, MDHC_MEDSA; DR O24047, MDHC_MESCR; P14152, MDHC_MOUSE; P11708, MDHC_PIG ; DR P22133, MDHC_YEAST; P57106, MDHD_ARATH; Q9ZP05, MDHG_ARATH; DR Q43743, MDHG_BRANA; P19446, MDHG_CITLA; P46488, MDHG_CUCSA; DR Q42972, MDHG_ORYSA; P37228, MDHG_SOYBN; Q9XFW3, MDHH_BRANA; DR O82399, MDHI_ARATH; Q9ZP06, MDHM_ARATH; Q43744, MDHM_BRANA; DR O02640, MDHM_CAEEL; Q42686, MDHM_CHLRE; P17783, MDHM_CITLA; DR P46487, MDHM_EUCGU; P83373, MDHM_FRAAN; P40926, MDHM_HUMAN; DR P08249, MDHM_MOUSE; P00346, MDHM_PIG ; P04636, MDHM_RAT ; DR P37227, MDHM_SCHMA; P17505, MDHM_YEAST; P32419, MDHP_YEAST; DR P80540, MDH_ACIDE ; P19977, MDH_ACTMI ; Q9YEA1, MDH_AERPE ; DR O67655, MDH_AQUAE ; Q9ZF99, MDH_AQUAR ; O08349, MDH_ARCFU ; DR Q9K849, MDH_BACHD ; Q59202, MDH_BACIS ; P49814, MDH_BACSU ; DR Q9X4K8, MDH_BACTC ; P80542, MDH_BREDI ; P80543, MDH_BREVE ; DR P80537, MDH_BURCE ; P80536, MDH_BURPS ; P80040, MDH_CHLAU ; DR P80039, MDH_CHLTE ; P80038, MDH_CHLVI ; P80539, MDH_COMAC ; DR P06994, MDH_ECOLI ; P44427, MDH_HAEIN ; Q07841, MDH_HALMA ; DR Q9HMV8, MDH_HALN1 ; P80037, MDH_HELGE ; P19978, MDH_KIBAR ; DR P80535, MDH_KLEPN ; P16142, MDH_METFE ; Q60176, MDH_METJA ; DR P19979, MDH_MICGL ; P50917, MDH_MYCLE ; O54592, MDH_MYCTU ; DR P10887, MDH_NITAL ; P19980, MDH_PHEIM ; P37226, MDH_PHOPR ; DR P19981, MDH_PLAVE ; P80538, MDH_PSEIN ; Q9V0D5, MDH_PYRAB ; DR O59028, MDH_PYRHO ; O33525, MDH_RHILV ; Q9EYJ6, MDH_RHIME ; DR P80458, MDH_RHOPA ; P80459, MDH_RHORU ; Q92IA0, MDH_RICCN ; DR Q9ZDF3, MDH_RICPR ; P25077, MDH_SALTY ; P82177, MDH_SHEON ; DR P19982, MDH_STRAR ; Q9K3J3, MDH_STRCO ; P19983, MDH_STRRS ; DR P11386, MDH_SULAC ; Q97VN4, MDH_SULSO ; P58407, MDH_SULTO ; DR P80460, MDH_SYNY4 ; Q9HJL5, MDH_THEAC ; P33163, MDH_THEAL ; DR P10584, MDH_THETH ; Q9KUT3, MDH_VIBCH ; P48364, MDH_VIBS5 ; DR P80541, MDH_XANMA ; // ID 1.1.1.38 DE Malate dehydrogenase (oxaloacetate decarboxylating). AN Malic enzyme. AN NAD-malic enzyme. AN Pyruvic-malic carboxylase. CA (S)-malate + NAD(+) = pyruvate + CO(2) + NADH. CC -!- Also decarboxylates added oxaloacetate. PR PROSITE; PDOC00294; DR P54572, MAO1_BACSU; P26616, MAO1_ECOLI; P45868, MAO2_BACSU; DR O34389, MAO3_BACSU; O34962, MAO4_BACSU; P27443, MAOM_ASCSU; DR P23368, MAOM_HUMAN; P16468, MAOX_BACST; P71880, MAOX_MYCTU; DR P40375, MAOX_SCHPO; P36013, MAOX_YEAST; // ID 1.1.1.39 DE Malate dehydrogenase (decarboxylating). AN Malic enzyme. AN NAD-malic enzyme. AN Pyruvic-malic carboxylase. CA (S)-malate + NAD(+) = pyruvate + CO(2) + NADH. CC -!- Does not decarboxylates added oxaloacetate. PR PROSITE; PDOC00294; DR O30807, MAO1_RHIME; P37224, MAOM_AMAHP; P37221, MAOM_SOLTU; DR P37225, MAON_SOLTU; // ID 1.1.1.40 DE Malate dehydrogenase (oxaloacetate decarboxylating) (NADP+). AN Malic enzyme. AN NADP-malic enzyme. AN Pyruvic-malic carboxylase. CA (S)-malate + NADP(+) = pyruvate + CO(2) + NADPH. CC -!- Also decarboxylates added oxaloacetate. PR PROSITE; PDOC00294; DR P76558, MAO2_ECOLI; P43837, MAO2_HAEIN; O30808, MAO2_RHIME; DR Q9ZDF6, MAO2_RICPR; Q9ZFV8, MAO2_SALTY; P36444, MAOC_FLAPR; DR P22178, MAOC_FLATR; P37222, MAOC_LYCES; P16243, MAOC_MAIZE; DR P43279, MAOC_ORYSA; Q16798, MAON_HUMAN; P28227, MAOX_ANAPL; DR Q92060, MAOX_CHICK; P40927, MAOX_COLLI; P48163, MAOX_HUMAN; DR P37223, MAOX_MESCR; P06801, MAOX_MOUSE; P12628, MAOX_PHAVU; DR Q29558, MAOX_PIG ; P34105, MAOX_POPTR; P13697, MAOX_RAT ; DR P51615, MAOX_VITVI; // ID 1.1.1.41 DE Isocitrate dehydrogenase (NAD+). AN Isocitric dehydrogenase. AN Beta-ketoglutaric-isocitric carboxylase. CA Isocitrate + NAD(+) = 2-oxoglutarate + CO(2) + NADH. CC -!- The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3- CC tricarboxylate, formerly termed threo-D(S)-isocitrate. CC -!- Does not decarboxylate added oxalosuccinate. PR PROSITE; PDOC00389; DR O13302, IDH1_AJECA; O94229, IDH1_KLULA; O13696, IDH1_SCHPO; DR P28834, IDH1_YEAST; O94230, IDH2_KLULA; Q9USP8, IDH2_SCHPO; DR P28241, IDH2_YEAST; P41563, IDHA_BOVIN; Q93714, IDHA_CAEEL; DR P54836, IDHA_CANFA; P50213, IDHA_HUMAN; Q28480, IDHA_MACFA; DR P56471, IDHA_PIG ; O77784, IDHB_BOVIN; Q93353, IDHB_CAEEL; DR O43837, IDHB_HUMAN; Q28479, IDHB_MACFA; P56472, IDHB_PIG ; DR P51553, IDHG_HUMAN; P41564, IDHG_MACFA; P70404, IDHG_MOUSE; DR P41566, IDHG_PIG ; P41565, IDHG_RAT ; // ID 1.1.1.42 DE Isocitrate dehydrogenase (NADP+). AN Oxalosuccinate decarboxylase. AN IDH. CA Isocitrate + NADP(+) = 2-oxoglutarate + CO(2) + NADPH. CC -!- The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3- CC tricarboxylate, formerly termed threo-D(S)-isocitrate. CC -!- Decarboxylates added oxalosuccinate. PR PROSITE; PDOC00389; DR O13285, IDH1_CANTR; P41560, IDH1_COLMA; O13294, IDH2_CANTR; DR P41561, IDH2_COLMA; O75874, IDHC_HUMAN; Q9Z2K9, IDHC_MICME; DR Q9Z2K8, IDHC_MICOH; O88844, IDHC_MOUSE; P20304, IDHC_PIG ; DR P41562, IDHC_RAT ; P50217, IDHC_SOLTU; Q06197, IDHC_SOYBN; DR P50218, IDHC_TOBAC; P41939, IDHC_YEAST; P53982, IDHH_YEAST; DR P79089, IDHP_ASPNG; Q04467, IDHP_BOVIN; P48735, IDHP_HUMAN; DR Q40345, IDHP_MEDSA; P54071, IDHP_MOUSE; P33198, IDHP_PIG ; DR P56574, IDHP_RAT ; O14254, IDHP_SCHPO; P21954, IDHP_YEAST; DR P50214, IDH_ANASP ; O67480, IDH_AQUAE ; O29610, IDH_ARCFU ; DR P16100, IDH_AZOVI ; P39126, IDH_BACSU ; P96318, IDH_CALNO ; DR Q8RQL9, IDH_COREF ; P50216, IDH_CORGL ; P08200, IDH_ECOLI ; DR Q9ZN36, IDH_HELPJ ; P56063, IDH_HELPY ; O53389, IDH_MYCTU ; DR Q92IR7, IDH_RICCN ; Q9ZDR0, IDH_RICPR ; P50215, IDH_SPHYA ; DR Q59940, IDH_STRMU ; Q59985, IDH_STRSL ; P80046, IDH_SYNY3 ; DR P33197, IDH_THETH ; // ID 1.1.1.43 DE 6-phosphogluconate 2-dehydrogenase. AN 6-phosphogluconic dehydrogenase. CA 6-phospho-D-gluconate + NAD(P)(+) = 6-phospho-2-dehydro-D-gluconate + CA NAD(P)H. // ID 1.1.1.44 DE Phosphogluconate dehydrogenase (decarboxylating). AN Phosphogluconic acid dehydrogenase. AN 6-phosphogluconic dehydrogenase. AN 6-phosphogluconic carboxylase. AN 6PGD. CA 6-phospho-D-gluconate + NADP(+) = D-ribulose 5-phosphate + CO(2) + CA NADPH. DI 6-phosphogluconate dehydrogenase deficiency; MIM: 172200. PR PROSITE; PDOC00390; DR P38720, 6PG1_YEAST; P80859, 6PG2_BACSU; P53319, 6PG2_YEAST; DR P37754, 6PG9_ECOLI; P70718, 6PGD_ACTAC; P52207, 6PGD_BACLI; DR P12013, 6PGD_BACSU; P57208, 6PGD_BUCAI; Q9ZHD9, 6PGD_BUCAP; DR Q89AX5, 6PGD_BUCBP; O13287, 6PGD_CANAL; P41570, 6PGD_CERCA; DR Q9PKX7, 6PGD_CHLMU; Q9Z8I3, 6PGD_CHLPN; O84066, 6PGD_CHLTR; DR P41581, 6PGD_CITAM; P41582, 6PGD_CITDI; P41583, 6PGD_CITFR; DR O60037, 6PGD_CUNEL; P41572, 6PGD_DROME; P41573, 6PGD_DROSI; DR P00350, 6PGD_ECOLI; P41574, 6PGD_ESCVU; P43774, 6PGD_HAEIN; DR P52209, 6PGD_HUMAN; P41575, 6PGD_KLEPL; P41576, 6PGD_KLEPN; DR P41577, 6PGD_KLETE; Q9CHU6, 6PGD_LACLA; P96789, 6PGD_LACLC; DR Q9DCD0, 6PGD_MOUSE; P14332, 6PGD_PIG ; P14062, 6PGD_SALTY; DR P78812, 6PGD_SCHPO; P00349, 6PGD_SHEEP; P41578, 6PGD_SHIBO; DR P41579, 6PGD_SHIDY; P37756, 6PGD_SHIFL; P41580, 6PGD_SHISO; DR P21577, 6PGD_SYNP7; P52208, 6PGD_SYNY3; O83351, 6PGD_TREPA; DR P31072, 6PGD_TRYBB; // ID 1.1.1.45 DE L-gulonate 3-dehydrogenase. AN L-3-aldonate dehydrogenase. CA L-gulonate + NAD(+) = 3-dehydro-L-gulonate + NADH. CC -!- Also oxidizes other L-3-hydroxyacids. // ID 1.1.1.46 DE L-arabinose 1-dehydrogenase. CA L-arabinose + NAD(+) = L-arabinono-1,4-lactone + NADH. // ID 1.1.1.47 DE Glucose 1-dehydrogenase. CA Beta-D-glucose + NAD(P)(+) = D-glucono-1,5-lactone + NAD(P)H. CC -!- Also oxidizes D-xylose. PR PROSITE; PDOC00060; PR PROSITE; PDOC00067; DR P39482, DHG1_BACME; P39483, DHG2_BACME; P80869, DHG2_BACSU; DR P39484, DHG3_BACME; P39485, DHG4_BACME; P10528, DHGA_BACME; DR P07999, DHGB_BACME; P40288, DHG_BACME ; P12310, DHG_BACSU ; DR P13203, DHG_THEAC ; O95479, G6PE_HUMAN; P56201, G6PE_RABIT; // ID 1.1.1.48 DE D-galactose 1-dehydrogenase. CA D-galactose + NAD(+) = D-galactono-1,4-lactone + NADH. DR P11886, GAL_PSEFL ; // ID 1.1.1.49 DE Glucose-6-phosphate 1-dehydrogenase. AN G6PD. CA D-glucose 6-phosphate + NADP(+) = D-glucono-1,5-lactone 6-phosphate + CA NADPH. CC -!- Also acts slowly on beta-D-glucose and other sugars. CC -!- Certain preparations also reduce NAD(+) as well as NADP(+). DI Hemolytic anemia due to G6PD deficiency; MIM:305900. PR PROSITE; PDOC00067; DR Q00612, G6P1_MOUSE; P97324, G6P2_MOUSE; O06573, G6P2_MYCTU; DR Q43839, G6PC_SOLTU; O24357, G6PC_SPIOL; Q43793, G6PC_TOBAC; DR P77809, G6PD_ACTAC; P48992, G6PD_ANASP; P48826, G6PD_ASPNG; DR P54547, G6PD_BACSU; O51581, G6PD_BORBU; P57405, G6PD_BUCAI; DR Q8K9M2, G6PD_BUCAP; Q27464, G6PD_CAEEL; P41571, G6PD_CERCA; DR Q9PKK8, G6PD_CHLMU; Q9Z8U6, G6PD_CHLPN; O84188, G6PD_CHLTR; DR Q23711, G6PD_CULPI; P15588, G6PD_DIDMA; P12646, G6PD_DROME; DR Q24625, G6PD_DROSI; Q27638, G6PD_DROYA; P22992, G6PD_ECOLI; DR P41764, G6PD_EMENI; P37986, G6PD_ERWCH; P54996, G6PD_FUGRU; DR P44311, G6PD_HAEIN; Q9ZKB2, G6PD_HELPJ; P56110, G6PD_HELPY; DR P11413, G6PD_HUMAN; Q25019, G6PD_HYACE; P48828, G6PD_KLULA; DR P11411, G6PD_LEUME; Q29492, G6PD_MACRO; Q42919, G6PD_MEDSA; DR O08407, G6PD_MYCTU; P48848, G6PD_NOSPU; P11410, G6PD_PICJA; DR O68282, G6PD_PSEAE; P05370, G6PD_RAT ; Q9Z3S2, G6PD_RHIME; DR Q25537, G6PD_SARBU; O00091, G6PD_SCHPO; P37830, G6PD_SOLTU; DR O54537, G6PD_STRPN; P29686, G6PD_SYNP7; P73411, G6PD_SYNY3; DR Q9X0N9, G6PD_THEMA; O83491, G6PD_TREPA; P11412, G6PD_YEAST; DR P21907, G6PD_ZYMMO; Q43727, GPD1_ARATH; Q9FY99, GPD2_ARATH; DR Q8L743, GPD3_ARATH; Q93ZW0, GPD4_ARATH; Q9LK23, GPD5_ARATH; DR Q9FJI5, GPD6_ARATH; // ID 1.1.1.50 DE 3-alpha-hydroxysteroid dehydrogenase (B-specific). AN Hydroxyprostaglandin dehydrogenase. AN 3-alpha-HSD. CA Androsterone + NAD(P)(+) = 5-alpha-androstane-3,17-dione + NAD(P)H. CC -!- Acts on other 3-alpha-hydroxysteroids and on 9-, 11- and 15- CC hydroxyprostaglandin. CC -!- B-specific with respect to NAD(+) or NADP(+) (cf. EC 1.1.1.213). PR PROSITE; PDOC00061; DR P17516, AKC4_HUMAN; P80702, DIDH_COMTE; P80701, DIDH_PSESP; DR P23457, DIDH_RAT ; // ID 1.1.1.51 DE 3(or 17)beta-hydroxysteroid dehydrogenase. CA Testosterone + NAD(P)(+) = androst-4-ene-3,17-dione + NAD(P)H. CC -!- Also acts on other 3-beta- or 17-beta-hydroxysteroids (cf. CC EC 1.1.1.209). PR PROSITE; PDOC00060; DR P19871, 3BHD_COMTE; // ID 1.1.1.52 DE 3-alpha-hydroxycholanate dehydrogenase. CA 3-alpha-hydroxy-5-beta-cholanate + NAD(+) = 3-oxo-5-beta-cholanate + CA NADH. CC -!- Also acts on other 3-alpha-hydroxysteroids with an acidic side- CC chain. // ID 1.1.1.53 DE 3-alpha(or 20-beta)-hydroxysteroid dehydrogenase. AN Cortisone reductase. AN (R)-20-hydroxysteroid dehydrogenase. CA Androstan-3-alpha,17-beta-diol + NAD(+) = 17-beta-hydroxyandrostan-3- CA one + NADH. CC -!- The 3-alpha-hydroxyl group or 20-beta-hydroxyl group of pregnane and CC androstane steroids can act as donors. PR PROSITE; PDOC00060; DR P19992, 2BHD_STREX; // ID 1.1.1.54 DE Allyl-alcohol dehydrogenase. CA Allyl-alcohol + NADP(+) = acrolein + NADPH. CC -!- Also acts on saturated primary alcohols. // ID 1.1.1.55 DE Lactaldehyde reductase (NADPH). CA Propane-1,2-diol + NADP(+) = L-lactaldehyde + NADPH. CC -!- May be identical with EC 1.1.1.2. // ID 1.1.1.56 DE Ribitol 2-dehydrogenase. CA Ribitol + NAD(+) = D-ribulose + NADH. PR PROSITE; PDOC00060; DR P00335, RIDH_KLEAE; // ID 1.1.1.57 DE Fructuronate reductase. AN D-mannonate oxidoreductase. AN D-mannonate dehydrogenase. AN Mannonic dehydrogenase. CA D-mannonate + NAD(+) = D-fructuronate + NADH. CC -!- Also reduces D-tagaturonate. PR PROSITE; PDOC00751; DR P39160, UXUB_ECOLI; // ID 1.1.1.58 DE Tagaturonate reductase. AN Tagaturonate dehydrogenase. AN Altronate oxidoreductase. AN Altronate dehydrogenase. AN Altronic oxidoreductase. CA D-altronate + NAD(+) = D-tagaturonate + NADH. DR P24214, UXAB_ECOLI; // ID 1.1.1.59 DE 3-hydroxypropionate dehydrogenase. CA 3-hydroxypropanoate + NAD(+) = 3-oxopropanoate + NADH. // ID 1.1.1.60 DE 2-hydroxy-3-oxopropionate reductase. AN Tartronate semialdehyde reductase. CA (R)-glycerate + NAD(P)(+) = 2-hydroxy-3-oxopropanoate + NAD(P)H. DR P23523, GARR_ECOLI; P77161, GLXR_ECOLI; // ID 1.1.1.61 DE 4-hydroxybutyrate dehydrogenase. CA 4-hydroxybutanoate + NAD(+) = succinate semialdehyde + NADH. PR PROSITE; PDOC00059; DR P38945, 4HDB_CLOKL; // ID 1.1.1.62 DE Estradiol 17 beta-dehydrogenase. AN 17-beta-hydroxysteroid dehydrogenase. AN 17-beta-HSD. AN Estrogen 17-oxidoreductase. CA Estradiol-17-beta + NAD(P)(+) = estrone + NAD(P)H. CC -!- Also acts on (S)-20-hydroxypregn-4-en-3-one and related compounds, CC oxidizing the (S)-20-group. CC -!- B-specific with respect to NAD(P)(+). DI Male pseudohermaphroditism; MIM:264300. PR PROSITE; PDOC00060; DR P14061, DHB1_HUMAN; P51656, DHB1_MOUSE; P51657, DHB1_RAT ; DR P37059, DHB2_HUMAN; P51658, DHB2_MOUSE; Q62730, DHB2_RAT ; DR P37058, DHB3_HUMAN; P70385, DHB3_MOUSE; O54939, DHB3_RAT ; DR P51659, DHB4_HUMAN; P51660, DHB4_MOUSE; P97852, DHB4_RAT ; DR P56937, DHB7_HUMAN; O88736, DHB7_MOUSE; Q62904, DHB7_RAT ; DR Q9GME3, DHB8_CALJA; Q92506, DHB8_HUMAN; P50171, DHB8_MOUSE; // ID 1.1.1.63 DE Testosterone 17-beta-dehydrogenase. AN 17-ketoreductase. CA Testosterone + NAD(+) = androst-4-ene-3,17-dione + NADH. // ID 1.1.1.64 DE Testosterone 17-beta-dehydrogenase (NADP+). AN 17-ketoreductase. CA Testosterone + NADP(+) = androst-4-ene-3,17-dione + NADPH. CC -!- Also oxidizes 3-hydroxyhexobarbital to 3-oxohexobarbital. // ID 1.1.1.65 DE Pyridoxine 4-dehydrogenase. AN Pyridoxine dehydrogenase. AN Pyridoxin dehydrogenase. AN Pyridoxal reductase. AN PL reductase. CA Pyridoxine + NADP(+) = pyridoxal + NADPH. CC -!- Also oxidizes pyridoxine phosphate. DR O14295, PLR_SCHPO ; // ID 1.1.1.66 DE Omega-hydroxydecanoate dehydrogenase. CA 10-hydroxydecanoate + NAD(+) = 10-oxodecanoate + NADH. CC -!- Also acts, more slowly, on 9-hydroxynonanoate and CC 11-hydroxyundecanoate. // ID 1.1.1.67 DE Mannitol 2-dehydrogenase. AN Mannitol dehydrogenase. CA D-mannitol + NAD(+) = D-fructose + NADH. PR PROSITE; PDOC00751; DR P33216, MTLK_RHOSH; // ID 1.1.1.68 DE Transferred entry: 1.7.99.5. // ID 1.1.1.69 DE Gluconate 5-dehydrogenase. AN 5-keto-D-gluconate 5-reductase. AN 5-ketogluconate 5-reductase. AN 5-ketogluconate reductase. CA D-gluconate + NAD(P)(+) = 5-dehydro-D-gluconate + NAD(P)H. PR PROSITE; PDOC00060; DR P50199, GNO_GLUOX ; P39345, IDNO_ECOLI; // ID 1.1.1.70 DE Transferred entry: 1.2.1.3. // ID 1.1.1.71 DE Alcohol dehydrogenase (NAD(P)+). AN Retinal reductase. CA An alcohol + NAD(P)(+) = an aldehyde + NAD(P)H. CC -!- Reduces aliphatic aldehydes of chain length from C(2) to C(14), CC with greatest activity on C(4), C(6) and C(8) aldehydes. CC -!- Also reduces retinal to retinol. // ID 1.1.1.72 DE Glycerol dehydrogenase (NADP+). CA Glycerol + NADP(+) = D-glyceraldehyde + NADPH. PR PROSITE; PDOC00061; DR P55804, DHGP_ASPNG; // ID 1.1.1.73 DE Octanol dehydrogenase. CA 1-octanol + NAD(+) = 1-octanal + NADH. CC -!- Acts, less rapidly, on other long-chain alcohols. PR PROSITE; PDOC00058; DR P46415, ADHX_DROME; // ID 1.1.1.74 DE Deleted entry. // ID 1.1.1.75 DE (R)-aminopropanol dehydrogenase. CA (R)-1-aminopropan-2-ol + NAD(+) = aminoacetone + NADH. CF Potassium. // ID 1.1.1.76 DE (S,S)-butanediol dehydrogenase. CA (S,S)-butane-2,3-diol + NAD(+) = acetoin + NADH. // ID 1.1.1.77 DE Lactaldehyde reductase. AN Propanediol oxidoreductase. CA (R) [or (S)]-propane-1,2-diol + NAD(+) = (R) [or (S)]-lactaldehyde + CA NADH. PR PROSITE; PDOC00059; DR P11549, FUCO_ECOLI; // ID 1.1.1.78 DE D-lactaldehyde dehydrogenase. AN Methylglyoxal reductase. CA (R)-lactaldehyde + NAD(+) = methylglyoxal + NADH. // ID 1.1.1.79 DE Glyoxylate reductase (NADP+). CA Glycolate + NADP(+) = glyoxylate + NADPH. CC -!- Also reduces hydroxypyruvate to glycerate. CC -!- Has some affinity for NAD(+). // ID 1.1.1.80 DE Isopropanol dehydrogenase (NADP+). CA Propan-2-ol + NADP(+) = acetone + NADPH. CC -!- Also acts on other short-chain secondary alcohols, and, slowly, CC on primary alcohols. // ID 1.1.1.81 DE Hydroxypyruvate reductase. AN D-glycerate dehydrogenase. CA D-glycerate + NAD(P)(+) = hydroxypyruvate + NAD(P)H. DR P70788, TUD3_AGRVI; Q44472, TUD4_AGRVI; // ID 1.1.1.82 DE Malate dehydrogenase (NADP+). AN NADP-linked malate dehydrogenase. CA (S)-malate + NADP(+) = oxaloacetate + NADPH. CC -!- Activated by light. PR PROSITE; PDOC00066; DR P46489, MDHP_FLABI; P15719, MDHP_MAIZE; O48902, MDHP_MEDSA; DR Q05145, MDHP_MESCR; P21528, MDHP_PEA ; P17606, MDHP_SORBI; DR P52426, MDHP_SPIOL; P37229, MDHQ_SORBI; P16142, MDH_METFE ; DR Q60176, MDH_METJA ; // ID 1.1.1.83 DE D-malate dehydrogenase (decarboxylating). CA (R)-malate + NAD(+) = pyruvate + CO(2) + NADH. // ID 1.1.1.84 DE Dimethylmalate dehydrogenase. CA (R)-3,3-dimethylmalate + NAD(+) = 3-methyl-2-oxo-butanoate + CO(2) + CA NADH. CF Potassium or Ammonia; Manganese or Cobalt. CC -!- Also acts on (R)-malate. // ID 1.1.1.85 DE 3-isopropylmalate dehydrogenase. AN Beta-isopropylmalate dehydrogenase. AN Beta-IPM dehydrogenase. AN IMDH. CA 3-carboxy-2-hydroxy-4-methylpentanoate + NAD(+) = 3-carboxy-4-methyl-2- CA oxopentanoate + NADH. CC -!- The product decarboxylates to 4-methyl-2-oxopentanoate. PR PROSITE; PDOC00389; DR Q9SA14, LE31_ARATH; P93832, LE32_ARATH; Q9FMT1, LE33_ARATH; DR P87256, LE3A_ASPNG; P87257, LE3B_ASPNG; P24404, LEU3_AGRT5; DR Q8YXA2, LEU3_ANASP; O66607, LEU3_AQUAE; O29627, LEU3_ARCFU; DR O60027, LEU3_ASHGO; P96197, LEU3_AZOVI; P05644, LEU3_BACCA; DR P12010, LEU3_BACCO; P54354, LEU3_BACFR; Q9K8E9, LEU3_BACHD; DR P41019, LEU3_BACME; P05645, LEU3_BACSU; P29102, LEU3_BRANA; DR Q8YCX4, LEU3_BRUME; P56933, LEU3_BUCAI; O85064, LEU3_BUCAP; DR P59515, LEU3_BUCBP; O85071, LEU3_BUCDN; Q9EVG3, LEU3_BUCML; DR P59027, LEU3_BUCPS; P48572, LEU3_BUCRP; O31292, LEU3_BUCTS; DR Q9EVG6, LEU3_BUCUA; Q9EVE1, LEU3_BUCUD; Q9EVH5, LEU3_BUCUE; DR Q9EVH8, LEU3_BUCUH; Q9AQC8, LEU3_BUCUL; Q9EVG9, LEU3_BUCUM; DR Q9EVI7, LEU3_BUCUN; Q9EVI1, LEU3_BUCUO; Q9EVI4, LEU3_BUCUS; DR Q9PLW0, LEU3_CAMJE; P87186, LEU3_CANAL; Q01987, LEU3_CANBO; DR O14429, LEU3_CANGA; P07139, LEU3_CANMA; Q9ABN3, LEU3_CAUCR; DR Q12545, LEU3_CEPAC; P59028, LEU3_CHLTE; Q97EE2, LEU3_CLOAB; DR P31958, LEU3_CLOPA; P94631, LEU3_CORGL; Q9RTH9, LEU3_DEIRA; DR Q8X9Z9, LEU3_ECO57; P30125, LEU3_ECOLI; P43860, LEU3_HAEIN; DR P23390, LEU3_KLULA; P41766, LEU3_KLUMA; Q02143, LEU3_LACLA; DR P24015, LEU3_LEPIN; Q92A27, LEU3_LISIN; Q8Y5R8, LEU3_LISMO; DR Q58130, LEU3_METJA; O27441, LEU3_METTH; P94929, LEU3_MYCBO; DR Q9Y897, LEU3_MYCGR; O33117, LEU3_MYCLE; P95313, LEU3_MYCTU; DR P50180, LEU3_NEILA; Q9JU79, LEU3_NEIMA; Q9JZI9, LEU3_NEIMB; DR P34738, LEU3_NEUCR; Q9CJN6, LEU3_PASMU; O59930, LEU3_PHACH; DR P34733, LEU3_PICAN; P08791, LEU3_PICJA; O94114, LEU3_PICST; DR Q51375, LEU3_PSEAE; Q8XXX5, LEU3_RALSO; Q98E57, LEU3_RHILO; DR Q92KY8, LEU3_RHIME; Q8Z9I1, LEU3_SALTI; P37412, LEU3_SALTY; DR P18869, LEU3_SCHPO; P29696, LEU3_SOLTU; Q00412, LEU3_SPIPL; DR Q99SJ4, LEU3_STAAM; Q8NVJ0, LEU3_STAAW; O86504, LEU3_STRCO; DR Q9UXB2, LEU3_SULSO; P50455, LEU3_SULTO; P59029, LEU3_SYNEL; DR P73960, LEU3_SYNY3; P24098, LEU3_THEAQ; Q9WZ26, LEU3_THEMA; DR P00351, LEU3_THETH; Q8RDK0, LEU3_THETN; Q56268, LEU3_THIFE; DR Q9KP82, LEU3_VIBCH; Q8PH05, LEU3_XANAC; Q8P5L1, LEU3_XANCP; DR Q9PAX3, LEU3_XYLFA; Q87BQ1, LEU3_XYLFT; P41926, LEU3_YAMOH; DR P18120, LEU3_YARLI; P04173, LEU3_YEAST; Q8ZIG9, LEU3_YERPE; // ID 1.1.1.86 DE Ketol-acid reductoisomerase. AN Dihydroxyisovalerate dehydrogenase (isomerizing). AN Acetohydroxy acid isomeroreductase. AN Alpha-keto-beta-hydroxylacil reductoisomerase. CA (R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (S)-2-hydroxy-2-methyl- CA 3-oxobutanoate + NADPH. CC -!- Also: (R)-2,3-dihydroxyacid-3-methylvalerate + NADP(+) = 2-aceto-2- CC hydroxybutyrate + NADPH. CC -!- Formerly EC 1.1.1.89. DR Q9Z565, ILC1_STRCO; Q9UWX9, ILC1_SULSO; Q9FBT8, ILC2_STRCO; DR Q97YJ9, ILC2_SULSO; Q97X13, ILC3_SULSO; Q05758, ILV5_ARATH; DR P38674, ILV5_NEUCR; O82043, ILV5_PEA ; P78827, ILV5_SCHPO; DR Q01292, ILV5_SPIOL; P06168, ILV5_YEAST; Q8UDV0, ILVC_AGRT5; DR Q8YUM5, ILVC_ANASP; O67289, ILVC_AQUAE; O28294, ILVC_ARCFU; DR Q9K8E7, ILVC_BACHD; P37253, ILVC_BACSU; Q89G50, ILVC_BRAJA; DR Q8YI21, ILVC_BRUME; Q8FZU1, ILVC_BRUSU; P57655, ILVC_BUCAI; DR O51888, ILVC_BUCAP; Q9RQ55, ILVC_BUCDN; Q9RQ47, ILVC_BUCMH; DR Q9AQ96, ILVC_BUCML; Q9RQ51, ILVC_BUCSC; Q9AQ97, ILVC_BUCUE; DR Q9AQ98, ILVC_BUCUL; Q9AQA0, ILVC_BUCUM; Q9AQ99, ILVC_BUCUN; DR Q9PHN5, ILVC_CAMJE; Q9A6H4, ILVC_CAUCR; Q8KER7, ILVC_CHLTE; DR Q8FPX1, ILVC_COREF; Q57179, ILVC_CORGL; Q9RU74, ILVC_DEIRA; DR P58256, ILVC_ECO57; Q8FBR2, ILVC_ECOL6; P05793, ILVC_ECOLI; DR P44822, ILVC_HAEIN; Q9ZMA9, ILVC_HELPJ; O25097, ILVC_HELPY; DR Q02138, ILVC_LACLA; P97115, ILVC_LEUMC; Q92A29, ILVC_LISIN; DR Q8Y5S0, ILVC_LISMO; Q8TJJ4, ILVC_METAC; Q58938, ILVC_METJA; DR Q8TX44, ILVC_METKA; Q8PZ26, ILVC_METMA; O27491, ILVC_METTH; DR Q59500, ILVC_MYCAV; O33114, ILVC_MYCLE; O53248, ILVC_MYCTU; DR Q9JTI3, ILVC_NEIMA; Q9JYI2, ILVC_NEIMB; Q8EN66, ILVC_OCEIH; DR Q9CLF1, ILVC_PASMU; Q9HVA2, ILVC_PSEAE; Q88DZ0, ILVC_PSEPK; DR Q888N4, ILVC_PSESM; Q9UZ09, ILVC_PYRAB; Q8ZTE1, ILVC_PYRAE; DR Q8U2A3, ILVC_PYRFU; Q98KM7, ILVC_RHILO; Q52955, ILVC_RHIME; DR O32414, ILVC_RHOMO; Q8Z381, ILVC_SALTI; P05989, ILVC_SALTY; DR Q99SJ6, ILVC_STAAM; Q8CRQ6, ILVC_STAEP; Q59818, ILVC_STRAW; DR Q9F0I7, ILVC_STRTR; Q8DGR0, ILVC_SYNEL; P29107, ILVC_SYNY3; DR Q9WZ20, ILVC_THEMA; Q8RDK4, ILVC_THETN; Q9KVI4, ILVC_VIBCH; DR Q87TN4, ILVC_VIBPA; Q8DDC8, ILVC_VIBVU; Q8PH09, ILVC_XANAC; DR Q8P5L5, ILVC_XANCP; Q9PCF9, ILVC_XYLFA; Q87CM2, ILVC_XYLFT; DR Q8ZAC2, ILVC_YERPE; Q9X5F8, ILVC_ZYMMO; // ID 1.1.1.87 DE 3-carboxy-2-hydroxyadipate dehydrogenase. CA 3-carboxy-2-hydroxyadipate + NAD(+) = 2-oxoadipate + CO(2) + NADH. // ID 1.1.1.88 DE Hydroxymethylglutaryl-CoA reductase. AN 3-hydroxy-3-methylglutaryl-coenzyme A reductase. AN HMG-CoA reductase. AN Beta-hydroxy-beta-methylglutaryl coenzyme A reductase. AN Beta-hydroxy-beta-methylglutaryl CoA-reductase. AN Hydroxymethylglutaryl coenzyme A reductase. CA (R)-mevalonate + CoA + 2 NAD(+) = 3-hydroxy-3-methylglutaryl-CoA + CA 2 NADH. PR PROSITE; PDOC00064; DR O51628, HMDH_BORBU; P13702, MVAA_PSEMV; // ID 1.1.1.89 DE Transferred entry: 1.1.1.86. // ID 1.1.1.90 DE Aryl-alcohol dehydrogenase. AN p-hydroxybenzyl alcohol dehydrogenase. AN Benzyl alcohol dehydrogenase. CA An aromatic alcohol + NAD(+) = an aromatic aldehyde + NADH. CC -!- A group of enzymes with broad specificity towards primary alcohols CC with an aromatic or cyclohex-1-ene ring, but with low or no activity CC towards short-chain aliphatic alcohols. PR PROSITE; PDOC00058; DR P46364, XYLB_ACIGB; P39849, XYLB_PSEPU; // ID 1.1.1.91 DE Aryl-alcohol dehydrogenase (NADP+). CA An aromatic alcohol + NADP(+) = an aromatic aldehyde + NADPH. CC -!- Also acts on some aliphatic aldehydes but cinnamaldehyde was the CC best substrate found. DR Q01752, AAD_PHACH ; // ID 1.1.1.92 DE Oxaloglycolate reductase (decarboxylating). CA D-glycerate + NAD(P)(+) + CO(2) = 2-hydroxy-3-oxosuccinate + NAD(P)H. CC -!- Also reduces hydroxypyruvate to D-glycerate and glyoxylate to CC glycolate. // ID 1.1.1.93 DE Tartrate dehydrogenase. AN Mesotartrate dehydrogenase. CA Tartrate + NAD(+) = oxaloglycolate + NADH. CF Manganese; Monovalent cation. CC -!- Meso-tartrate and (R,R)-tartrate act as substrates. DR Q44471, TTC1_AGRVI; P70787, TTC2_AGRVI; O34296, TTC3_AGRVI; DR P70792, TTC4_AGRVI; O34295, TTC5_AGRVI; P76251, TTUC_ECOLI; DR Q51945, TTUC_PSEPU; // ID 1.1.1.94 DE Glycerol-3-phosphate dehydrogenase (NAD(P)+). AN NAD(P)H-dependent dihydroxyacetone-phosphate reductase. CA Sn-glycerol 3-phosphate + NAD(P)(+) = glycerone phosphate + NAD(P)H. PR PROSITE; PDOC00740; DR O53761, GPD2_MYCTU; Q8UC48, GPDA_AGRT5; Q8YWC2, GPDA_ANASP; DR O67555, GPDA_AQUAE; O29390, GPDA_ARCFU; Q9KCD2, GPDA_BACHD; DR P46919, GPDA_BACSU; Q8YJB2, GPDA_BRUME; Q9PN99, GPDA_CAMJE; DR P58141, GPDA_CAUCR; Q9PLL2, GPDA_CHLMU; Q9Z751, GPDA_CHLPN; DR Q8KG76, GPDA_CHLTE; O84719, GPDA_CHLTR; Q97ID6, GPDA_CLOAB; DR Q8XJK2, GPDA_CLOPE; Q8NQV3, GPDA_CORGL; Q93FR9, GPDA_COWRU; DR Q9RR76, GPDA_DEIRA; P37606, GPDA_ECOLI; Q8RF18, GPDA_FUSNN; DR P43798, GPDA_HAEIN; Q9ZKP0, GPDA_HELPJ; O25614, GPDA_HELPY; DR Q93FD0, GPDA_LACDE; Q9CFX6, GPDA_LACLA; Q92A72, GPDA_LISIN; DR Q8Y5W9, GPDA_LISMO; O26468, GPDA_METTH; Q9CBR9, GPDA_MYCLE; DR P95113, GPDA_MYCTU; Q9JWH0, GPDA_NEIMA; Q9JXG6, GPDA_NEIMB; DR Q9CL17, GPDA_PASMU; Q9I3A8, GPDA_PSEAE; Q59680, GPDA_PSELE; DR Q8Y2H9, GPDA_RALSO; P58142, GPDA_RHILO; Q9R9L6, GPDA_RHIME; DR Q9ZDA0, GPDA_RICPR; P40716, GPDA_SALTY; Q8KRM1, GPDA_SERMA; DR Q99U16, GPDA_STAAM; Q8NWM9, GPDA_STAAW; Q9ZBS0, GPDA_STRCO; DR Q97NF1, GPDA_STRPN; P58143, GPDA_STRPY; Q935Z2, GPDA_SYNP7; DR P73033, GPDA_SYNY3; Q8R9J3, GPDA_THETN; O83973, GPDA_TREPA; DR Q9KNT0, GPDA_VIBCH; Q87KZ2, GPDA_VIBPA; Q8DCW4, GPDA_VIBVU; DR Q8D216, GPDA_WIGBR; Q8PQU9, GPDA_XANAC; Q8PDY0, GPDA_XANCP; DR Q9PCH7, GPDA_XYLFA; Q87CK3, GPDA_XYLFT; Q8ZJM6, GPDA_YERPE; // ID 1.1.1.95 DE Phosphoglycerate dehydrogenase. AN D-3-phosphoglycerate dehydrogenase. AN PGDH. CA 3-phosphoglycerate + NAD(+) = 3-phosphohydroxypyruvate + NADH. DI 3-phosphoglycerate dehydrogenase deficiency; MIM:601815. PR PROSITE; PDOC00063; DR P40510, SE33_YEAST; O04130, SERA_ARATH; O29445, SERA_ARCFU; DR P35136, SERA_BACSU; P08328, SERA_ECOLI; P43885, SERA_HAEIN; DR O43175, SERA_HUMAN; Q58424, SERA_METJA; O27051, SERA_METTH; DR Q61753, SERA_MOUSE; O33116, SERA_MYCLE; O53243, SERA_MYCTU; DR O08651, SERA_RAT ; P87228, SERA_SCHPO; P73821, SERA_SYNY3; DR P40054, SERA_YEAST; // ID 1.1.1.96 DE Diiodophenylpyruvate reductase. CA Beta-(3,5-diiodo-4-hydroxyphenyl)lactate + NAD(+) = CA beta-(3,5-diiodo-4-hydroxyphenyl)pyruvate + NADH. CC -!- Substrates contain an aromatic ring with a pyruvate side chain. CC -!- The most active substrates are halogenated derivatives. CC -!- Compounds with hydroxyl or amino groups in the 3 or 5 position are CC inactive. // ID 1.1.1.97 DE 3-hydroxybenzyl-alcohol dehydrogenase. AN m-hydroxybenzyl alcohol dehydrogenase. CA 3-hydroxybenzyl alcohol + NADP(+) = 3-hydroxybenzaldehyde + NADPH. // ID 1.1.1.98 DE (R)-2-hydroxy-fatty-acid dehydrogenase. AN D-2-hydroxy fatty acid dehydrogenase. CA (R)-2-hydroxystearate + NAD(+) = 2-oxostearate + NADH. // ID 1.1.1.99 DE (S)-2-hydroxy-fatty-acid dehydrogenase. AN L-2-hydroxy fatty acid dehydrogenase. CA (S)-2-hydroxystearate + NAD(+) = 2-oxostearate + NADH. // ID 1.1.1.100 DE 3-oxoacyl-[acyl-carrier protein] reductase. CA (3R)-3-hydroxyacyl-[acyl-carrier protein] + NADP(+) = 3-oxoacyl- CA [acyl-carrier protein] + NADPH. CC -!- Exhibits a marked preference for acyl-carrier protein derivatives CC over CoA derivatives as substrates. PR PROSITE; PDOC00060; DR P70720, FABG_ACTAC; O67610, FABG_AQUAE; P33207, FABG_ARATH; DR P51831, FABG_BACSU; P27582, FABG_BRANA; P57432, FABG_BUCAI; DR Q8K9J5, FABG_BUCAP; Q89AG9, FABG_BUCBP; Q9PKF7, FABG_CHLMU; DR Q9Z8P2, FABG_CHLPN; P38004, FABG_CHLTR; P28643, FABG_CUPLA; DR P25716, FABG_ECOLI; P43713, FABG_HAEIN; O07399, FABG_MYCAV; DR P71534, FABG_MYCSM; Q48930, FABG_MYCTU; P27583, FABG_PERAE; DR O54438, FABG_PSEAE; P50941, FABG_RICPR; O85141, FABG_SALTY; DR Q9X248, FABG_THEMA; Q9KQH7, FABG_VIBCH; P55336, FABG_VIBHA; DR P73574, FAG1_SYNY3; P73826, FAG2_SYNY3; P43098, FAS2_CANAL; DR P15368, FAS2_PENPA; Q10289, FAS2_SCHPO; P19097, FAS2_YEAST; DR P12276, FAS_CHICK ; P49327, FAS_HUMAN ; P19096, FAS_MOUSE ; DR P12785, FAS_RAT ; Q9RPT1, RHLG_PSEAE; // ID 1.1.1.101 DE Acylglycerone-phosphate reductase. AN Palmitoyldihydroxyacetone-phosphate reductase. CA 1-palmitoylglycerol 3-phosphate + NADP(+) = palmitoylglycerone phosphate CA + NADPH. CC -!- Also acts on alkylglycerone-3-phosphate and alkylglycerol CC 3-phosphate. // ID 1.1.1.102 DE 3-dehydrosphinganine reductase. CA Sphinganine + NADP(+) = 3-dehydrosphinganine + NADPH. // ID 1.1.1.103 DE L-threonine 3-dehydrogenase. CA L-threonine + NAD(+) = L-2-amino-3-oxobutanoate + NADH. CC -!- The product spontaneously decarboxylates to aminoacetone. PR PROSITE; PDOC00058; DR O31776, TDH_BACSU ; Q9RTU4, TDH_DEIRA ; Q8XEJ1, TDH_ECO57 ; DR Q8FCA2, TDH_ECOL6 ; P07913, TDH_ECOLI ; Q9UYX0, TDH_PYRAB ; DR Q8U259, TDH_PYRFU ; O58389, TDH_PYRHO ; Q983J7, TDH_RHILO ; DR Q52998, TDH_RHIME ; Q8Z2F4, TDH_SALTI ; Q8ZL52, TDH_SALTY ; DR Q8E8J1, TDH_SHEON ; P59409, TDH_SHIFL ; Q9L233, TDH_STRCO ; DR Q8R7K0, TDH_THETN ; Q9KL62, TDH_VIBCH ; P59410, TDH_VIBPA ; DR Q8D442, TDH_VIBVU ; Q8PNN2, TDH_XANAC ; O34268, TDH_XANCP ; DR Q8ZJN2, TDH_YERPE ; // ID 1.1.1.104 DE 4-oxoproline reductase. AN Hydroxyproline oxidase. CA 4-hydroxy-L-proline + NAD(+) = 4-oxoproline + NADH. DI Hydroxyprolinemia; MIM:237000. // ID 1.1.1.105 DE Retinol dehydrogenase. CA Retinol + NAD(+) = retinal + NADH. PR PROSITE; PDOC00060; DR Q27979, RDH1_BOVIN; Q92781, RDH1_HUMAN; P50169, ROH1_RAT ; DR P50170, ROH2_RAT ; P55006, ROH3_RAT ; // ID 1.1.1.106 DE Pantoate 4-dehydrogenase. AN Panthothenase. CA (R)-pantoate + NAD(+) = (R)-4-dehydropantoate + NADH. // ID 1.1.1.107 DE Pyridoxal 4-dehydrogenase. CA Pyridoxal + NAD(+) = 4-pyridoxolactone + NADH. CC -!- The enzyme acts on the hemiacetal form of the substrate. // ID 1.1.1.108 DE Carnitine 3-dehydrogenase. CA Carnitine + NAD(+) = 3-dehydrocarnitine + NADH. // ID 1.1.1.109 DE Transferred entry: 1.3.1.28. // ID 1.1.1.110 DE Indole-3-lactate dehydrogenase. AN Indolelactate dehydrogenase. CA Indole-3-lactate + NAD(+) = indole-3-pyruvate + NADH. // ID 1.1.1.111 DE 3-(imidazol-5-yl)lactate dehydrogenase. CA (S)-3-(imidazol-5-yl)lactate + NAD(P)(+) = 3-(imidazol-5-yl)pyruvate + CA NAD(P)H. // ID 1.1.1.112 DE Indanol dehydrogenase. CA Indan-1-ol + NAD(P)(+) = indanone + NAD(P)H. CC -!- 3(20) alpha-hydroxysteroids are also oxidized, more slowly. // ID 1.1.1.113 DE L-xylose 1-dehydrogenase. CA L-xylose + NADP(+) = L-xylono-1,4-lactone + NADPH. CC -!- Also oxidizes D-arabinose and D-lyxose. // ID 1.1.1.114 DE Apiose 1-reductase. AN D-apiose reductase. AN D-apiitol reductase. CA D-apiitol + NAD(+) = D-apiose + NADH. // ID 1.1.1.115 DE Ribose 1-dehydrogenase (NADP+). AN NADP-pentose-dehydrogenase. CA D-ribose + NADP(+) + H(2)O = D-ribonate + NADPH. CC -!- Also acts, more slowly, on D-xylose and other pentoses. // ID 1.1.1.116 DE D-arabinose 1-dehydrogenase. CA D-arabinose + NAD(+) = D-arabinono-1,4-lactone + NADH. // ID 1.1.1.117 DE D-arabinose 1-dehydrogenase (NAD(P)+). CA D-arabinose + NAD(P)(+) = D-arabinono-1,4-lactone + NAD(P)H. CC -!- Also acts on L-galactose, 6-deoxy- and 3,6-dideoxy-L-galactose. DR P38115, ARA1_YEAST; // ID 1.1.1.118 DE Glucose 1-dehydrogenase (NAD+). CA D-glucose + NAD(+) = D-glucono-1,5-lactone + NADH. // ID 1.1.1.119 DE Glucose 1-dehydrogenase (NADP+). CA D-glucose + NADP(+) = D-glucono-1,4-lactone + NADPH. CC -!- Also oxidizes D-mannose, 2-deoxy-D-glucose and 2-amino-2-deoxy-D- CC mannose. // ID 1.1.1.120 DE Galactose 1-dehydrogenase (NADP+). CA D-galactose + NADP(+) = D-galactonolactone + NADPH. CC -!- Also acts on L-arabinose, 6-deoxy- and 2-deoxy-D-galactose. // ID 1.1.1.121 DE Aldose 1-dehydrogenase. CA D-aldose + NAD(+) = D-aldonolactone + NADH. CC -!- Also acts on D-glucose, 2-deoxy- and 6-deoxy-D-glucose, D-galactose, CC 6-deoxy-D-galactose, 2-deoxy-L-arabinose and D-xylose. // ID 1.1.1.122 DE D-threo-aldose 1-dehydrogenase. AN L-fucose dehydrogenase. AN (2S,3R)-aldose dehydrogenase. CA A D-threo-aldose + NAD(+) = a D-threo-aldono-1,5-lactone + NADH. CC -!- Acts on L-fucose, D-arabinose and L-xylose. CC -!- The animal enzyme was also shown to act on L-arabinose, and the CC enzyme from Pseudomonas caryophylli on L-glucose. // ID 1.1.1.123 DE Sorbose 5-dehydrogenase (NADP+). AN 5-ketofructose reductase. CA L-sorbose + NADP(+) = 5-dehydro-D-fructose + NADPH. // ID 1.1.1.124 DE Fructose 5-dehydrogenase (NADP+). AN 5-ketofructose reductase (NADP+). CA D-fructose + NADP(+) = 5-dehydro-D-fructose + NADPH. DR P19574, DHF5_ERWCI; // ID 1.1.1.125 DE 2-deoxy-D-gluconate 3-dehydrogenase. AN 2-keto-3-deoxygluconate oxidoreductase. CA 2-deoxy-D-gluconate + NAD(+) = 3-dehydro-2-deoxy-D-gluconate + NADH. PR PROSITE; PDOC00060; DR P50842, KDUD_BACSU; P37769, KDUD_ECOLI; Q05528, KDUD_ERWCH; // ID 1.1.1.126 DE 2-dehydro-3-deoxy-D-gluconate 6-dehydrogenase. AN 2-keto-3-deoxy-D-gluconate dehydrogenase. CA 2-dehydro-3-deoxy-D-gluconate + NADP(+) = (4S,5S)-4,5-dehydroxy-2,6- CA dioxohexanoate + NADPH. // ID 1.1.1.127 DE 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase. AN 2-keto-3-deoxygluconate dehydrogenase. CA 2-dehydro-3-deoxy-D-gluconate + NAD(+) = (4S)-4,6-dihydroxy-2,5- CA dioxohexanoate + NADH. CC -!- The enzyme from Pseudomonas acts equally well on NAD(+) or NADP(+), CC while those from Erwinia chrysanthemi and E.coli are more specific CC for NAD(+). // ID 1.1.1.128 DE L-idonate 2-dehydrogenase. AN 5-ketogluconate 2-reductase. CA L-idonate + NADP(+) = 5-dehydro-D-gluconate + NADPH. // ID 1.1.1.129 DE L-threonate 3-dehydrogenase. AN L-threonic acid dehydrogenase. CA L-threonate + NAD(+) = 3-dehydro-L-threonate + NADH. // ID 1.1.1.130 DE 3-dehydro-L-gulonate 2-dehydrogenase. AN 3-keto-L-gulonate dehydrogenase. CA 3-dehydro-L-gulonate + NAD(P)(+) = (4R,5S)-4,5,6-trihydroxy-2,3- CA dioxohexanoate + NAD(P)H. // ID 1.1.1.131 DE Mannuronate reductase. AN Mannonate dehydrogenase. CA D-mannonate + NAD(P)(+) = D-mannuronate + NAD(P)H. CC -!- Formerly EC 1.1.1.180 and EC 1.2.1.34. // ID 1.1.1.132 DE GDP-mannose 6-dehydrogenase. CA GDP-mannose + 2 NAD(+) + H(2)O = GDP-D-mannuronate + 2 NADH. CC -!- Also uses the corresponding deoxynucleoside diphosphate derivative CC as a substrate. DR P51585, ALGD_AZOVI; P11759, ALGD_PSEAE; O07299, ALGD_PSESH; // ID 1.1.1.133 DE dTDP-4-dehydrorhamnose reductase. AN dTDP-4-keto-L-rhamnose reductase. AN dTDP-6-deoxy-L-mannose dehydrogenase. CA dTDP-6-deoxy-L-mannose + NADP(+) = dTDP-4-dehydro-6-deoxy-L-mannose + CA NADPH. CC -!- In the reverse direction reduction on the 4-position of the hexose CC moiety takes place only while the substrate is bound to another CC enzyme which catalyzes epimerization at C-3-and C-5; the complex CC has been referred to as dTDP-L-rhamnose synthase. DR P37760, RBD1_ECOLI; Q46769, RBD2_ECOLI; P55463, RFBD_RHISN; DR P26392, RFBD_SALTY; P37778, RFBD_SHIFL; P29781, STRL_STRGR; // ID 1.1.1.134 DE dTDP-6-deoxy-L-talose 4-dehydrogenase. CA dTDP-6-deoxy-L-talose + NADP(+) = dTDP-4-dehydro-6-deoxy-L-mannose + CA NADPH. CC -!- Oxidation on the 4-position of the hexose moiety takes place only CC while the substrate is bound to another enzyme which catalyzes CC epimerization at C-3 and C-5. // ID 1.1.1.135 DE GDP-6-deoxy-D-talose 4-dehydrogenase. CA GDP-6-deoxy-D-talose + NAD(P)(+) = GDP-4-dehydro-6-deoxy-D-talose + CA NAD(P)H. // ID 1.1.1.136 DE UDP-N-acetylglucosamine 6-dehydrogenase. CA UDP-N-acetyl-D-glucosamine + 2 NAD(+) + H(2)O = UDP-N-acetyl-2-amino- CA 2-deoxy-D-glucuronate + 2 NADH. // ID 1.1.1.137 DE Ribitol-5-phosphate 2-dehydrogenase. CA D-ribitol 5-phosphate + NAD(P)(+) = D-ribulose 5-phosphate + NAD(P)H. // ID 1.1.1.138 DE Mannitol 2-dehydrogenase (NADP+). AN NADP-dependent mannitol dehydrogenase. CA D-mannitol + NADP(+) = D-fructose + NADPH. PR PROSITE; PDOC00060; DR O93868, MTDH_AGABI; O00058, MTDH_UROFA; // ID 1.1.1.139 DE Transferred entry: 1.1.1.21. // ID 1.1.1.140 DE Sorbitol-6-phosphate 2-dehydrogenase. AN Ketosephosphate reductase. AN Glucitol-6-phosphate dehydrogenase. CA D-sorbitol 6-phosphate + NAD(+) = D-fructose 6-phosphate + NADH. PR PROSITE; PDOC00060; DR P37079, SORD_KLEPN; P05707, SRLD_ECOLI; // ID 1.1.1.141 DE 15-hydroxyprostaglandin dehydrogenase (NAD+). CA (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprost-13-enoate + NAD(+) = CA (5Z,13E)-11-alpha-hydroxy-9,15-dioxoprost-13-enoate + NADH. CC -!- Acts on prostaglandins E2, F2-alpha and B1, but not on prostaglandin CC D2 (cf. EC 1.1.1.196 and EC 1.1.1.197). PR PROSITE; PDOC00060; DR P15428, PGDH_HUMAN; // ID 1.1.1.142 DE D-pinitol dehydrogenase. CA 5D-5-O-methyl-chiro-inositol + NADP(+) = 5D-5-O-methyl-2,3,5/4,6- CA pentahydroxycyclohexanone + NADPH. // ID 1.1.1.143 DE Sequoyitol dehydrogenase. CA 5-O-methyl-myo-inositol + NAD(+) = 5D-5-O-methyl-2,3,5/4,6- CA pentahydroxycyclohexanone + NADH. // ID 1.1.1.144 DE Perillyl-alcohol dehydrogenase. CA Perillyl alcohol + NAD(+) = perillyl aldehyde + NADH. CC -!- Oxidizes a number of primary alcohols with the alcohol group allylic CC to an endocyclic double bond and a 6-membered ring, either aromatic CC or hydroaromatic. // ID 1.1.1.145 DE 3-beta-hydroxy-delta(5)-steroid dehydrogenase. AN 3-beta-hydroxy-5-ene steroid dehydrogenase. AN Progesterone reductase. CA 3-beta-hydroxy-delta(5)-steroid + NAD(+) = 3-oxo-delta(5)-steroid + NADH. CC -!- Acts on 3-beta-hydroxyandrost-5-en-17-one to form androst-4-ene- CC 3,17-dione and on 3-beta-hydroxypregn-5-en-20-one to form CC progesterone. DI Hepatitis, giant cell, neonatal; MIM:231100. DR P14060, 3BH1_HUMAN; Q60555, 3BH1_MESAU; P24815, 3BH1_MOUSE; DR P22071, 3BH1_RAT ; P26439, 3BH2_HUMAN; Q64421, 3BH2_MESAU; DR P26149, 3BH2_MOUSE; P22072, 3BH2_RAT ; O35296, 3BH3_MESAU; DR P26150, 3BH3_MOUSE; P27364, 3BH3_RAT ; Q61767, 3BH4_MOUSE; DR Q62878, 3BH4_RAT ; Q61694, 3BH5_MOUSE; O35469, 3BH6_MOUSE; DR O46516, 3BHD_HORSE; P14893, 3BHS_BOVIN; Q67477, 3BHS_FOWPV; DR P27365, 3BHS_MACMU; P21097, 3BHS_VACCC; P26670, 3BHS_VACCV; DR P53199, ER26_YEAST; // ID 1.1.1.146 DE 11-beta-hydroxysteroid dehydrogenase. AN Corticosteroid 11-beta-dehydrogenase. CA An 11-beta-hydroxysteroid + NADP(+) = an 11-oxosteroid + NADPH. PR PROSITE; PDOC00060; DR P28845, DHI1_HUMAN; P50172, DHI1_MOUSE; P16232, DHI1_RAT ; DR Q29608, DHI1_SAISC; P51975, DHI1_SHEEP; O77667, DHI2_BOVIN; DR P80365, DHI2_HUMAN; P51661, DHI2_MOUSE; P51976, DHI2_RABIT; DR P50233, DHI2_RAT ; P50168, DHI2_SHEEP; // ID 1.1.1.147 DE 16-alpha-hydroxysteroid dehydrogenase. CA A 16-alpha-hydroxysteroid + NAD(P)(+) = a 16-oxosteroid + NAD(P)H. // ID 1.1.1.148 DE Estradiol 17-alpha-dehydrogenase. CA Estradiol-17-alpha + NAD(P)(+) = estrone + NAD(P)H. // ID 1.1.1.149 DE 20-alpha-hydroxysteroid dehydrogenase. CA 17-alpha,20-alpha-dihydroxypregn-4-en-3-one + NAD(P)(+) = 17-alpha- CA hydroxyprogesterone + NAD(P)H. CC -!- A-specific with respect to NAD(P)(+). PR PROSITE; PDOC00061; DR P35430, AHD2_TETPY; P16116, ALDR_BOVIN; P80508, PE2R_RABIT; DR P51652, PE2R_RAT ; // ID 1.1.1.150 DE 21-hydroxysteroid dehydrogenase (NAD+). CA Pregnan-21-ol + NAD(+) = pregnan-21-al + NADH. CC -!- Acts on a number of 21-hydroxycorticosteroids. // ID 1.1.1.151 DE 21-hydroxysteroid dehydrogenase (NADP+). CA Pregnan-21-ol + NADP(+) = pregnan-21-al + NADPH. CC -!- Acts on a number of 21-hydroxycorticosteroids. // ID 1.1.1.152 DE 3-alpha-hydroxy-5-beta-androstane-17-one 3-alpha-dehydrogenase. AN Etiocholanolone 3-alpha-dehydrogenase. CA 3-alpha-hydroxy-5-beta-androstan-17-one + NAD(+) = 5-beta-androstane- CA 3,17-dione + NADH. // ID 1.1.1.153 DE Sepiapterin reductase. CA 7,8-dihydrobiopterin + NADP(+) = sepiapterin + NADPH. DR P35270, SPRE_HUMAN; Q64105, SPRE_MOUSE; P18297, SPRE_RAT ; // ID 1.1.1.154 DE Ureidoglycolate dehydrogenase. CA (S)-ureidoglycolate + NAD(P)(+) = oxalureate + NAD(P)H. DR P58408, ALLD_ECO57; P77555, ALLD_ECOLI; // ID 1.1.1.155 DE Homoisocitrate dehydrogenase. CA (-)-1-hydroxy-1,2,4-butanetricarboxylate + NAD(+) = 2-oxoadipate + CA CO(2) + NADH. // ID 1.1.1.156 DE Glycerol 2-dehydrogenase (NADP+). AN Dihydroxyacetone reductase. CA Glycerol + NADP(+) = glycerone + NADPH. // ID 1.1.1.157 DE 3-hydroxybutyryl-CoA dehydrogenase. AN Beta-hydroxybutyryl-CoA dehydrogenase. AN BHBD. CA (S)-3-hydroxybutanoyl-CoA + NADP(+) = 3-acetoacetyl-CoA + NADPH. PR PROSITE; PDOC00065; DR P45856, HBD_BACSU ; Q45223, HBD_BRAJA ; P52041, HBD_CLOAB ; DR P45364, HBD_CLODI ; P81343, HBD_CLOPA ; P77851, HBD_CLOTS ; DR Q9RVG1, HBD_DEIRA ; P76083, PAAH_ECOLI; // ID 1.1.1.158 DE UDP-N-acetylmuramate dehydrogenase. AN UDP-N-acetylenolpyruvoylglucosamine reductase. AN UDP-N-acetylglucosamine-enoylpyruvate reductase. AN UDP-GlcNAc-enoylpyruvate reductase. AN Uridine diphosphoacetylpyruvoylglucosamine reductase. AN Uridine diphospho-N-acetylglucosamine-enolpyruvate reductase. AN Uridine-5'-diphospho-N-acetyl-2-amino-2-deoxy-3-O-lactylglucose:NADP- AN oxidoreductase. CA UDP-N-acetylmuramate + NADP(+) = UDP-N-acetyl-3-O-(1-carboxyvinyl)- CA D-glucosamine + NADPH. CF FAD. CC -!- Sodium dithionite, sodium borohydride and, to a lesser extent, NADH CC can replace NADPH. DR Q8NTF4, MUB1_CORGL; Q8NTB0, MUB2_CORGL; Q8UDN0, MURB_AGRT5; DR Q8YM74, MURB_ANASP; O66805, MURB_AQUAE; Q9K9T1, MURB_BACHD; DR Q45305, MURB_BACLI; P18579, MURB_BACSU; O51544, MURB_BORBU; DR Q9X6Y8, MURB_BORPE; Q8YI64, MURB_BRUME; Q8FZP4, MURB_BRUSU; DR P57153, MURB_BUCAI; Q8KA63, MURB_BUCAP; P59450, MURB_BUCBP; DR Q9PM01, MURB_CAMJE; Q9A5A7, MURB_CAUCR; Q9PL89, MURB_CHLMU; DR Q9Z6S1, MURB_CHLPN; O84838, MURB_CHLTR; Q97LP4, MURB_CLOAB; DR Q8XNI0, MURB_CLOPE; Q9RWN8, MURB_DEIRA; Q8X711, MURB_ECO57; DR Q8FB88, MURB_ECOL6; P08373, MURB_ECOLI; Q8RDQ3, MURB_FUSNN; DR P44605, MURB_HAEIN; Q9ZJJ4, MURB_HELPJ; O25963, MURB_HELPY; DR Q9CGD5, MURB_LACLA; Q8EZC5, MURB_LEPIN; Q92BT5, MURB_LISIN; DR Q8Y776, MURB_LISMO; Q9CB48, MURB_MYCLE; Q11148, MURB_MYCTU; DR Q9JV28, MURB_NEIMA; Q9K016, MURB_NEIMB; Q8ESR4, MURB_OCEIH; DR P57952, MURB_PASMU; Q9HZM7, MURB_PSEAE; Q8XWC4, MURB_RALSO; DR Q98KB5, MURB_RHILO; Q92NM1, MURB_RHIME; Q92IT8, MURB_RICCN; DR Q9ZDS7, MURB_RICPR; Q8Z316, MURB_SALTI; P37417, MURB_SALTY; DR Q8EK85, MURB_SHEON; Q99VN6, MURB_STAAM; Q93G02, MURB_STAAW; DR Q8CPZ7, MURB_STAEP; Q8E553, MURB_STRA3; Q9L0L7, MURB_STRCO; DR Q8DUF8, MURB_STRMU; Q8K7K5, MURB_STRP3; Q8P150, MURB_STRP8; DR Q97Q41, MURB_STRPN; Q99ZS9, MURB_STRPY; Q8DLV6, MURB_SYNEL; DR P95837, MURB_SYNP7; P74529, MURB_SYNY3; Q9X239, MURB_THEMA; DR Q8R8Z6, MURB_THETN; O83128, MURB_TREPA; Q9KV40, MURB_VIBCH; DR Q87KP5, MURB_VIBPA; Q8DD33, MURB_VIBVU; Q8D243, MURB_WIGBR; DR Q8PLJ3, MURB_XANAC; Q8P9R1, MURB_XANCP; Q9PAE6, MURB_XYLFA; DR Q87A76, MURB_XYLFT; Q8ZAN4, MURB_YERPE; Q9RNM8, MURB_ZYMMO; // ID 1.1.1.159 DE 7-alpha-hydroxysteroid dehydrogenase. CA 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + NAD(+) = CA 3-alpha,12-alpha-dihydroxy-7-oxo-5-beta-cholanate + NADH. CC -!- Catalyzes the oxidation of the 7-alpha-hydroxyl group of bile acids CC and alcohols both in their free and conjugated forms. CC -!- The Bacteroides fragilis and clostridium enzymes can also utilize CC NADP(+). PR PROSITE; PDOC00060; DR P07914, BA71_EUBSP; P19337, BA72_EUBSP; P50200, HDHA_CLOSO; DR P25529, HDHA_ECOLI; // ID 1.1.1.160 DE Dihydrobunolol dehydrogenase. AN Bunolol reductase. CA (+-)-5-[(tert-butylaminol)-2'-hydroxypropoxy]-1,2,3,4-tetrahydro-1- CA naphthol + NADP(+) = (+-)-5-[(tert-butylaminol)-2'-hydroxypropoxy]- CA 3,4-dihydro-1(2H)-naphthalenone + NADPH. CC -!- Also acts, more slowly, with NAD(+). // ID 1.1.1.161 DE Cholestanetetraol 26-dehydrogenase. AN TEHC-NAD oxidoreductase. CA 5-beta-cholestane-3-alpha,7-alpha,12-alpha,26-tetraol + NAD(+) = CA 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-al + NADH. // ID 1.1.1.162 DE Erythrulose reductase. AN D-Erythrulose reductase. CA Erythritol + NADP(+) = D-erythrulose + NADPH. CC -!- Also acts, more slowly, with NAD(+). // ID 1.1.1.163 DE Cyclopentanol dehydrogenase. CA Cyclopentanol + NAD(+) = cyclopentanone + NADH. // ID 1.1.1.164 DE Hexadecanol dehydrogenase. CA Hexadecanol + NAD(+) = hexadecanal + NADH. CC -!- The liver enzyme acts on long-chain alcohols from C(8) to C(16). CC -!- The Euglena enzyme also oxidizes the aldehydes to fatty acids. // ID 1.1.1.165 DE 2-alkyn-1-ol dehydrogenase. CA 2-butyne-1,4-diol + NAD(+) = 4-hydroxy-2-butynal + NADH. CC -!- Also acts on a variety of 2-alkyn-1-ols, and also 1,4-butanediol. CC -!- NADP(+) acts as acceptor, more slowly. // ID 1.1.1.166 DE Hydroxycyclohexanecarboxylate dehydrogenase. CA (1S,3R,4S)-3,4-dihydroxycyclohexane-1-carboxylate + NAD(+) = CA (1S,4S)-4-hydroxy-3-oxocyclohexane-1-carboxylate + NADH. CC -!- Acts on hydroxycyclohexanecarboxylates having an equatorial carboxyl CC group at C-1, an axial hydroxyl group at C-3 and an equatorial CC hydroxyl or carbonyl group at C-4, including (-)-quinate and CC (-)-shikimate. // ID 1.1.1.167 DE Hydroxymalonate dehydrogenase. CA Hydroxymalonate + NAD(+) = oxomalonate + NADH. // ID 1.1.1.168 DE 2-dehydropantolactone reductase (A-specific). AN 2-dehydropantoyl-lactone reductase (A-specific). AN Ketopantoyl lactone reductase. AN 2-Ketopantoyl lactone reductase. CA (R)-pantolactone + NADP(+) = 2-dehydropantolactone + NADPH. CC -!- The yeast enzyme differs from that from E.coli (EC 1.1.1.214), which CC is specific for the B-face of NADP, and in receptor requirements from CC EC 1.1.99.26. // ID 1.1.1.169 DE 2-dehydropantoate 2-reductase. AN Ketopantoate reductase. AN Ketopantoic acid reductase. AN KPA reductase. CA (R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH. DR Q8YX96, PANE_ANASP; O67619, PANE_AQUAE; O28578, PANE_ARCFU; DR O34661, PANE_BACSU; Q9ABG6, PANE_CAUCR; Q8XE72, PANE_ECO57; DR P77728, PANE_ECOLI; Q9HRF0, PANE_HALN1; Q9CFY8, PANE_LACLA; DR Q929X1, PANE_LISIN; Q8Y5L2, PANE_LISMO; Q50648, PANE_MYCTU; DR Q9HW09, PANE_PSEAE; Q9V0N0, PANE_PYRAB; Q8ZT70, PANE_PYRAE; DR O50098, PANE_PYRHO; Q987N5, PANE_RHILO; Q8Z8W3, PANE_SALTI; DR P37402, PANE_SALTY; Q9HDU6, PANE_SCHPO; Q8P1F1, PANE_STRP8; DR Q9A0B3, PANE_STRPY; Q9KPQ9, PANE_VIBCH; P38787, PANE_YEAST; DR Q8ZC51, PANE_YERPE; // ID 1.1.1.170 DE Sterol-4-alpha-carboxylate 3-dehydrogenase (decarboxylating). AN 3-beta-hydroxy-4-alpha-methylcholestenecarboxylate 3-dehydrogenase AN (decarboxylating). AN Sterol 4-alpha-carboxylic decarboxylase. AN 3-beta-hydroxy-4-beta-methylcholestenecarboxylate 3-dehydrogenase AN (decarboxylating). AN 3-beta-hydroxy-4-beta-methylcholestenoate dehydrogenase. AN 3-beta-hydroxy-4-beta-methylcholestenoate dehydrogenase. CA 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha- CA carboxylate + NAD(P)+ = 4-alpha-methyl-5-alpha-cholest-7-en-3-one CA + CO(2) + NAD(P)H. CC -!- Also acts on 3-beta-hydroxy-5-alpha-cholest-7-ene-4-alpha- CC carboxylate. // ID 1.1.1.171 DE Transferred entry: 1.5.1.20. // ID 1.1.1.172 DE 2-oxoadipate reductase. AN Alpha-ketoadipate reductase. AN 2-ketoadipate reductase. CA 2-hydroxyadipate + NAD(+) = 2-oxoadipate + NADH. // ID 1.1.1.173 DE L-rhamnose 1-dehydrogenase. CA L-rhamnofuranose + NAD(+) = L-rhamno-1,4-lactone + NADH. // ID 1.1.1.174 DE Cyclohexane-1,2-diol dehydrogenase. CA Trans-cyclohexane-1,2-diol + NAD(+) = 2-hydroxycyclohexan-1-one + NADH. CC -!- Also oxidizes, more slowly the cis isomer and 2-hydroxycyclohexanone. // ID 1.1.1.175 DE D-xylose 1-dehydrogenase. AN NAD-D-xylose dehydrogenase. AN D-Xylose dehydrogenase. AN NAD-linked D-xylose dehydrogenase. CA D-xylose + NAD(+) = D-xylonolactone + NADH. // ID 1.1.1.176 DE 12-alpha-hydroxysteroid dehydrogenase. CA 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholanate + NADP(+) = CA 3-alpha,7-alpha-dihydroxy-12-oxo-5-beta-cholanate + NADPH. CC -!- Catalyzes the oxidation of the 12-alpha-hydroxyl group of bile CC acids, both in their free and conjugated form. CC -!- Also acts on bile alcohols. DR P21215, 12AH_CLOS4; // ID 1.1.1.177 DE Glycerol-3-phosphate 1-dehydrogenase (NADP+). CA Sn-glycerol 3-phosphate + NADP(+) = D-glyceraldehyde 3-phosphate + NADPH. // ID 1.1.1.178 DE 3-hydroxy-2-methylbutyryl-CoA dehydrogenase. AN 2-methyl-3-hydroxybutyryl-CoA dehydrogenase. CA (2S,3S)-3-hydroxy-2-methylbutanol-CoA + NAD(+) = 2-methylacetoacetyl-CoA CA + NADH. CC -!- Also acts, more slowly, on (2S,3S)-2-hydroxy-3-methylpentanoyl-CoA. // ID 1.1.1.179 DE D-xylose 1-dehydrogenase (NADP+). AN D-xylose-NADP dehydrogenase. CA D-xylose + NADP(+) = D-xylono-1,5-lactone + NADPH. CC -!- Also acts, more slowly, on L-arabinose and D-ribose. // ID 1.1.1.180 DE Transferred entry: 1.1.1.131. // ID 1.1.1.181 DE Cholest-5-ene-3-beta,7-alpha-diol 3-beta-dehydrogenase. AN 3-beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase. CA Cholest-5-ene-3-beta,7-alpha-diol + NAD(+) = 7-alpha-hydroxycholest-4- CA en-3-one + NADH. CC -!- Highly specific for 3-beta-hydroxy-C(27)-steroids with delta(5)- CC double bond. // ID 1.1.1.182 DE Transferred entry: 1.1.1.198, 1.1.1.227 and 1.1.1.228. // ID 1.1.1.183 DE Geraniol dehydrogenase. CA Geraniol + NADP(+) = geranial + NADPH. CC -!- Also acts, more slowly, on nerol, farnesol and citronellol. // ID 1.1.1.184 DE Carbonyl reductase (NADPH). AN Aldehyde reductase I. AN Xenobiotic ketone reductase. AN NADPH-dependent carbonyl reductase. AN Prostaglandin 9-ketoreductase. CA R-CHOH-R' + NADP(+) = R-CO-R' + NADPH. CC -!- Acts on a wide range of carbonyl compounds, including quinones, CC aromatic aldehydes, ketoaldehydes, daunorubicin, and prostaglandins CC E and F, reducing them to the corresponding alcohol. CC -!- B-specific with respect to NADPH (cf. EC 1.1.1.2). PR PROSITE; PDOC00060; DR Q21929, CBR2_CAEEL; P08074, CBR2_MOUSE; Q29529, CBR2_PIG ; DR O75828, DHC3_HUMAN; P16152, DHCA_HUMAN; P48758, DHCA_MOUSE; DR P47844, DHCA_RABIT; P47727, DHCA_RAT ; // ID 1.1.1.185 DE L-glycol dehydrogenase. CA An L-glycol + NAD(P)(+) = a 2-hydroxycarbonyl compound + NAD(P)H. CC -!- The 2-hydroxycarbonyl compound formed can be further oxidized to a CC vicinal dicarbonyl compound. CC -!- In the reverse direction, vicinal diketones, glyceraldehyde, CC glyoxal, methylglyoxal, 2-oxohydroxyketones and 2-keto-acid esters CC can be reduced. // ID 1.1.1.186 DE dTDP-galactose 6-dehydrogenase. AN Thymidine-diphosphate-galactose dehydrogenase. CA dTDP-D-galactose + 2 NADP(+) + H(2)O = dTDP-D-galacturonate + 2 NADPH. // ID 1.1.1.187 DE GDP-4-dehydro-D-rhamnose reductase. AN GDP-4-keto-6-deoxy-D-mannose reductase. AN GDP-4-keto-D-rhamnose reductase. AN Guanosine diphosphate-4-keto-D-rhamnose reductase. CA GDP-6-deoxy-D-mannose + NAD(P)(+) = GDP-4-dehydro-6-deoxy-D-mannose + CA NAD(P)H. CC -!- In the reverse reaction, a mixture of GDP-D-rhamnose and its C-4 CC epimer is formed. // ID 1.1.1.188 DE Prostaglandin-F synthase. AN Prostaglandin-D2 11-reductase. AN PGD2 11-ketoreductase. AN Prostaglandin 11-ketoreductase. AN Prostaglandin-D2 11-ketoreductase. AN Prostaglandin-D2 ketoreductase. AN Prostaglandin-F synthetase. AN PGF synthetase. CA (5Z,13E)-(15S)-9-alpha,11-alpha,15-trihydroxyprosta-5,13-dienoate + CA NADP(+) = (5Z,13E)-(15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate CA + NADPH. CC -!- Reduces prostaglandin D2 and prostaglandin H2 to prostaglandin F2. CC -!- Prostaglandin D2 is not an intermediate in the reduction of CC prostaglandin H2. CC -!- Also catalyzes the reduction of an number of carbonyl compounds, CC such as 9,10-phenanthrenequinone and 4-nitroacetophenone. PR PROSITE; PDOC00061; DR P42330, AKC3_HUMAN; P52897, PGF2_BOVIN; P05980, PGFS_BOVIN; // ID 1.1.1.189 DE Prostaglandin-E2 9-reductase. AN 9-keto-prostaglandin E2 reductase. AN 9-ketoprostaglandin reductase. AN PGE2 9-oxoreductase. AN PGE2 9-ketoreductase. AN Prostaglandin-E2 9-oxoreductase. CA (5Z,13E)-(15S)-9,11,15-trihydroxyprosta-5,13-dienoate + NADP(+) = CA (5Z,13E)-(15S)-11,15-dihydroxy-9-oxoprosta-5,13-dienoate + NADPH. CC -!- Reduces prostaglandin E2 to prostaglandin F2-alpha. CC -!- A number of other 9-oxo- and 15-oxo-prostaglandin derivatives can CC also be reduced to the corresponding hydroxy compound. CC -!- May be identical with EC 1.1.1.197. PR PROSITE; PDOC00060; DR P16152, DHCA_HUMAN; P80508, PE2R_RABIT; // ID 1.1.1.190 DE Indole-3-acetaldehyde reductase (NADH). CA Indole-3-ethanol + NAD(+) = indole-3-acetaldehyde + NADH. // ID 1.1.1.191 DE Indole-3-acetaldehyde reductase (NADPH). CA Indole-3-ethanol + NADP(+) = indole-3-acetaldehyde + NADPH. // ID 1.1.1.192 DE Long-chain-alcohol dehydrogenase. AN Fatty alcohol oxidoreductase. CA A long-chain alcohol + 2 NAD(+) + H(2)O = a long-chain carboxylate + CA 2 NADH. CC -!- Hexadecanol is a good substrate. // ID 1.1.1.193 DE 5-amino-6-(5-phosphoribosylamino)uracil reductase. CA 5-amino-6-(5-phosphoribitylamino)uracil + NADP(+) = 5-amino-6-(5- CA phosphoribosylamino)uracil + NADPH. DR O28272, RIB7_ARCFU; Q9P4B8, RIB7_KLUMA; Q58085, RIB7_METJA; DR O26337, RIB7_METTH; P95872, RIB7_SULSO; P33312, RIB7_YEAST; DR P50853, RIBD_ACTPL; O66534, RIBD_AQUAE; P70814, RIBD_BACAM; DR P17618, RIBD_BACSU; Q9PLJ6, RIBD_CHLMU; Q9Z735, RIBD_CHLPN; DR O84735, RIBD_CHLTR; O24750, RIBD_CORAM; P25539, RIBD_ECOLI; DR P44326, RIBD_HAEIN; P71677, RIBD_MYCTU; Q55158, RIBD_SYNY3; DR P57534, RID2_BUCAI; Q8K9A3, RID2_BUCAP; // ID 1.1.1.194 DE Coniferyl-alcohol dehydrogenase. CA Coniferyl alcohol + NADP(+) = coniferyl aldehyde + NADPH. CC -!- Specific for coniferyl alcohol; does not act on cinnamyl alcohol, CC 4-coumaryl alcohol or sinapyl alcohol. // ID 1.1.1.195 DE Cinnamyl-alcohol dehydrogenase. AN CAD. CA Cinnamyl alcohol + NADP(+) = cinnamaldehyde + NADPH. CC -!- Acts on coniferyl alcohol, sinapyl alcohol, 4-coumaryl alcohol and CC cinnamyl alcohol (cf. EC 1.1.1.194). PR PROSITE; PDOC00058; DR P42495, CAD1_ARACO; P48523, CAD1_ARATH; Q42726, CAD1_EUCGU; DR O49482, CAD2_ARATH; P31655, CAD2_EUCGU; O82035, CAD2_PICAB; DR P30359, CAD4_TOBAC; Q08350, CAD7_PICAB; P30360, CAD9_TOBAC; DR P50746, CADH_EUCBO; O64969, CADH_EUCGL; O22380, CADH_LOLPR; DR O24562, CADH_MAIZE; P31656, CADH_MEDSA; Q40976, CADH_PINRA; DR P41637, CADH_PINTA; P31657, CADH_POPDE; O82056, CADH_SACOF; // ID 1.1.1.196 DE 15-hydroxyprostaglandin-D dehydrogenase (NADP+). AN Prostaglandin-D 15-dehydrogenase (NADP+). CA (5Z,13E)-(15S)-9-alpha,15-dihydroxy-11-oxoprosta-5,13-dienoate + NADP(+) CA = (5Z,13E)-9-alpha-hydroxy-11,15-dioxoprosta-5,13-dienoate + NADPH. CC -!- Specific for prostaglandins D (cf. EC 1.1.1.141 and EC 1.1.1.197). // ID 1.1.1.197 DE 15-hydroxyprostaglandin dehydrogenase (NADP+). CA (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprost-13-enoate + NADP(+) = CA (5Z,13E)-11-alpha-hydroxy-9,15-dioxoprost-13-enoate + NADPH. CC -!- Acts on prostaglandins E2, F2-alpha and B1, but not on prostaglandin CC D2 (cf. EC 1.1.1.141 and EC 1.1.1.196). CC -!- May be identical with EC 1.1.1.189. PR PROSITE; PDOC00060; DR P16152, DHCA_HUMAN; // ID 1.1.1.198 DE (+)-borneol dehydrogenase. CA (+)-borneol + NAD(+) = (+)-camphor + NADH. CC -!- NADP(+) can also act, more slowly. CC -!- Formerly EC 1.1.1.182. // ID 1.1.1.199 DE (S)-usnate reductase. CA In the reverse direction, (S)-usnate is reduced by NADH with cleavage of CA the ether bond to form a 7-hydroxy group. // ID 1.1.1.200 DE Aldose-6-phosphate reductase (NADPH). AN NADP-dependent D-sorbitol-6-phosphate dehydrogenase. CA D-sorbitol 6-phosphate + NADP(+) = D-glucose 6-phosphate + NADPH. CC -!- In the reverse reaction, acts also on D-galactose 6-phosphate, and, CC more slowly, on D-mannose 6-phosphate and 2-deoxy-D-glucose CC 6-phosphate. PR PROSITE; PDOC00061; DR P28475, S6PD_MALDO; // ID 1.1.1.201 DE 7-beta-hydroxysteroid dehydrogenase (NADP+). AN NADP-dependent 7-beta-hydroxysteroid dehydrogenase. CA A 7-beta-hydroxysteroid + NADP(+) = a 7-oxosteroid + NADPH. CC -!- Catalyzes the oxidation of the 7-beta-hydroxyl group of bile acids CC such as ursodeoxycholate. // ID 1.1.1.202 DE 1,3-propanediol dehydrogenase. AN 3-hydroxypropionaldehyde reductase. AN 1,3-propanediol oxidoreductase. CA Propane-1,3-diol + NAD(+) = 3-hydroxypropanal + NADH. PR PROSITE; PDOC00059; DR P45513, DHAT_CITFR; Q59477, DHAT_KLEPN; // ID 1.1.1.203 DE Uronate dehydrogenase. AN Uronic acid dehydrogenase. CA D-galacturonate + NAD(+) + H(2)O = D-galactarate + NADH. CC -!- Also acts on D-glucuronate. CC -!- Formerly EC 1.2.1.35. // ID 1.1.1.204 DE Xanthine dehydrogenase. AN Xanthine oxidoreductase. CA Xanthine + NAD(+) + H(2)O = urate + NADH. CF Molybdenum. CC -!- Acts on a variety of purines and aldehydes. CC -!- The animal enzyme can be interconverted to EC 1.1.3.22 (oxidase CC form). That from liver exists in vivo mainly in the dehydrogenase CC form, but can be converted into EC 1.1.3.22 by storage at -20C, by CC treatment with proteolytic agents or organic solvents, or by thiol CC reagents such as Cu(2+), N-ethylmaleimide or 4-hydroxy- CC mercuribenzoate. The effect of thiol reagents can be reversed by CC thiols such as 1,4-dithioerythritol. CC -!- EC 1.1.1.204 can also be converted into EC 1.1.3.22 by EC 1.8.4.7 in CC the presence of oxidized glutathione. CC -!- In other animal tissues the enzyme exists almost entirely as CC EC 1.1.3.22, but can be converted into the dehydrogenase form by CC 1,4-dithioerythritol. CC -!- Formerly EC 1.2.1.37. PR PROSITE; PDOC00484; DR O32147, XDHA_BACSU; Q8X6C7, XDHA_ECO57; Q46799, XDHA_ECOLI; DR Q8X6C5, XDHB_ECO57; Q46800, XDHB_ECOLI; O32145, XDHC_BACSU; DR O32144, XDHD_BACSU; O32143, XDHE_BACSU; P80457, XDH_BOVIN ; DR P08793, XDH_CALVI ; P47990, XDH_CHICK ; P10351, XDH_DROME ; DR P22811, XDH_DROPS ; P91711, XDH_DROSU ; Q12553, XDH_EMENI ; DR P47989, XDH_HUMAN ; Q00519, XDH_MOUSE ; P22985, XDH_RAT ; DR Q8X6J4, YAGR_ECO57; P77489, YAGR_ECOLI; Q8X6J0, YAGS_ECO57; DR P77324, YAGS_ECOLI; // ID 1.1.1.205 DE IMP dehydrogenase. AN Inosine-5'-monophosphate dehydrogenase. AN Inosinic acid dehydrogenase. AN Inosinate dehydrogenase. AN IMP oxidoreductase. AN Inosine monophosphate oxidoreductase. CA Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH. CC -!- The enzyme acts on the hydroxyl group of the hydrated derivative of CC the substrate. CC -!- Formerly EC 1.2.1.14. PR PROSITE; PDOC00391; DR P20839, IMD1_HUMAN; P50096, IMD1_MOUSE; P39567, IMD1_YEAST; DR P12268, IMD2_HUMAN; P12269, IMD2_MESAU; P24547, IMD2_MOUSE; DR P38697, IMD2_YEAST; P50095, IMD3_YEAST; P50094, IMD4_YEAST; DR P31002, IMDH_ACICA; O67820, IMDH_AQUAE; P21879, IMDH_BACSU; DR P49058, IMDH_BORBU; Q8KCW4, IMDH_CHLTE; O50316, IMDH_CHLVI; DR Q07152, IMDH_DROME; P06981, IMDH_ECOLI; P44334, IMDH_HAEIN; DR Q9ZL14, IMDH_HELPJ; P56088, IMDH_HELPY; P21620, IMDH_LEIDO; DR Q59011, IMDH_METJA; Q49729, IMDH_MYCLE; Q50715, IMDH_MYCTU; DR Q9L6B7, IMDH_PASMU; Q12658, IMDH_PNECA; Q9UY49, IMDH_PYRAB; DR P42851, IMDH_PYRFU; O58045, IMDH_PYRHO; Q9KH33, IMDH_RHITR; DR O14344, IMDH_SCHPO; Q8K5G1, IMDH_STRP3; P50099, IMDH_STRPY; DR P50097, IMDH_TRIFO; P50098, IMDH_TRYBB; P47996, IMH1_ARATH; DR Q9SA34, IMH2_ARATH; O00086, IMH3_CANAL; // ID 1.1.1.206 DE Tropine dehydrogenase. CA Tropine + NADP(+) = tropinone + NADPH. CC -!- Oxidizes other tropan-3-alpha-ols, but not the corresponding beta- CC derivatives. PR PROSITE; PDOC00060; DR P50162, TRN1_DATST; // ID 1.1.1.207 DE (-)-menthol dehydrogenase. AN Monoterpenoid dehydrogenase. CA (-)-menthol + NADP(+) = (-)-menthone + NADPH. CC -!- Acts on a number of other cyclohexanols and cyclohexenols. CC -!- Not identical with EC 1.1.1.208. // ID 1.1.1.208 DE (+)-neomenthol dehydrogenase. AN Monoterpenoid dehydrogenase. CA (+)-neomenthol + NADP(+) = (-)-menthone + NADPH. CC -!- Acts on a number of other cyclohexanols and cyclohexenols. CC -!- Not identical with EC 1.1.1.207. // ID 1.1.1.209 DE 3(or 17)-alpha-hydroxysteroid dehydrogenase. CA Androsterone + NAD(P)(+) = 5-alpha-androstane-3,17-dione + NAD(P)H. CC -!- Acts on the 3-alpha-hydroxyl group of androgens of the 5-alpha- CC androstane series; and also, more slowly, on the 17-alpha-hydroxyl CC group of both androgenic and estrogenic substrates (cf. EC 1.1.1.51). // ID 1.1.1.210 DE 3-beta(or 20-alpha)-hydroxysteroid dehydrogenase. AN Progesterone reductase. AN 3-beta-HSD. CA 5-alpha-androstan-3-beta,17-beta-diol + NADP(+) = 17-beta-hydroxy- CA 5-alpha-androstan-3-one + NADPH. CC -!- Also acts on 20-alpha-hydroxysteroids. DI Adrenal hyperplasia II; MIM:201810. // ID 1.1.1.211 DE Long-chain-3-hydroxyacyl-CoA dehydrogenase. AN Beta-hydroxyacyl-CoA dehydrogenase. CA (S)-3-hydroxyacyl-CoA + NAD(+) = 3-oxoacyl-CoA + NADH. CC -!- Acts most rapidly on derivatives with chain length C(8) or C(10) CC (cf. EC 1.1.1.35). // ID 1.1.1.212 DE 3-oxoacyl-[acyl-carrier protein] reductase (NADH). CA (3R)-3-hydroxyacyl-[acyl-carrier protein] + NAD(+) = 3-oxoacyl- CA [acyl-carrier protein] + NADH. CC -!- Forms part of the fatty acid synthase system in plants. Can be CC separated from EC 1.1.1.100. // ID 1.1.1.213 DE 3-alpha-hydroxysteroid dehydrogenase (A-specific). CA Androsterone + NAD(P)(+) = 5-alpha-androstane-3,17-dione + NAD(P)H. CC -!- Also acts on other 3-alpha-hydroxysteroids. CC -!- A-specific with respect to NAD(+) or NADP(+). // ID 1.1.1.214 DE 2-dehydropantolactone reductase (B-specific). AN 2-dehydropantoyl-lactone reductase (B-specific). AN 2-ketopantoyl lactone reductase. AN Ketopantoyl lactone reductase. CA (R)-pantolactone + NADP(+) = 2-dehydropantolactone + NADPH. CC -!- The E.coli enzyme differs from that from yeast (EC 1.1.1.168), which CC is specific for the A-face of NADP, and in receptor requirements from CC EC 1.1.99.26. // ID 1.1.1.215 DE Gluconate 2-dehydrogenase. AN 2-keto-d-gluconate reductase. AN 2-ketogluconate reductase. CA D-gluconate + NADP(+) = 2-dehydro-D-gluconate + NADPH. CC -!- Also acts on L-idonate, D-galactonate and D-xylonate. DR O32264, TKRA_BACSU; P58220, TKRA_ECO57; P37666, TKRA_ECOLI; DR P58000, TKRA_ERWHE; // ID 1.1.1.216 DE Farnesol dehydrogenase. CA 2-trans,6-trans-farnesol + NADP(+) = 2-trans,6-trans-farnesal + NADPH. CC -!- Also acts, more slowly, on 2-cis,6-trans-farnesol, geraniol, CC citronerol and nerol. // ID 1.1.1.217 DE Benzyl-2-methyl-hydroxybutyrate dehydrogenase. AN Benzyl 2-methyl-3-hydroxybutyrate dehydrogenase. CA Benzyl (2R,3S)-2-methyl-3-hydroxybutanoate + NADP(+) = benzyl CA 2-methyl-3-oxobutanoate + NADPH. CC -!- Also acts on benzyl (2S,3S)-2-methyl-3-hydroxybutanoate; otherwise CC highly specific. // ID 1.1.1.218 DE Morphine 6-dehydrogenase. AN Naloxone reductase. CA Morphine + NAD(P)(+) = morphinone + NAD(P)H. CC -!- Also acts on other alkaloids, including codeine, normorphine and CC ethylmorphine, but only very slowly on 7,8-saturated derivatives CC such as dihydromorphine and dihydrocodeine. CC -!- In the reverse direction, also reduces naloxone to the 6-alpha- CC hydroxy analog. CC -!- Activated by 2-mercaptoethanol. PR PROSITE; PDOC00061; DR P82809, AKCD_MESAU; Q02198, MORA_PSEPU; P82810, MORA_RABIT; // ID 1.1.1.219 DE Dihydrokaempferol 4-reductase. AN Dihydroflavonol 4-reductase. AN NADPH-dihydromyricetin reductase. CA Cis-3,4-leucopelargonidin + NADP(+) = (+)-dihydrokaempferol + NADPH. CC -!- Also acts, in the reverse direction, on (+)-dihydroquercetin and CC (+)-dihydromyricetin. CC -!- Each dihydroflavonol is reduced to the corresponding cis-flavon- CC 3,4-diol. CC -!- NAD(+) can act instead of NADP(+), more slowly. CC -!- Involved in the biosynthesis of anthocyanidins in plants. DR P14721, DFRA_ANTMA; P51102, DFRA_ARATH; P51103, DFRA_CALCH; DR P51104, DFRA_DIACA; P51105, DFRA_GERHY; P51106, DFRA_HORVU; DR P51107, DFRA_LYCES; P51108, DFRA_MAIZE; P51109, DFRA_MEDSA; DR P14720, DFRA_PETHY; P73212, DFRA_SYNY3; P51110, DFRA_VITVI; // ID 1.1.1.220 DE 6-pyruvoyltetrahydropterin 2'-reductase. AN 6PPH4(2'-oxo) reductase. AN 6-pyruvoyl tetrahydropterin (2'-oxo)reductase. AN 6-pyruvoyl-tetrahydropterin 2'-reductase. AN Pyruvoyl-tetrahydropterin reductase. CA 6-lactoyl-5,6,7,8-tetrahydropterin + NADP(+) = CA 6-pyruvoyl-tetrahydropterin + NADPH. CC -!- Not identical with EC 1.1.1.153. // ID 1.1.1.221 DE Vomifoliol 4'-dehydrogenase. CA (+-)-6-hydroxy-3-oxo-alpha-ionol + NAD(+) = (+-)-6-hydroxy-3-oxo- CA alpha-ionone + NADH. CC -!- Oxidizes vomifoliol to dehydrovomifoliol. CC -!- Involved in the metabolism of abscisic acid in Corynebacterium sp. // ID 1.1.1.222 DE (R)-4-hydroxyphenyllactate dehydrogenase. AN (R)-aromatic lactate dehydrogenase. CA (R)-3-(4-hydroxyphenyl)lactate + NAD(P)(+) = 3-(4-hydroxyphenyl)pyruvate CA + NAD(P)H. CC -!- Also acts, more slowly, on (R)-3-phenyllactate, (R)-3-(indole-3- CC yl)lactate and (R)-lactate. // ID 1.1.1.223 DE Isopiperitenol dehydrogenase. CA (-)-trans-isopiperitenol + NAD(+) = (-)-isopiperitenone + NADH. CC -!- Acts on (-)-trans-isopiperitenol, (+)-trans-piperitenol and CC (+)-trans-pulegol. CC -!- Involved in the biosynthesis of menthol and related monoterpenes in CC peppermint (Mentha piperita) leaves. // ID 1.1.1.224 DE Mannose-6-phosphate 6-reductase. AN NADPH-dependent M6P reductase. AN NADPH-mannose-6-P reductase. CA D-mannitol 1-phosphate + NADP(+) = D-mannose 6-phosphate + NADPH. CC -!- Involved in the biosynthesis of mannitol in celery (Apium CC graveolens) leaves. // ID 1.1.1.225 DE Chlordecone reductase. AN CDR. CA Chlordecone alcohol + NADP(+) = chlordecone + NADPH. CC -!- Chlordecone, an organochlorine pesticide, is 1,1A,3,3A,4,5,5A,5B,6- CC decachlorooctahydro-1,3,4-metheno-2H-cyclobuta[CD]pentalen-2-one. PR PROSITE; PDOC00061; DR P17516, AKC4_HUMAN; // ID 1.1.1.226 DE 4-hydroxycyclohexanecarboxylate dehydrogenase. CA 4-hydroxycyclohexanecarboxylate + NAD(+) = 4-oxocyclohexanecarboxylate CA + NADH. CC -!- The enzyme, from Corynebacterium cyclohexanicum, is highly specific CC for the trans-4-hydroxy derivative. // ID 1.1.1.227 DE (-)-borneol dehydrogenase. CA (-)-borneol + NAD(+) = (-)-camphor + NADH. CC -!- NADP(+) can also act, more slowly. CC -!- Formerly EC 1.1.1.182. // ID 1.1.1.228 DE (+)-sabinol dehydrogenase. CA (-)-cis-sabinol + NAD(+) = (+)-sabinone + NADH. CC -!- NADP(+) can also act, more slowly. CC -!- Involved in the biosynthesis of (+)-3-thujone and (-)-3-isothujone. CC -!- Formerly EC 1.1.1.182. // ID 1.1.1.229 DE Diethyl 2-methyl-3-oxosuccinate reductase. CA Diethyl (2R,3R)-2-methyl-3-hydroxysuccinate + NADP(+) = diethyl- CA 2-methyl-3-oxosuccinate + NADPH. CC -!- Also acts on diethyl (2S,3R)-2-methyl-3-hydroxysuccinate, and CC on the corresponding dimethyl esters. // ID 1.1.1.230 DE 3-alpha-hydroxyglycyrrhetinate dehydrogenase. CA 3-alpha-hydroxyglycyrrhetinate + NADP(+) = 3-oxoglycyrrhetinate + CA NADPH. CC -!- Highly specific to 3-alpha-hydroxy derivatives of glycyrrhetinate CC and its analogs. CC -!- Not identical to EC 1.1.1.50. // ID 1.1.1.231 DE 15-hydroxyprostaglandin-I dehydrogenase (NADP+). AN PG I2 dehydrogenase. AN Prostacyclin dehydrogenase. CA (5Z,13E)-(15S)-6,9-alpha-epoxy-11-alpha,15-dihydroxyprosta-5,13- CA dienoate + NADP(+) = (5Z,13E)-6,9-alpha-epoxy-11-alpha-hydroxy-15- CA oxoprosta-5,13-dienoate + NADPH. CC -!- Specific for prostaglandin I2. // ID 1.1.1.232 DE 15-hydroxyicosatetraenoate dehydrogenase. CA (15S)-15-hydroxy-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)(+) = CA 15-oxo-5,8,11-cis-13-trans-icosatetraenoate + NAD(P)H. // ID 1.1.1.233 DE N-acylmannosamine 1-dehydrogenase. AN N-acetyl-D-mannosamine dehydrogenase. AN N-acyl-D-mannosamine dehydrogenase. AN N-acylmannosamine dehydrogenase. CA N-acyl-D-mannosamine + NAD(+) = N-acyl-D-mannosaminolactone + NADH. CC -!- Acts on acetyl-D-mannosamine and glycolyl-D-mannosamine. CC -!- Highly specific. PR PROSITE; PDOC00060; DR P22441, DHMA_FLAS1; // ID 1.1.1.234 DE Flavonone 4-reductase. CA (2S)-flavon-4-ol + NADP(+) = (2S)-flavonone + NADPH. CC -!- Involved in the biosynthesis of 3-deoxyanthocyanidins from CC flavonones such as naringenin or eriodictyol. // ID 1.1.1.235 DE 8-oxocoformycin reductase. CA Coformycin + NADP(+) = 8-oxocoformycin + NADPH. CC -!- B-specific with respect to NADPH. CC -!- Also reduces 8-oxodeoxy-coformycin to the nucleoside antibiotic CC deoxycoformycin. // ID 1.1.1.236 DE Tropinone reductase. AN Tropinone reductase II. AN Pseudotropine forming tropinone reductase. CA Pseudotropine + NADP(+) = tropinone + NADPH. PR PROSITE; PDOC00060; DR P50163, TRN2_DATST; P50164, TRN2_HYONI; // ID 1.1.1.237 DE Hydroxyphenylpyruvate reductase. CA 3-(4-hydroxyphenyl)lactate + NAD(+) = 3-(4-hydroxyphenyl)pyruvate + CA NADH. CC -!- Also acts on 3-(3,4-dihydroxyphenyl)lactate. CC -!- Involved with EC 2.3.1.140 in the biosynthesis of rosmarinic acid. // ID 1.1.1.238 DE 12-beta-hydroxysteroid dehydrogenase. CA 3-alpha,7-alpha,12-beta-trihydroxy-5-beta-cholanate + NADP(+) = CA 3-alpha,7-alpha-dihydroxy-12-oxo-5-beta-cholanate + NADPH. CC -!- Acts on a number of bile acids, both in their free and conjugated CC forms. // ID 1.1.1.239 DE 3-alpha (17-beta)-hydroxysteroid dehydrogenase (NAD+). CA Testosterone + NAD(+) = androst-4-ene-3,17-dione + NADH. CC -!- Also acts on other 17-beta-hydroxysteroids, on the 3-alpha- CC hydroxy group of pregnanes and bile acids, and on benzene CC dihydrodiol. CC -!- Different from EC 1.1.1.50 or EC 1.1.1.213. // ID 1.1.1.240 DE N-acetylhexosamine 1-dehydrogenase. CA N-acetyl-D-glucosamine + NAD(+) = N-acetyl-D-glucosaminate + NADH. CC -!- Also acts on N-acetylgalactosamine and, more slowly, on CC N-acetylmannosamine. // ID 1.1.1.241 DE 6-endo-hydroxycineole dehydrogenase. CA 6-endo-hydroxycineole + NAD(+) = 6-oxocineole + NADH. // ID 1.1.1.242 DE Transferred entry: 1.3.1.69. // ID 1.1.1.243 DE Carveol dehydrogenase. CA (-)-trans-carveol + NADP(+) = (-)-carvone + NADPH. DR Q9RA05, LIMC_RHOER; // ID 1.1.1.244 DE Methanol dehydrogenase. CA Methanol + NAD(+) = formaldehyde + NADH. PR PROSITE; PDOC00059; DR P31005, MEDH_BACMT; // ID 1.1.1.245 DE Cyclohexanol dehydrogenase. CA Cyclohexanol + NAD(+) = cyclohexanone + NADH. CC -!- Also oxidizes some other alicyclic alcohols and diols. // ID 1.1.1.246 DE Pterocarpin synthase. CA Medicarpin + NADP(+) = vestitone + NADPH. CC -!- Catalyzes the final step in the biosynthesis of the pterocarpin CC phytoalexins medicarpin and maackiain. // ID 1.1.1.247 DE Codeinone reductase (NADPH). CA Codeine + NADP(+) = codeinone + NADPH. CC -!- Catalyzes the reversible reduction of codeinone to codeine, which CC is a direct precursor of morphine in the opium poppy plant, CC Papaver somniferum. // ID 1.1.1.248 DE Salutaridine reductase (NADPH). CA Salutaridinol + NADP(+) = salutaridine + NADPH. CC -!- Catalyzes the reversible reduction of salutaridine to CC salutaridinol, which is a direct precursor of morphinan alkaloids CC in the poppy plant. // ID 1.1.1.249 DE Transferred entry: 2.5.1.46. // ID 1.1.1.250 DE D-arabinitol 2-dehydrogenase. AN D-arabinitol 2-dehydrogenase (ribulose-forming). CA D-arabinitol + NAD(+) = D-ribulose + NADH. PR PROSITE; PDOC00060; DR P43066, ARDH_CANAL; P50166, ARDH_CANTR; P50167, ARDH_PICST; // ID 1.1.1.251 DE Galactitol-1-phosphate 5-dehydrogenase. CA Galactitol-1-phosphate + NAD(+) = L-tagatose 6-phosphate + NADH. CF Zinc. PR PROSITE; PDOC00058; DR P37190, GATD_ECOLI; // ID 1.1.1.252 DE Tetrahydroxynaphthalene reductase. AN T4HN reductase. CA Scytalone + NADP(+) = 1,3,6,8-tetrahydroxynaphthalene + NADPH. CC -!- Reduces 1,3,6,8-tetrahydroxynaphthalene to scytalone and also reduces CC 1,3,8-trihydroxynaphthalene to vermelone. CC -!- Involved with EC 4.2.1.94 in the biosynthesis of melanin in CC pathogenic fungi. CC -!- Formerly EC 1.3.1.50. PR PROSITE; PDOC00060; DR Q12634, T4HR_MAGGR; // ID 1.1.1.253 DE Pteridine reductase. AN Pteridine reductase 1. CA 5,6,7,8-tetrahydrobiopterin + 2 NADP(+) = biopterin + 2 NADPH. CC -!- The enzyme from Leishmania (both amastigote and promastigote forms) CC catalyzes the NADPH-dependent reduction of folate and a wide variety CC of unconjugated pterins, including biopterin, to their tetrahydro CC forms. It also catalyzes the reduction of 7,8-dihydropterins and CC 7,8-dihydrofolate to their tetrahydro forms. CC -!- In contrast to EC 1.5.1.3 and EC 1.6.99.7, pteridine reductase will CC not catalyze the reduction of the quinonoid form of dihydrobiopterin. CC -!- The enzyme is specific for NADPH; no activity has been detected with CC NADH. It also differs from EC 1.5.1.3 in being specific for the B CC side of NADPH. PR PROSITE; PDOC00060; DR Q01782, PTR1_LEIMA; P42556, PTR1_LEITA; // ID 1.1.1.254 DE (S)-carnitine 3-dehydrogenase. AN D-carnitine dehydrogenase. CA (S)-carnitine + NAD(+) = 3-dehydrocarnitine + NADH. CC -!- Specific for the (S)-enantiomer of carnitine, i.e. the enantiomer of CC the substrate of EC 1.1.1.108. // ID 1.1.1.255 DE Mannitol dehydrogenase. AN NAD-dependent mannitol dehydrogenase. AN MTD. CA D-mannitol + NAD(+) = D-mannose + NADH. CC -!- The enzyme from Apium graveolens (celery) oxidizes alditols with a CC minimum requirement of 2R chirality at the carbon adjacent to the CC primary carbon undergoing the oxidation. CC -!- The enzyme is specific for NAD and does not use NADP. DR Q02971, MTD1_ARATH; Q43137, MTD1_STYHU; Q02972, MTD2_ARATH; DR Q43138, MTD3_STYHU; P42734, MTDH_ARATH; Q38707, MTD_APIGR ; DR Q9ZRF1, MTD_FRAAN ; O82515, MTD_MEDSA ; P93257, MTD_MESCR ; DR P42754, MTD_PETCR ; // ID 1.1.1.256 DE Fluoren-9-ol dehydrogenase. CA Fluoren-9-ol + 2 NAD(P)(+) = fluoren-9-one + 2 NADPH. CC -!- Involved in the pathway for fluorene metabolism in Arthrobacter sp. // ID 1.1.1.257 DE 4-(hydroxymethyl)benzenesulfonate dehydrogenase. CA 4-(hydroxymethyl)benzenesulfonate + NAD(+) = 4-formylbenzenesulfonate + CA NADH. CC -!- Involved in the toluene-4-sulfonate degradation pathway in CC C.testosteroni. // ID 1.1.1.258 DE 6-hydroxyhexanoate dehydrogenase. CA 6-hydroxyhexanoate + NAD(+) = 6-oxohexanoate + NADH. CC -!- Involved in the cyclohexanol degradation pathway in Acinetobacter CC NCIB 9871. // ID 1.1.1.259 DE 3-hydroxypimeloyl-CoA dehydrogenase. CA 3-hydroxypimeloyl-CoA + NAD(+) = 3-oxopimeloyl-CoA + NADH. CC -!- Involved in the anaerobic pathway of benzoate degradation in CC bacteria. // ID 1.1.1.260 DE Sulcatone reductase. CA Sulcatol + NAD(+) = sulcatone + NADH. CC -!- Studies on the effects of growth-stage and nutrient supply on the CC stereochemistry of sulcatone reduction in Clostridia pasteurianum, CC C. tyrobutyricum and Lactobacillus brevis suggest that there may CC be at least two sulcatone reductases with different CC stereospecificities. // ID 1.1.1.261 DE Glycerol-1-phosphate dehydrogenase [NAD(P)]. CA Sn-glycerol-1-phosphate + NAD(P)(+) = glycerone phosphate + NAD(P)H. CC -!- This enzyme is responsible for the formation of archaea-specific CC glycerophosphate and is stereospecifically different from CC EC 1.1.1.94. DR Q9YER2, EGSA_AERPE; O28599, EGSA_ARCFU; Q9HS49, EGSA_HALN1; DR Q8TJU1, EGSA_METAC; Q58122, EGSA_METJA; Q8TW08, EGSA_METKA; DR Q8PZA4, EGSA_METMA; P72010, EGSA_METTH; Q9V0V0, EGSA_PYRAB; DR Q8ZWP5, EGSA_PYRAE; Q8U147, EGSA_PYRFU; O59144, EGSA_PYRHO; DR Q9UXE7, EGSA_SULSO; P58460, EGSA_SULTO; Q9HJ16, EGSA_THEAC; DR Q979B1, EGSA_THEVO; // ID 1.1.1.262 DE 4-hydroxythreonine-4-phosphate dehydrogenase. AN NAD-dependent threonine 4-phosphate dehydrogenase. AN L-threonine 4-phosphate dehydrogenase. AN 4-(phosphohydroxy)-L-threonine dehydrogenase. CA 4-(phosphonooxy)-threonine + NAD(+) = 2-amino-3-oxo-4- CA phosphonooxybutyrate + NADH. CC -!- The product of the reaction undergoes decarboxylation to give CC 3-amino-2-oxopropyl phosphate. DR Q8UGD4, PDXA_AGRT5; P58711, PDXA_ANASP; O67019, PDXA_AQUAE; DR Q9RC88, PDXA_BACHD; P58712, PDXA_BRUME; Q9PN58, PDXA_CAMJE; DR Q9A7N4, PDXA_CAUCR; P58713, PDXA_ECO57; P19624, PDXA_ECOLI; DR Q47824, PDXA_ERWHE; Q8RGR0, PDXA_FUSNN; Q9ZJ28, PDXA_HELPJ; DR O26103, PDXA_HELPY; Q9JX42, PDXA_NEIMA; Q9K1F9, PDXA_NEIMB; DR Q9CKG8, PDXA_PASMU; P58714, PDXA_RALSO; Q984S6, PDXA_RHILO; DR O85987, PDXA_SPHAR; Q55982, PDXA_SYNY3; Q9KUS1, PDXA_VIBCH; DR Q87ST5, PDXA_VIBPA; Q8DED3, PDXA_VIBVU; Q8PP24, PDXA_XANAC; DR Q8PCE2, PDXA_XANCP; Q9PF39, PDXA_XYLFA; Q87AJ1, PDXA_XYLFT; DR P58719, PDXA_YERPE; Q9I5U4, PXA1_PSEAE; Q92QZ0, PXA1_RHIME; DR P58715, PXA1_SALTI; P58717, PXA1_SALTY; Q9I1Q5, PXA2_PSEAE; DR Q92X16, PXA2_RHIME; P58716, PXA2_SALTI; P58718, PXA2_SALTY; DR Q92TP3, PXA3_RHIME; // ID 1.1.1.263 DE 1,5-anhydro-D-fructose reductase. AN AF reductase. CA 1,5-anhydro-D-glucitol + NADP(+) = 1,5-anhydro-D-fructose + NADPH. CC -!- Also reduces pyridine-3-aldehyde and 2,3-butanedione. CC -!- Acetaldehyde, 2-dehydroglucose (glucosone) and glucuronate are CC poor substrates, but there is no detectable action on glucose, CC mannose and fructose. DR P82125, AFR_PIG ; // ID 1.1.1.264 DE L-idonate 5-dehydrogenase. CA L-idonate + NAD(P)(+) = 5-dehydrogluconate + NAD(P)H. CF Zinc. CC -!- The enzyme from Escherichia coli cannot oxidize D-gluconate to CC form 5-dehydrogluconate, a reaction that is catalyzed by CC EC 1.1.1.69. PR PROSITE; PDOC00058; DR P39346, IDND_ECOLI; // ID 1.1.1.265 DE 3-methylbutanal reductase. CA 3-methylbutanol + NAD(P)(+) = 3-methylbutanal + NAD(P)H. CC -!- The enzyme purified from Saccharomyces cerevisiae catalyzes the CC reduction of a number of straight-chain and branched aldehydes, CC as well as some aromatic aldehydes. // ID 1.1.1.266 DE dTDP-4-dehydro-6-deoxyglucose reductase. AN dTDP-4-keto-6-deoxyglucose reductase. CA dTDP-D-fucose + NADP(+) = dTDP-4-dehydro-6-deoxy-D-glucose + NADPH. CC -!- The enzyme from the gram-negative bacterium Actinobacillus CC actinomycetemcomitans forms activated fucose for incorporation CC into capsular polysaccharide. // ID 1.1.1.267 DE 1-deoxy-D-xylulose-5-phosphate reductoisomerase. AN DXP-reductoisomerase. AN 1-deoxyxylulose-5-phosphate reductoisomerase. CA 2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose CA 5-phosphate + NADPH. CF Manganese or Cobalt or Magnesium. CC -!- The enzyme from several eubacteria, including E.coli, forms part CC of an alternative nonmevalonate pathway for terpenoid CC biosynthesis. DR Q8UC86, DXR_AGRT5 ; Q8YP49, DXR_ANASP ; O66722, DXR_AQUAE ; DR Q9XFS9, DXR_ARATH ; Q9KA69, DXR_BACHD ; O31753, DXR_BACSU ; DR Q8A684, DXR_BACTN ; Q8G7Y7, DXR_BIFLO ; Q89KP9, DXR_BRAJA ; DR P57329, DXR_BUCAI ; Q8K9S7, DXR_BUCAP ; Q9PMV3, DXR_CAMJE ; DR Q9A709, DXR_CAUCR ; Q9PKW8, DXR_CHLMU ; Q9Z8J8, DXR_CHLPN ; DR Q8KG43, DXR_CHLTE ; O84074, DXR_CHLTR ; Q97I58, DXR_CLOAB ; DR Q8XJR1, DXR_CLOPE ; Q895K5, DXR_CLOTE ; Q8NP10, DXR_CORGL ; DR Q9RU84, DXR_DEIRA ; Q8X8Y1, DXR_ECO57 ; P45568, DXR_ECOLI ; DR Q8R622, DXR_FUSNN ; P44055, DXR_HAEIN ; Q9ZML6, DXR_HELPJ ; DR P56139, DXR_HELPY ; Q9AJD7, DXR_KITGR ; Q8F146, DXR_LEPIN ; DR Q92C37, DXR_LISIN ; Q8Y7G4, DXR_LISMO ; Q9XES0, DXR_MENPI ; DR Q9CBU3, DXR_MYCLE ; Q10798, DXR_MYCTU ; Q9JX33, DXR_NEIMA ; DR Q9K1G8, DXR_NEIMB ; P57985, DXR_PASMU ; Q9KGU6, DXR_PSEAE ; DR Q88MH4, DXR_PSEPK ; Q886N7, DXR_PSESM ; Q8XZI5, DXR_RALSO ; DR Q92LP6, DXR_RHIME ; Q8Z9A6, DXR_SALTI ; Q8ZRP3, DXR_SALTY ; DR Q8EGG9, DXR_SHEON ; Q9KYS1, DXR_STRCO ; Q8DK30, DXR_SYNEL ; DR Q9RCT1, DXR_SYNLE ; Q55663, DXR_SYNY3 ; Q9WZZ1, DXR_THEMA ; DR Q8RA28, DXR_THETN ; O83610, DXR_TREPA ; Q9KPV8, DXR_VIBCH ; DR Q87ME3, DXR_VIBPA ; Q8DBF5, DXR_VIBVU ; Q8D2G6, DXR_WIGBR ; DR Q8PML1, DXR_XANAC ; Q8PAV9, DXR_XANCP ; Q9PEI0, DXR_XYLFA ; DR Q87EH9, DXR_XYLFT ; Q8ZH62, DXR_YERPE ; Q9X5F2, DXR_ZYMMO ; // ID 1.1.1.268 DE 2-(R)-hydroxypropyl-CoM dehydrogenase. AN 2-(2-(R)-hydroxypropylthio)ethanesulfonate dehydrogenase. CA 2-(R)-hydroxypropyl-CoM + NAD(+) = 2-oxopropyl-CoM + NADH. CC -!- The enzyme is highly specific for (R)-2-hydroxyalkyl thioethers CC of CoM, in contrast to EC 1.1.1.269, which is highly specific for CC the (S)-enantiomer. CC -!- This enzyme forms component III of a four-component enzyme system CC (comprising EC 4.2.99.19 (component I), EC 1.8.1.5 (component II), CC EC 1.1.1.268 (component III) and EC 1.1.1.269 (component IV)) that CC is involved in epoxyalkane carboxylation in Xanthobacter sp. CC strain Py2. DR Q56840, HCDR_XANP2; // ID 1.1.1.269 DE 2-(S)-hydroxypropyl-CoM dehydrogenase. AN 2-(2-(S)-hydroxypropylthio)ethanesulfonate dehydrogenase. CA 2-(S)-hydroxypropyl-CoM + NAD(+) = 2-oxopropyl-CoM + NADH. CC -!- The enzyme is highly specific for (S)-2-hydroxyalkyl thioethers CC of CoM, in contrast to EC 1.1.1.268, which is highly specific for CC the (R)-enantiomer. CC -!- This enzyme forms component IV of a four-component enzyme system CC (comprising EC 4.2.99.19 (component I), EC 1.8.1.5 (component II), CC EC 1.1.1.268 (component III) and EC 1.1.1.269 (component IV)) that CC is involved in epoxyalkane carboxylation in Xanthobacter sp. CC strain Py2. DR Q56841, HCDS_XANP2; // ID 1.1.1.270 DE 3-keto-steroid reductase. AN 3-KSR. CA 4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + NADP(+) = 4-alpha- CA methyl-5-alpha-cholest-7-en-3-one + NADPH. CC -!- Also acts on 5-alpha-cholest-7-en-3-one. // ID 1.1.1.271 DE GDP-L-fucose synthase. AN GDP-fucose synthetase. AN GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase. CA GDP-L-fucose + NADP(+) = GDP-4-dehydro-6-deoxy-D-mannose + NADPH. DR P32055, FCL_ECOLI ; Q13630, FCL_HUMAN ; P23591, FCL_MOUSE ; // ID 1.1.1.272 DE (R)-2-hydroxyacid dehydrogenase. AN (R)-sulfolactate:NAD(P)(+) oxidoreductase. AN L-sulfolactate dehydrogenase. CA (S)-3-sulfolactate + NAD(P)(+) = 3-sulfopyruvate + NAD(P)H. CC -!- This dehydrogenase acts on (R)-lactate and other 2-hydroxycarboxylic CC acids with this configuration. DR Q58820, COMC_METJA; P16142, MDH_METFE ; // ID 1.1.1.273 DE Vellosimine dehydrogenase. CA 10-deoxysarpagine + NADP(+) = vellosimine + NADPH. CC -!- Also acts on related alkaloids with an endo-aldehyde group as CC vellosimine (same stereochemistry at C-16) but only slight CC activity with exo-aldehydes. CC -!- Detected in many cell suspension cultures of plants from the CC family Apocynaceae. // ID 1.1.1.274 DE 2,5-didehydrogluconate reductase. AN 2,5-diketo-D-gluconate reductase. CA 2-dehydro-D-gluconate + NADP(+) = 2,5-didehydro-D-gluconate + NADPH. CC -!- Key enzyme in the microbial production of ascorbate. CC -!- Can also reduce ethyl 2-methylacetoacetate stereoselectively to CC ethyl (2R)-methyl-(3S)-hydroxybutanoate and can also accept some CC other beta-keto esters. CC -!- The identification of a bacterial beta-keto ester reductase as a CC 2,5-didehydrogluconate reductase links two previously separate areas CC of biocatalysis, i.e., asymmetric carbonyl reduction and microbial CC vitamin C production. PR PROSITE; PDOC00061; DR P06632, DKGA_CORSP; Q8XBT6, DKGA_ECO57; Q46857, DKGA_ECOLI; DR P58744, DKGA_SALTI; Q8ZM06, DKGA_SALTY; Q8ZI40, DKGA_YERPE; DR P15339, DKGB_CORSP; Q8X7Z7, DKGB_ECO57; P30863, DKGB_ECOLI; DR Q8Z988, DKGB_SALTI; Q8ZRM7, DKGB_SALTY; Q8ZH36, DKGB_YERPE; // ID 1.1.2.1 DE Transferred entry: 1.1.99.5. // ID 1.1.2.2 DE Mannitol dehydrogenase (cytochrome). AN Polyol dehydrogenase. CA D-mannitol + ferricytochrome c = D-fructose + ferrocytochrome c. CC -!- Acts on polyols with a D-lyxo configuration, such as D-mannitol CC and D-sorbitol. // ID 1.1.2.3 DE L-lactate dehydrogenase (cytochrome). AN Lactic acid dehydrogenase. AN Cytochrome b2. AN L-lactate ferricytochrome c oxidoreductase. CA (S)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c. CF FMN; Protoheme IX. PR PROSITE; PDOC00482; PR PROSITE; PDOC00170; DR P09437, CYB2_HANAN; P00175, CYB2_YEAST; P33232, LLDD_ECOLI; DR P46454, LLDD_HAEIN; // ID 1.1.2.4 DE D-lactate dehydrogenase (cytochrome). AN Lactic acid dehydrogenase. AN D-lactate ferricytochrome c oxidoreductase. CA (R)-lactate + 2 ferricytochrome c = pyruvate + 2 ferrocytochrome c. CF FAD. DR Q12627, DLD1_KLULA; P32891, DLD1_YEAST; P39976, DLD3_YEAST; // ID 1.1.2.5 DE D-lactate dehydrogenase (cytochrome c-553). CA (R)-lactate + 2 ferricytochrome c-553 = pyruvate + 2 ferrocytochrome CA c-553. CC -!- From Desulfovibrio vulgaris. // ID 1.1.3.1 DE Transferred entry: 1.1.3.15. // ID 1.1.3.2 DE Transferred entry: 1.13.12.4. // ID 1.1.3.3 DE Malate oxidase. AN Malic oxidase. CA (S)-malate + O(2) = oxaloacetate + H(2)O(2). CF FAD. // ID 1.1.3.4 DE Glucose oxidase. AN Glucose oxyhydrase. AN Beta-D-glucose:oxygen 1-oxido-reductase. AN Glucose aerodehydrogenase. AN D-Glucose-1-oxidase. AN Glucose oxyhydrase. AN GOD. CA Beta-D-glucose + O(2) = D-glucono-1,5-lactone + H(2)O(2). CF FAD. PR PROSITE; PDOC00543; DR P13006, GOX_ASPNG ; P81156, GOX_PENAG ; Q92452, GOX_TALFL ; // ID 1.1.3.5 DE Hexose oxidase. CA Beta-D-glucose + O(2) = D-glucono-1,5-lactone + H(2)O(2). CF Copper. CC -!- Also oxidizes D-galactose, D-mannose, maltose, lactose and CC cellobiose. // ID 1.1.3.6 DE Cholesterol oxidase. AN Cholesterol-O2 oxidoreductase. CA Cholesterol + O(2) = cholest-4-en-3-one + H(2)O(2). CF FAD. PR PROSITE; PDOC00543; DR P22637, CHOD_BREST; P12676, CHOD_STRSQ; // ID 1.1.3.7 DE Aryl-alcohol oxidase. AN Veratryl alcohol oxidase. CA An aromatic primary alcohol + O(2) = an aromatic aldehyde + H(2)O(2). CC -!- Oxidizes many primary alcohols containing an aromatic ring; best CC substrates are (2-naphthyl)-methanol and 3-methoxybenzyl alcohol. // ID 1.1.3.8 DE L-gulonolactone oxidase. AN L-gulono-gamma-lactone oxidase. CA L-gulono-1,4-lactone + O(2) = L-xylo-hex-3-ulonolactone + H(2)O(2). CF FAD. CC -!- The product spontaneously isomerizes to L-ascorbate. PR PROSITE; PDOC00674; DR P58710, GGLO_MOUSE; P10867, GGLO_RAT ; Q90YK3, GGLO_SCYTO; // ID 1.1.3.9 DE Galactose oxidase. AN Beta-Galactose oxidase. CA D-galactose + O(2) = D-galacto-hexodialose + H(2)O(2). CF Copper. DR Q01745, GAOA_DACDE; // ID 1.1.3.10 DE Pyranose oxidase. AN Glucose 2-oxidase. CA D-glucose + O(2) = 2-dehydro-D-glucose + H(2)O(2). CC -!- Also oxidizes D-xylose, L-sorbose and D-glucono-1,5-lactone, which CC have the same ring conformation and configuration at C-2, C-3 and CC C-4. DR P79076, PROD_CORVE; P59097, PROD_TRAHI; // ID 1.1.3.11 DE L-sorbose oxidase. CA L-sorbose + O(2) = 5-dehydro-D-fructose + H(2)O(2). CC -!- Also acts on D-glucose, D-galactose and D-xylose, but not on CC D-fructose. CC -!- 2,6-dichloroindophenol can act as acceptor. // ID 1.1.3.12 DE Pyridoxine 4-oxidase. AN Pyridoxin 4-oxidase. CA Pyridoxine + O(2) = pyridoxal + H(2)O(2). CF FAD. CC -!- 2,6-dichloroindophenol can act as acceptor. // ID 1.1.3.13 DE Alcohol oxidase. AN Methanol oxidase. AN AOX. CA A primary alcohol + O(2) = an aldehyde + H(2)O(2). CF FAD. CC -!- Acts on lower primary alcohols and unsaturated alcohols but branched- CC chain and secondary alcohols are not attacked. PR PROSITE; PDOC00543; DR Q00922, ALOX_CANBO; P04841, ALOX_PICAN; P04842, ALOX_PICPA; // ID 1.1.3.14 DE Catechol oxidase (dimerizing). CA 4 catechol + 3 O(2) = 2 dibenzo[1,4]dioxin-2,3-dione + 6 H(2)O(2). // ID 1.1.3.15 DE (S)-2-hydroxy-acid oxidase. AN Glycolate oxidase. AN Hydroxy-acid oxidase A. AN Hydroxy-acid oxidase B. CA (S)-2-hydroxy-acid + O(2) = 2-oxo acid + H(2)O(2). CF FMN. CC -!- Exists as two major isoenzymes; the A form preferentially oxidizes CC short-chain aliphatic hydroxy acids; the B form preferentially CC oxidizes long-chain and aromatic hydroxy acids. The rat isoenzyme B CC also acts as EC 1.4.3.2. CC -!- Formerly EC 1.1.3.1. PR PROSITE; PDOC00482; DR Q9LRS0, GOX1_ARATH; Q9LRR9, GOX2_ARATH; P05414, GOX_SPIOL ; DR Q9UJM8, HAO1_HUMAN; Q9WU19, HAO1_MOUSE; Q9NYQ3, HAO2_HUMAN; DR Q9NYQ2, HAO3_MOUSE; Q07523, HAO3_RAT ; // ID 1.1.3.16 DE Ecdysone oxidase. CA Ecdysone + O(2) = 3-dehydroecdysone + H(2)O(2). CC -!- 2,6-dichloroindophenol can act as acceptor. // ID 1.1.3.17 DE Choline oxidase. CA Choline + O(2) = betaine aldehyde + H(2)O(2). CF FAD. CC -!- Also oxidizes betaine aldehyde to betaine. DR P16101, CHOX_ALCSP; // ID 1.1.3.18 DE Secondary-alcohol oxidase. CA A secondary alcohol + O(2) = a ketone + H(2)O(2). CF Iron. CC -!- Acts on secondary alcohols with five or more carbons, and polyvinyl CC alcohols with molecular mass over 300 Da. // ID 1.1.3.19 DE 4-hydroxymandelate oxidase. CA (S)-2-hydroxy-2-(4-hydroxyphenyl)acetate + O(2) = 4-hydroxybenzaldehyde + CA CO(2) + H(2)O(2). CF FAD; Manganese. // ID 1.1.3.20 DE Long-chain-alcohol oxidase. CA 2 long-chain alcohol + O(2) = 2 long-chain aldehyde + 2 H(2)O. CC -!- Oxidizes long-chain fatty alcohols; best substrate is dodecyl CC alcohol. // ID 1.1.3.21 DE Glycerol-3-phosphate oxidase. AN Alpha-glycerophosphate oxidase. CA Sn-glycerol 3-phosphate + O(2) = glycerone phosphate + H(2)O(2). CF FAD. DR O86963, GLPO_ENTCA; Q9CG65, GLPO_LACLA; Q8K666, GLPO_STRP3; DR Q8NZX0, GLPO_STRP8; P35596, GLPO_STRPN; Q99YI8, GLPO_STRPY; // ID 1.1.3.22 DE Xanthine oxidase. AN Xanthine oxidoreductase. AN Hypoxanthine oxidase. AN Hypoxanthine-xanthine oxidase. AN Schardinger enzyme. CA Xanthine + H(2)O + O(2) = urate + H(2)O(2). CF FAD; Iron-molybdenum. CC -!- Also oxidizes hypoxanthine, some other purines and pterins, and CC aldehydes (i.e. possesses the activity of EC 1.2.3.1); probably CC acts on the hydrated derivatives of these substrates. CC -!- Under some conditions the product is mainly superoxide rather than CC peroxide: R-H + H(2)O + 2 O(2) = ROH + 2 H(+) + 2 O(2)(-). CC -!- The enzyme from animal tissues can be interconverted to EC 1.1.1.204. CC that from liver exists in vivo mainly as the dehydrogenase form, but CC can be converted into the oxidase form by storage at -20C, by CC treatment with proteolytic enzymes or with organic solvents, or by CC thiol reagents such as Cu(2+), N-ethylmaleimide or 4-mercuribenzoate. CC The effect of thiol reagents can be reversed by thiols such as CC 1,4-dithioerythritol. CC -!- EC 1.1.1.204 can also be converted into EC 1.1.3.22 by EC 1.8.4.7 in CC the presence of oxidized glutathione. CC -!- The Micrococcus enzyme can use ferredoxin as acceptor. CC -!- Formerly EC 1.2.3.2. DI Xanthinuria; MIM:278300. PR PROSITE; PDOC00484; DR P80457, XDH_BOVIN ; P47990, XDH_CHICK ; P47989, XDH_HUMAN ; DR Q00519, XDH_MOUSE ; P22985, XDH_RAT ; // ID 1.1.3.23 DE Thiamine oxidase. AN Thiamine dehydrogenase. CA Thiamine + 2 O(2) = oxidized thiamine + 2 H(2)O(2). CF FAD. CC -!- The product differs from thiamine in replacement of -CH(2)-CH(2)-OH CC by -CH(2)-COOH; the two-step oxidation proceeds without the release CC of the intermediate aldehyde from the enzyme. // ID 1.1.3.24 DE L-galactonolactone oxidase. AN L-xylono-1,4-lactone oxidase. CA L-galactono-1,4-lactone + O(2) = L-ascorbate + H(2)O(2). CF FAD. CC -!- Acts on the 1,4-lactones of L-galactonic, D-altronic, L-fuconic, CC D-arabinic and D-threonic acids. CC -!- Not identical with EC 1.1.3.8 (cf. EC 1.3.2.3). // ID 1.1.3.25 DE Cellobiose oxidase. CA Cellobiose + O(2) = cellobiono-1,5-lactone + H(2)O(2). CF Flavoprotein; Heme. CC -!- Also oxidizes cellodextrins, lactose, and, more slowly, 4-beta-D- CC glucosyl-D-mannose. // ID 1.1.3.26 DE Transferred entry: EC 1.21.3.2. // ID 1.1.3.27 DE Hydroxyphytanate oxidase. CA L-2-hydroxyphytanate + O(2) = 2-oxyphytanate + H(2)O(2). // ID 1.1.3.28 DE Nucleoside oxidase. CA Inosine + O(2) = 9-riburonosylhypoxanthine + H(2)O. CC -!- Other purine and pyrimidine nucleosides (as well as CC 2'-deoxynucleosides) are substrates, but ribose and nucleotides CC are not substrates. CC -!- The overall reaction takes place in two separate steps: CC (1) 2 inosine + O(2) = 2 5'-dehydroinosine + 2 H(2)O. CC (2) 2 5'-dehydroinosine + O(2) = 2 9-riburonosylhypoxanthine + CC 2 H(2)O. CC -!- The 5'-dehydro nucleoside is being released from the enzyme to CC serve as substrate for the second reaction. CC -!- This enzyme differs from EC 1.1.3.39 as it produces water rather CC than hydrogen peroxide. // ID 1.1.3.29 DE N-acylhexosamine oxidase. CA N-acetyl-D-glucosamine + O(2) = N-acetyl-D-glucosaminate + H(2)O(2). CC -!- Also acts on N-glycolylglucosamine, N-acetylgalactosamine and, CC more slowly, on N-acetylmannosamine. // ID 1.1.3.30 DE Polyvinyl-alcohol oxidase. AN PVA oxidase. CA Polyvinyl alcohol + O(2) = oxidized polyvinyl alcohol + H(2)O(2). // ID 1.1.3.31 DE Methanol oxidase. CA Methanol + O(2) = formaldehyde + H(2)O(2). CF FAD. CC -!- Acts on some other aliphatic alcohols, more slowly. // ID 1.1.3.32 DE Transferred entry: EC 1.14.21.1. // ID 1.1.3.33 DE Transferred entry: EC 1.14.21.2. // ID 1.1.3.34 DE Transferred entry: EC 1.14.21.3. // ID 1.1.3.35 DE Transferred entry: EC 1.14.21.4. // ID 1.1.3.36 DE Transferred entry: EC 1.14.21.5. // ID 1.1.3.37 DE D-arabinono-1,4-lactone oxidase. CA D-arabinono-1,4-lactone + O(2) = D-erythro-ascorbate + H(2)O(2). CF FAD. PR PROSITE; PDOC00674; DR O93852, ALO_CANAL ; P54783, ALO_YEAST ; // ID 1.1.3.38 DE Vanillyl-alcohol oxidase. AN 4-hydroxy-2-methoxybenzyl alcohol oxidase. CA Vanillyl alcohol + O(2) = vanillin + H(2)O(2). CF FAD. CC -!- Converts a wide range of 4-hydroxybenzyl alcohols and CC 4-hydroxybenzylamines into the corresponding aldehydes. CC -!- The allyl group of 4-allylphenols is also converted into the CC -CH=CH-CH(2)OH group. DR P56216, VAOX_PENSI; // ID 1.1.3.39 DE Nucleoside oxidase (H(2)O(2)-forming). CA Adenosine + 2 O(2) = 9-riburonosyladenine + 2 H(2)O(2). CF Heme; FAD. CC -!- Other purine and pyrimidine nucleosides (as well as CC 2'-deoxynucleosides and arabinosides) are substrates, but ribose CC and nucleotides are not substrates. CC -!- The overall reaction takes place in two separate steps: CC (1) Adenosine + O(2) = 5'-dehydroadenosine + H(2)O(2). CC (2) 5'-dehydroadenosine + O(2) = 9-riburonosyladenine + H(2)O(2). CC -!- The 5'-dehydro nucleoside is being released from the enzyme to CC serve as substrate for the second reaction. CC -!- This enzyme differs from EC 1.1.3.28 as it produces hydrogen CC peroxide rather than water. // ID 1.1.3.40 DE D-mannitol oxidase. AN Mannitol oxidase. AN D-arabinitol oxidase. CA Mannitol + O(2) = mannose + H(2)O(2). CC -!- The enzyme also catalyzes the oxidation of D-arabinitol and, to a CC lesser extent, D-glucitol (sorbitol), whereas L-arabinitol is not CC a good substrate. CC -!- The enzyme from the snails Helix aspersa and Arion ater is found CC in a specialised tubular organelle that has been termed the CC mannosome. // ID 1.1.3.41 DE Xylitol oxidase. CA Xylitol + O(2) = xylose + H(2)O(2). CF FAD. CC -!- The enzyme also oxidizes D-sorbitol. PR PROSITE; PDOC00674; DR Q9ZBU1, XYOA_STRCO; Q9KX73, XYOA_STRSQ; // ID 1.1.4.1 DE Vitamin-K-epoxide reductase (warfarin-sensitive). AN Vitamin K1 epoxide reductase. AN Phylloquinone epoxide reductase. CA 2-methyl-3-phytyl-1,4-naphthoquinone + oxidized dithiothreitol + H(2)O = CA 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl-1,4-naphthoquinone + CA 1,4-dithiothreitol. CC -!- In the reverse reaction, vitamin K 2,3-epoxide is reduced to vitamin CC K and possibly to vitamin K hydroquinone by 1,4-dithioerythritol, CC which is oxidized to a disulfide; some other dithiols and butane-4- CC thiol can also act. CC -!- Inhibited strongly by warfarin (cf. EC 1.1.4.2). // ID 1.1.4.2 DE Vitamin-K-epoxide reductase (warfarin-insensitive). AN Vitamin K 2,3-epoxide reductase. CA 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone + oxidized CA dithiothreitol + H(2)O = 2,3-epoxy-2,3-dihydro-2-methyl-3-phytyl- CA 1,4-naphthoquinone + 1,4-dithiothreitol. CC -!- In the reverse reaction, vitamin K 2,3-epoxide is reduced to CC 3-hydroxy- (and 2-hydroxy-) vitamin K by 1,4-dithioerythritol, which CC is oxidized to a disulfide. CC -!- Not inhibited by warfarin (cf. EC 1.1.4.1). // ID 1.1.5.1 DE Transferred entry: 1.1.99.18. // ID 1.1.99.1 DE Choline dehydrogenase. AN Choline oxidase. CA Choline + acceptor = betaine aldehyde + reduced acceptor. CF PQQ. PR PROSITE; PDOC00543; DR P17444, BETA_ECOLI; P54223, BETA_RHIME; // ID 1.1.99.2 DE 2-hydroxyglutarate dehydrogenase. CA (S)-2-hydroxyglutarate + acceptor = 2-oxoglutarate + reduced acceptor. // ID 1.1.99.3 DE Gluconate 2-dehydrogenase (acceptor). CA D-gluconate + acceptor = 2-dehydro-D-gluconate + reduced acceptor. CF FAD. // ID 1.1.99.4 DE Dehydrogluconate dehydrogenase. AN Ketoglutonate dehydrogenase. CA 2-dehydro-D-gluconate + acceptor = 2,5-didehydro-D-gluconate + reduced CA acceptor. CF Flavoprotein. // ID 1.1.99.5 DE Glycerol-3-phosphate dehydrogenase. CA Sn-glycerol 3-phosphate + acceptor = glycerone phosphate + reduced CA acceptor. CF Flavin. CC -!- Formerly EC 1.1.2.1. PR PROSITE; PDOC00740; DR P13032, GLPA_ECOLI; P43799, GLPA_HAEIN; P13033, GLPB_ECOLI; DR P43800, GLPB_HAEIN; P18158, GLPD_BACSU; P13035, GLPD_ECOLI; DR P53435, GLPD_MYCLE; Q10502, GLPD_MYCTU; P52111, GLPD_PSEAE; DR O83004, GLPD_PSETO; P74257, GLPD_SYNY3; P90795, GPDM_CAEEL; DR P43304, GPDM_HUMAN; Q64521, GPDM_MOUSE; P35571, GPDM_RAT ; DR O14400, GPDM_SCHPO; P32191, GPDM_YEAST; // ID 1.1.99.6 DE D-2-hydroxy-acid dehydrogenase. CA (R)-lactate + acceptor = pyruvate + reduced acceptor. CF FAD; Zinc. CC -!- Acts on a variety of (R)-2-hydroxy acids. // ID 1.1.99.7 DE Lactate--malate transhydrogenase. CA (S)-lactate + oxaloacetate = pyruvate + malate. CC -!- Catalyzes hydrogen transfer from C(3) or C(4) (S)-2-hydroxy acids to CC 2-oxo acids. CC -!- Contains tightly bound nicotinamide nucleotide in its active centre. CC this prosthetic group cannot be removed without denaturation of the CC protein. // ID 1.1.99.8 DE Alcohol dehydrogenase (acceptor). AN Methanol dehydrogenase. CA A primary alcohol + acceptor = an aldehyde + reduced acceptor. CF PQQ. CC -!- Acts on a wide range of primary alcohols, including methanol. PR PROSITE; PDOC00375; DR P18278, DHET_ACEAC; Q44002, DHET_ACEEU; P28036, DHET_ACEPO; DR O05542, DHET_GLUOX; P16027, DHM1_METEX; P38539, DHM1_METME; DR P15279, DHM1_METOR; P12293, DHM1_PARDE; P14775, DHM2_METEX; DR P38540, DHM2_METME; P29898, DHM2_PARDE; // ID 1.1.99.9 DE Pyridoxine 5-dehydrogenase. AN Pyridoxol-5-dehydrogenase. CA Pyridoxine + acceptor = isopyridoxal + reduced acceptor. CF FAD. // ID 1.1.99.10 DE Glucose dehydrogenase (acceptor). AN Glucose dehydrogenase (Aspergillus). CA D-glucose + acceptor = D-glucono-1,5-lactone + reduced acceptor. CF FAD. CC -!- 2,6-dichloroindophenol can act as acceptor. PR PROSITE; PDOC00543; DR P18173, DHGL_DROME; P18172, DHGL_DROPS; // ID 1.1.99.11 DE Fructose 5-dehydrogenase. AN D-Fructose dehydrogenase. CA D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor. CC -!- 2,6-dichloroindophenol can act as acceptor. // ID 1.1.99.12 DE Sorbose dehydrogenase. CA L-sorbose + acceptor = 5-dehydro-D-fructose + reduced acceptor. CC -!- 2,6-dichloroindophenol can act as acceptor. // ID 1.1.99.13 DE Glucoside 3-dehydrogenase. AN D-aldohexopyranoside dehydrogenase. CA Sucrose + acceptor = 3-dehydro-alpha-D-glucosyl-beta-D-fructofuranoside + CA reduced acceptor. CF FAD. CC -!- The enzyme acts on D-glucose, D-galactose, D-glucosides and CC D-galactosides, but D-glucosides react more rapidly than CC D-galactosides. // ID 1.1.99.14 DE Glycolate dehydrogenase. AN Glycolate oxidoreductase. AN Glycolic acid dehydrogenase. CA Glycolate + acceptor = glyoxylate + reduced acceptor. CC -!- Also acts on (R)-lactate. CC -!- 2,6-dichloroindophenol and phenazine methosulfate can act as CC acceptors. // ID 1.1.99.15 DE Transferred entry: 1.7.99.5. // ID 1.1.99.16 DE Malate dehydrogenase (acceptor). CA (S)-malate + acceptor = oxaloacetate + reduced acceptor. CF FAD. DR Q9HYF4, MQO1_PSEAE; Q99RR2, MQO1_STAAM; Q9HVF1, MQO2_PSEAE; DR Q99R30, MQO2_STAAM; Q8NUM4, MQO2_STAAW; Q8UH73, MQO_AGRT5 ; DR Q9Z9Q7, MQO_BACHD ; P56954, MQO_CAMJE ; O69282, MQO_CORGL ; DR Q8XE45, MQO_ECO57 ; P33940, MQO_ECOLI ; Q9ZMY5, MQO_HELPJ ; DR O24913, MQO_HELPY ; O32719, MQO_KLEPN ; O05807, MQO_MYCTU ; DR Q9JWK3, MQO_NEIMA ; Q9JXD7, MQO_NEIMB ; Q8XRL7, MQO_RALSO ; DR Q8D1V2, MQO_WIGBR ; Q9PET6, MQO_XYLFA ; Q87AS0, MQO_XYLFT ; // ID 1.1.99.17 DE Glucose dehydrogenase (pyrroloquinoline-quinone). AN Quinoprotein glucose dehydrogenase. CA D-glucose + acceptor = D-glucono-1,5-lactone + reduced acceptor. CF PQQ. CC -!- Different from EC 1.1.99.10. PR PROSITE; PDOC00375; DR P05465, DHGA_ACICA; P13650, DHGB_ACICA; P15877, DHG_ECOLI ; DR P27175, DHG_GLUOX ; // ID 1.1.99.18 DE Cellobiose dehydrogenase (acceptor). AN Cellobiose dehydrogenase. AN Cellobiose dehydrogenase (quinone). AN Cellobiose-quinone oxidoreductase. CA Cellobiose + acceptor = cellobiono-1,5-lactone + reduced acceptor. CF FAD; Heme. CC -!- 2,6-Dichloroindophenol can act as acceptor. CC -!- Also acts, more slowly, on cello-oligosaccharides, lactose and CC D-glucosyl-1,4-beta-D-mannose. CC -!- Includes EC 1.1.5.1, which is now known to be a proteolytic product CC of this enzyme. DR Q01738, CDH_PHACH ; // ID 1.1.99.19 DE Uracil dehydrogenase. AN Uracil oxidase. CA Uracil + acceptor = barbiturate + reduced acceptor. CC -!- Also oxidizes thymine. CC -!- Acts on the hydrated derivative of the substrate. CC -!- Formerly EC 1.2.99.1. // ID 1.1.99.20 DE Alkan-1-ol dehydrogenase (acceptor). AN Polyethylene glycol dehydrogenase. CA Primary alcohol + acceptor = aldehyde + reduced acceptor. CF PQQ. CC -!- Acts on C(3)-C(16) linear-chain saturated primary alcohols, C(4)-C(7) CC aldehydes, and non-ionic surfactants containing polyethylene glycol CC residues such as between 40 and 60, but not on methanol and only very CC slowly on ethanol. CC -!- 2,6-dichloroindophenol can act as acceptor. // ID 1.1.99.21 DE D-sorbitol dehydrogenase. CA D-sorbitol + acceptor = L-sorbose + reduced acceptor. CF FAD. // ID 1.1.99.22 DE Glycerol dehydrogenase (acceptor). CA Glycerol + acceptor = glycerone + reduced acceptor. CF PQQ. CC -!- Also acts, more slowly, on a number of other polyols including CC D-sorbitol, D-arabinitol, meso-erythritol, adonitol and propylene CC glycol. // ID 1.1.99.23 DE Polyvinyl-alcohol dehydrogenase (acceptor). AN PVA dehydrogenase. CA Polyvinyl alcohol + acceptor = oxidized polyvinyl alcohol + reduced CA acceptor. CF PQQ. CC -!- Phenazine methosulfate and 2,6-dichloroindophenol can act as CC acceptors. CC -!- Also acts, more slowly, on 2-hexanol and some other secondary CC alcohols (cf. EC 1.1.99.8 and EC 1.1.99.20). // ID 1.1.99.24 DE Hydroxyacid-oxoacid transhydrogenase. CA (S)-3-hydroxybutanoate + 2-oxoglutarate = acetoacetate + CA (R)-2-hydroxyglutarate. CC -!- 4-hydroxybutanoate and (R)-2-hydroxyglutarate can also act as CC donors; 4-oxobutanoate can also act as acceptor. // ID 1.1.99.25 DE Quinate dehydrogenase (pyrroloquinoline-quinone). AN NAD(P)-independent quinate dehydrogenase. CA Quinate + pyrroloquinoline-quinone = 5-dehydroquinate + reduced CA pyrroloquinoline-quinone. DR Q59086, QUIA_ACICA; Q9XD78, QUIA_XANCJ; // ID 1.1.99.26 DE 3-hydroxycyclohexanone dehydrogenase. CA 3-hydroxycyclohexanone + acceptor = cyclohexane-1,3-dione + CA reduced acceptor. CC -!- 2,6-dichloroindophenol and methylene blue can act as acceptors. // ID 1.1.99.27 DE (R)-pantolactone dehydrogenase (flavin). AN 2-dehydropantolactone reductase (flavin). AN 2-dehydropantoyl-lactone reductase (flavin). AN (R)-pantoyllactone dehydrogenase (flavin). CA (R)-pantolactone + acceptor = 2-dehydropantolactone + reduced acceptor. CF FMN. CC -!- High specificity for (R)-pantolactone. CC -!- Phenazine methosulfate (PMS) can act as acceptor. CC -!- The enzyme has been studied in Nocardia asteroides and shown to CC be membrane-bound and induced by 1,2-propanediol. // ID 1.1.99.28 DE Glucose--fructose oxidoreductase. CA D-glucose + D-fructose = D-gluconolactone + D-glucitol. CC -!- D-mannose, D-xylose, D-galactose, 2-deoxy-D-erythro-hexose and CC L-arabinose will function as aldose substrates, but with low CC affinities. CC -!- The ketose substrate must be in the open-chain form. CC -!- The apparent affinity for fructose is low, because little of the CC fructose substrate is in the open-chain form. CC -!- Xylulose and glycerone (dihydroxyacetone) will replace fructose, but CC they are poor substrates. CC -!- The enzyme from Z.mobilis contains tightly bound NADP. DR Q07982, GFO_ZYMMO ; // ID 1.2.1.1 DE Formaldehyde dehydrogenase (glutathione). AN Formic dehydrogenase. AN NAD-linked formaldehyde dehydrogenase. AN Formaldehyde dehydrogenase. CA Formaldehyde + glutathione + NAD(+) = S-formylglutathione + NADH. CC -!- Some 2-oxoaldehydes are also oxidized. CC -!- In the reverse direction, NADPH can replace NADH. CC -!- Also specifically reduces S-nitrosylglutathione. PR PROSITE; PDOC00058; DR P25437, ADH3_ECOLI; P44557, ADH3_HAEIN; P39450, ADH3_PASPI; DR P73138, ADH3_SYNY3; P81600, ADHH_GADMO; P72324, ADHI_RHOSH; DR P81601, ADHL_GADMO; Q96533, ADHX_ARATH; Q17335, ADHX_CAEEL; DR P46415, ADHX_DROME; P19854, ADHX_HORSE; P11766, ADHX_HUMAN; DR P93629, ADHX_MAIZE; P28474, ADHX_MOUSE; P80360, ADHX_MYXGL; DR P81431, ADHX_OCTVU; P93436, ADHX_ORYSA; P80572, ADHX_PEA ; DR O19053, ADHX_RABIT; P12711, ADHX_RAT ; P79896, ADHX_SPAAU; DR P80467, ADHX_UROHA; Q06099, FADH_CANMA; P47734, FADH_METMR; DR P45382, FADH_PARDE; O74685, FADH_PICPA; P32771, FADH_YEAST; DR P78870, FAH1_SCHPO; O74540, FAH2_SCHPO; // ID 1.2.1.2 DE Formate dehydrogenase. CA Formate + NAD(+) = CO(2) + NADH. CC -!- Together with EC 1.12.1.2, forms a system previously known as CC formate hydrogenlyase. PR PROSITE; PDOC00063; PR PROSITE; PDOC00392; DR P06131, FDHA_METFO; Q60314, FDHA_METJA; P06130, FDHB_METFO; DR Q60316, FDHB_METJA; Q50570, FDHB_METTF; P07658, FDHF_ECOLI; DR Q9S7E4, FDH_ARATH ; Q03134, FDH_EMENI ; Q9ZRI8, FDH_HORVU ; DR Q07103, FDH_NEUCR ; Q9SXP2, FDH_ORYSA ; P33677, FDH_PICAN ; DR P33160, FDH_PSESR ; Q07511, FDH_SOLTU ; P24183, FDNG_ECOLI; DR P32176, FDOG_ECOLI; P46448, FDXG_HAEIN; // ID 1.2.1.3 DE Aldehyde dehydrogenase (NAD+). CA An aldehyde + NAD(+) + H(2)O = an acid + NADH. CC -!- Wide specificity, including oxidation of D-glucuronolactone to CC D-glucarate. CC -!- Formerly EC 1.1.1.70. DI Acute alcohol intolerance; MIM:100650. PR PROSITE; PDOC00068; DR P83402, D7A1_ACASC; Q9SYG7, D7A1_ARATH; Q41247, D7A1_BRANA; DR P46562, D7A1_CAEEL; P83401, D7A1_DICDI; P49419, D7A1_HUMAN; DR Q9ZPB7, D7A1_MALDO; Q9DBF1, D7A1_MOUSE; P25795, D7A1_PEA ; DR Q64057, D7A1_RAT ; P42236, DHA1_BACSU; P48644, DHA1_BOVIN; DR P27463, DHA1_CHICK; P30840, DHA1_ENTHI; P15437, DHA1_HORSE; DR P00352, DHA1_HUMAN; P24549, DHA1_MOUSE; P51647, DHA1_RAT ; DR P51977, DHA1_SHEEP; P46368, DHA2_ALCEU; P45959, DHA2_BACST; DR P39616, DHA2_BACSU; O94788, DHA2_HUMAN; Q62148, DHA2_MOUSE; DR Q63639, DHA2_RAT ; P46329, DHA3_BACSU; P51648, DHA4_HUMAN; DR P47740, DHA4_MOUSE; P30839, DHA4_RAT ; P46367, DHA4_YEAST; DR P52476, DHA5_BOVIN; P30837, DHA5_HUMAN; P40047, DHA5_YEAST; DR P54115, DHA6_YEAST; Q94688, DHA9_POLMI; P13601, DHAC_RAT ; DR Q28399, DHAE_ELEED; Q29490, DHAE_MACPR; Q56694, DHAF_VIBHA; DR P49189, DHAG_HUMAN; Q29228, DHAG_PIG ; O74187, DHAL_AGABI; DR P42041, DHAL_ALTAL; P41751, DHAL_ASPNG; P42329, DHAL_BACST; DR P40108, DHAL_CLAHE; Q9RYG9, DHAL_DEIRA; P23883, DHAL_ECOLI; DR P08157, DHAL_EMENI; Q27640, DHAL_ENCBU; O53743, DHAL_MYCTU; DR P12693, DHAL_PSEOL; P33008, DHAL_PSESP; Q9ZA11, DHAL_RHORU; DR Q9RJZ6, DHAL_STRCO; P23240, DHAL_VIBCH; P20000, DHAM_BOVIN; DR P12762, DHAM_HORSE; P05091, DHAM_HUMAN; Q25417, DHAM_LEITA; DR P81178, DHAM_MESAU; P47738, DHAM_MOUSE; P11884, DHAM_RAT ; DR Q29491, DHAN_MACPR; O93344, DHAS_CHICK; P22281, DHAX_YEAST; DR P32872, DHAY_YEAST; P46369, THCA_RHOER; // ID 1.2.1.4 DE Aldehyde dehydrogenase (NADP+). CA An aldehyde + NADP(+) + H(2)O = an acid + NADPH. // ID 1.2.1.5 DE Aldehyde dehydrogenase (NAD(P)+). CA An aldehyde + NAD(P)(+) + H(2)O = an acid + NAD(P)H. PR PROSITE; PDOC00068; DR P47771, DHA2_YEAST; P54114, DHA3_YEAST; P47895, DHA6_HUMAN; DR P43353, DHA7_HUMAN; P48448, DHA8_HUMAN; P30907, DHAP_BOVIN; DR P30838, DHAP_HUMAN; P47739, DHAP_MOUSE; P11883, DHAP_RAT ; // ID 1.2.1.6 DE Deleted entry. // ID 1.2.1.7 DE Benzaldehyde dehydrogenase (NADP+). CA Benzaldehyde + NADP(+) + H(2)O = benzoate + NADPH. // ID 1.2.1.8 DE Betaine-aldehyde dehydrogenase. CA Betaine aldehyde + NAD(+) + H(2)O = betaine + NADH. PR PROSITE; PDOC00068; DR O04895, DHAB_AMAHP; Q9S795, DHAB_ARATH; P42757, DHAB_ATRHO; DR P71016, DHAB_BACSU; P28237, DHAB_BETVU; P17445, DHAB_ECOLI; DR P56533, DHAB_GADCA; Q40024, DHAB_HORVU; O24174, DHAB_ORYSA; DR P54222, DHAB_RHIME; O59808, DHAB_SCHPO; P17202, DHAB_SPIOL; DR P77674, YDCW_ECOLI; // ID 1.2.1.9 DE Glyceraldehyde-3-phosphate dehydrogenase (NADP+). AN Triosephosphate dehydrogenase. CA D-glyceraldehyde 3-phosphate + NADP(+) + H(2)O = 3-phospho-D-glycerate + CA NADPH. PR PROSITE; PDOC00068; DR Q43272, GAPN_MAIZE; P93338, GAPN_NICPL; P81406, GAPN_PEA ; DR Q59931, GAPN_STRMU; // ID 1.2.1.10 DE Acetaldehyde dehydrogenase (acetylating). CA Acetaldehyde + CoA + NAD(+) = acetyl-CoA + NADH. CC -!- Also acts, more slowly, on glycolaldehyde, propanal and butanal. PR PROSITE; PDOC00059; DR Q24803, ADH2_ENTHI; P33744, ADHE_CLOAB; P17547, ADHE_ECOLI; DR P77580, MHPF_ECOLI; // ID 1.2.1.11 DE Aspartate-semialdehyde dehydrogenase. AN Aspartic semialdehyde dehydrogenase. AN L-aspartate-beta-semialdehyde dehydrogenase. AN ASA dehydrogenase. CA L-aspartate-4-semialdehyde + phosphate + NADP(+) = L-4-aspartyl CA phosphate + NADPH. PR PROSITE; PDOC00847; DR Q44151, DHAS_ACTPL; O67716, DHAS_AQUAE; O28766, DHAS_ARCFU; DR P96198, DHAS_AZOVI; Q04797, DHAS_BACSU; P41399, DHAS_BORPE; DR P57523, DHAS_BUCAI; Q8K9B5, DHAS_BUCAP; Q59291, DHAS_CAMJE; DR P41400, DHAS_CORFL; P26511, DHAS_CORGL; P00353, DHAS_ECOLI; DR P44801, DHAS_HAEIN; Q9ZK28, DHAS_HELPJ; O25801, DHAS_HELPY; DR O31219, DHAS_LEGPN; P41394, DHAS_LEPIN; Q57658, DHAS_METJA; DR O26890, DHAS_METTH; P47730, DHAS_MYCBO; P41404, DHAS_MYCSM; DR P97049, DHAS_MYCTU; P57008, DHAS_NEIMA; P30903, DHAS_NEIMB; DR P49420, DHAS_PROMA; Q51344, DHAS_PSEAE; Q9ZDL2, DHAS_RICPR; DR O30706, DHAS_SALTY; P78780, DHAS_SCHPO; Q56732, DHAS_SHESP; DR Q56734, DHAS_SHEVI; Q53612, DHAS_STRAK; P10539, DHAS_STRMU; DR Q55512, DHAS_SYNY3; P23247, DHAS_VIBCH; Q60080, DHAS_VIBMI; DR P13663, DHAS_YEAST; // ID 1.2.1.12 DE Glyceraldehyde 3-phosphate dehydrogenase (phosphorylating). AN NAD-dependent glyceraldehyde-3-phosphate dehydrogenase. AN Triosephosphate dehydrogenase. AN GAPDH. CA D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D- CA glyceroyl phosphate + NADH. CC -!- Also acts very slowly on D-glyceraldehyde and some other aldehydes. CC -!- Thiols can replace phosphate. PR PROSITE; PDOC00069; DR P32635, G3P1_AGABI; P80506, G3P1_ANASP; P34916, G3P1_ANAVA; DR P09124, G3P1_BACSU; P04970, G3P1_CAEEL; P07486, G3P1_DROME; DR P06977, G3P1_ECOLI; P24751, G3P1_ESCVU; P53429, G3P1_GIALA; DR O16027, G3P1_GLORO; P00354, G3P1_HUMAN; P80534, G3P1_JACOR; DR Q9C136, G3P1_RHIRA; P24165, G3P1_SALTY; P78958, G3P1_SCHPO; DR P49433, G3P1_SYNY3; P17729, G3P1_TRIKO; P00360, G3P1_YEAST; DR P32636, G3P2_AGABI; P58554, G3P2_ANASP; P34917, G3P2_ANAVA; DR P32809, G3P2_CAEBR; P17329, G3P2_CAEEL; P07487, G3P2_DROME; DR O44104, G3P2_DROPS; O44105, G3P2_DROSU; P04406, G3P2_HUMAN; DR P80447, G3P2_JACOR; Q01077, G3P2_KLUMA; Q96UF2, G3P2_RHIRA; DR P29272, G3P2_RHOSH; O43026, G3P2_SCHPO; P17730, G3P2_TRIKO; DR P00358, G3P2_YEAST; P58559, G3P3_ANASP; P34918, G3P3_ANAVA; DR P32810, G3P3_CAEBR; P17330, G3P3_CAEEL; P58072, G3P3_ECO57; DR P33898, G3P3_ECOLI; Q96UF1, G3P3_RHIRA; P00359, G3P3_YEAST; DR P17331, G3P4_CAEEL; P50321, G3PC_ALCEU; P25861, G3PC_ANTMA; DR P25858, G3PC_ARATH; P49644, G3PC_CHLRE; P34920, G3PC_CHOCR; DR Q42671, G3PC_CRAPL; P34921, G3PC_DIACA; Q39769, G3PC_GINBI; DR P54270, G3PC_GRAVE; P08477, G3PC_HORVU; Q01558, G3PC_LEIME; DR P26518, G3PC_MAGLI; P08735, G3PC_MAIZE; P17878, G3PC_MESCR; DR Q42977, G3PC_ORYSA; P34922, G3PC_PEA ; P26519, G3PC_PETCR; DR P26520, G3PC_PETHY; P34923, G3PC_PHYPA; P34924, G3PC_PINSY; DR P26521, G3PC_RANAC; P04796, G3PC_SINAL; Q41595, G3PC_TAXBA; DR P09094, G3PC_TOBAC; P10097, G3PC_TRYBB; Q09054, G3PD_MAIZE; DR Q43247, G3PE_MAIZE; O96423, G3PG_CRIFA; Q27890, G3PG_LEIME; DR P22512, G3PG_TRYBB; P22513, G3PG_TRYCR; P50322, G3PP_ALCEU; DR O14556, G3PT_HUMAN; Q64467, G3PT_MOUSE; P26517, G3PX_HORVU; DR Q9HFX1, G3P_AJECA ; P55071, G3P_AMAMU ; O67161, G3P_AQUAE ; DR Q12552, G3P_ASPNG ; Q9HGY7, G3P_ASPOR ; P34783, G3P_ATRNU ; DR P15115, G3P_BACCO ; Q59199, G3P_BACFR ; P23722, G3P_BACME ; DR P00362, G3P_BACST ; Q00301, G3P_BOLED ; P46795, G3P_BORBU ; DR P46796, G3P_BORHE ; P10096, G3P_BOVIN ; P48812, G3P_BRUMA ; DR P57384, G3P_BUCAI ; Q07234, G3P_BUCAP ; Q92211, G3P_CANAL ; DR Q28259, G3P_CANFA ; P70685, G3P_CAVPO ; P00356, G3P_CHICK ; DR Q9PJN6, G3P_CHLMU ; Q9Z7T0, G3P_CHLPN ; Q46450, G3P_CHLTR ; DR P24748, G3P_CITFR ; Q00584, G3P_CLAPU ; O52631, G3P_CLOAB ; DR Q59309, G3P_CLOPA ; P29497, G3P_COCHE ; Q8J1H3, G3P_COCPO ; DR P35143, G3P_COLGL ; O57479, G3P_COLLI ; P54117, G3P_COLLN ; DR Q01651, G3P_CORGL ; Q05025, G3P_COTJA ; P17244, G3P_CRIGR ; DR Q9Y796, G3P_CRYCU ; Q9Y8E9, G3P_CRYNE ; P19089, G3P_CRYPA ; DR P28844, G3P_CURLU ; Q94469, G3P_DICDI ; Q01597, G3P_DROHY ; DR Q27652, G3P_ECHMU ; P20445, G3P_EMENI ; P24163, G3P_ENTAE ; DR Q00640, G3P_ERYGR ; P24749, G3P_ESCBL ; P24746, G3P_ESCFE ; DR P24750, G3P_ESCHE ; P44304, G3P_HAEIN ; Q9ZKT0, G3P_HELPJ ; DR P55971, G3P_HELPY ; P00357, G3P_HOMAM ; P24164, G3P_KLEPN ; DR P17819, G3P_KLULA ; O32755, G3P_LACDE ; P55070, G3P_LACDT ; DR P52987, G3P_LACLA ; Q9UR38, G3P_LENED ; Q92243, G3P_LYOSH ; DR Q9N655, G3P_MASBA ; O57672, G3P_MELGA ; P51640, G3P_MESAU ; DR P53430, G3P_MONAN ; P16858, G3P_MOUSE ; P94915, G3P_MYCAV ; DR P47543, G3P_MYCGE ; P46713, G3P_MYCLE ; P75358, G3P_MYCPN ; DR O06822, G3P_MYCTU ; P54118, G3P_NEUCR ; Q8TFJ2, G3P_OMPOL ; DR O42259, G3P_ONCMY ; O01360, G3P_ONCVO ; P56649, G3P_PALVE ; DR Q8X1X3, G3P_PARBR ; Q01982, G3P_PHACH ; Q9P8C0, G3P_PHANO ; DR O13507, G3P_PHARH ; P26988, G3P_PHYIN ; O59841, G3P_PICAN ; DR Q9UVC0, G3P_PICCI ; Q92263, G3P_PICPA ; P00355, G3P_PIG ; DR Q9UW96, G3P_PLESA ; P32637, G3P_PODAN ; P27726, G3P_PSEAE ; DR P46406, G3P_RABIT ; P52694, G3P_RALSO ; P04797, G3P_RAT ; DR Q8NK47, G3P_RHIMI ; P32638, G3P_SCHCO ; P20287, G3P_SCHMA ; DR Q96US8, G3P_SCLSC ; P24166, G3P_SERMA ; P24753, G3P_SEROD ; DR Q28554, G3P_SHEEP ; Q8WZN0, G3P_SORMA ; P54226, G3P_STRAE ; DR Q59800, G3P_STRAU ; Q9Z518, G3P_STRCO ; Q59906, G3P_STREQ ; DR Q8K8M9, G3P_STRP3 ; P50467, G3P_STRPY ; P00361, G3P_THEAQ ; DR P17721, G3P_THEMA ; O83816, G3P_TREPA ; P87197, G3P_TRIHA ; DR P09317, G3P_USTMA ; P51009, G3P_XANFL ; P51469, G3P_XENLA ; DR P08439, G3P_ZYGRO ; P09316, G3P_ZYMMO ; // ID 1.2.1.13 DE Glyceraldehyde 3-phosphate dehydrogenase (NADP+) (phosphorylating). AN NADP-dependent glyceraldehyde-3-phosphate dehydrogenase. AN Triosephosphate dehydrogenase (NADP+). CA D-glyceraldehyde 3-phosphate + phosphate + NADP(+) = 3-phospho-D- CA glyceroyl phosphate + NADPH. DR P25856, G3PA_ARATH; P50362, G3PA_CHLRE; P34919, G3PA_CHOCR; DR P30724, G3PA_GRAVE; P09315, G3PA_MAIZE; P12858, G3PA_PEA ; DR P09672, G3PA_SINAL; P19866, G3PA_SPIOL; P09043, G3PA_TOBAC; DR P25857, G3PB_ARATH; P12859, G3PB_PEA ; P12860, G3PB_SPIOL; DR P09044, G3PB_TOBAC; // ID 1.2.1.14 DE Transferred entry: 1.1.1.205. // ID 1.2.1.15 DE Malonate-semialdehyde dehydrogenase. CA 3-oxopropanoate + NAD(P)(+) + H(2)O = malonate + NAD(P)H. // ID 1.2.1.16 DE Succinate-semialdehyde dehydrogenase (NAD(P)+). CA Succinate semialdehyde + NAD(P)(+) + H(2)O = succinate + NAD(P)H. DI 4-hydroxybutyricaciduria; MIM:271980. PR PROSITE; PDOC00068; DR O32507, GABD_DEIRA; P25526, GABD_ECOLI; P55653, GABD_RHISN; DR Q55585, GABD_SYNY3; P38947, SUCD_CLOKL; P38067, UGA2_YEAST; // ID 1.2.1.17 DE Glyoxylate dehydrogenase (acylating). CA Glyoxylate + CoA + NADP(+) = oxalyl-CoA + NADPH. // ID 1.2.1.18 DE Malonate-semialdehyde dehydrogenase (acetylating). CA 3-oxopropanoate + CoA + NAD(P)(+) = acetyl-CoA + CO(2) + NAD(P)H. // ID 1.2.1.19 DE Aminobutyraldehyde dehydrogenase. AN Gamma-guanidinobutyraldehyde dehydrogenase. CA 4-aminobutanal + NAD(+) + H(2)O = 4-aminobutanoate + NADH. CC -!- The plant enzyme also acts on 4-guanidinobutanal. PR PROSITE; PDOC00068; DR P49189, DHAG_HUMAN; Q29228, DHAG_PIG ; // ID 1.2.1.20 DE Glutarate-semialdehyde dehydrogenase. CA Glutarate semialdehyde + NAD(+) + H(2)O = glutarate + NADH. // ID 1.2.1.21 DE Glycolaldehyde dehydrogenase. CA Glycolaldehyde + NAD(+) + H(2)O = glycolate + NADH. // ID 1.2.1.22 DE Lactaldehyde dehydrogenase. CA (S)-lactaldehyde + NAD(+) + H(2)O = (S)-lactate + NADH. PR PROSITE; PDOC00068; DR P25553, ALDA_ECOLI; P37685, ALDB_ECOLI; // ID 1.2.1.23 DE 2-oxoaldehyde dehydrogenase (NAD+). AN Alpha-ketoaldehyde dehydrogenase. AN Methylglyoxal dehydrogenase. CA A 2-oxoaldehyde + NAD(+) + H(2)O = a 2-oxo acid + NADH. CC -!- Not identical with EC 1.2.1.49. // ID 1.2.1.24 DE Succinate-semialdehyde dehydrogenase. CA Succinate semialdehyde + NAD(+) + H(2)O = succinate + NADH. DI 4-hydroxybutyricaciduria; MIM:271980. PR PROSITE; PDOC00068; DR P51649, SSDH_HUMAN; P51650, SSDH_RAT ; // ID 1.2.1.25 DE 2-oxoisovalerate dehydrogenase (acylating). CA 3-methyl-2-oxobutanoate + CoA + NAD(+) = 2-methylpropanoyl-CoA + CO(2) + CA NADH. CC -!- Also acts on (S)-3-methyl-2-oxopentanoate and 4-methyl-2- CC oxopentanoate. // ID 1.2.1.26 DE 2,5-dioxovalerate dehydrogenase. CA 2,5-dioxopentanoate + NADP(+) + H(2)O = 2-oxoglutarate + NADPH. // ID 1.2.1.27 DE Methylmalonate-semialdehyde dehydrogenase (acylating). CA 2-methyl-3-oxopropanoate + CoA + NAD(+) = propanoyl-CoA + CO(2) + NADH. CC -!- Also converts propanal to propanoyl-CoA. PR PROSITE; PDOC00068; DR P42412, MMSA_BACSU; Q07536, MMSA_BOVIN; P52713, MMSA_CAEEL; DR Q02252, MMSA_HUMAN; P28810, MMSA_PSEAE; Q02253, MMSA_RAT ; // ID 1.2.1.28 DE Benzaldehyde dehydrogenase (NAD+). CA Benzaldehyde + NAD(+) + H(2)O = benzoate + NADH. PR PROSITE; PDOC00068; DR P46365, XYC1_ACIGB; P46366, XYC2_ACIGB; P43503, XYLC_PSEPU; // ID 1.2.1.29 DE Aryl-aldehyde dehydrogenase. CA An aromatic aldehyde + NAD(+) + H(2)O = an aromatic acid + NADH. CC -!- Oxidizes a number of aromatic aldehydes, but not aliphatic aldehydes. // ID 1.2.1.30 DE Aryl-aldehyde dehydrogenase (NADP+). CA An aromatic aldehyde + NADP(+) + AMP + diphosphate + H(2)O = an aromatic CA acid + NADPH + ATP. // ID 1.2.1.31 DE Aminoadipate-semialdehyde dehydrogenase. AN Alpha-aminoadipate reductase. CA L-2-aminoadipate 6-semialdehyde + NADP(+) + H(2)O = L-2-aminoadipate + CA NADPH. PR PROSITE; PDOC00427; DR Q12572, LYS2_CANAL; P40976, LYS2_SCHPO; P07702, LYS2_YEAST; DR P50113, LYS5_YEAST; // ID 1.2.1.32 DE Aminomuconate-semialdehyde dehydrogenase. CA 2-aminomuconate 6-semialdehyde + NAD(+) + H(2)O = 2-aminomuconate + CA NADH. CC -!- Also acts on 2-hydroxymuconate semialdehyde. // ID 1.2.1.33 DE (R)-dehydropantoate dehydrogenase. AN D-aldopantoate dehydrogenase. CA (R)-4-dehydropantoate + NAD(+) + H(2)O = (R)-3,3-dimethylmalate + NADH. // ID 1.2.1.34 DE Transferred entry: 1.1.1.131. // ID 1.2.1.35 DE Transferred entry: 1.1.1.203. // ID 1.2.1.36 DE Retinal dehydrogenase. CA Retinal + NAD(+) + H(2)O = retinoate + NADH. CF FAD. CC -!- Acts on both the 11-trans- and 13-cis-forms of retinal. // ID 1.2.1.37 DE Transferred entry: 1.1.1.204. // ID 1.2.1.38 DE N-acetyl-gamma-glutamyl-phosphate reductase. AN N-acetyl-glutamate semialdehyde dehydrogenase. AN NAGSA dehydrogenase. CA N-acetyl-L-glutamate 5-semialdehyde + NADP(+) + phosphate = CA N-acetyl-5-glutamyl phosphate + NADPH. PR PROSITE; PDOC00941; DR P78586, AR56_CANAL; P54898, AR56_NEUCR; P31318, AR56_SCHPO; DR Q01217, AR56_YEAST; P59391, ARC1_LACPL; Q9RVQ9, ARC2_DEIRA; DR O08318, ARC2_LACPL; O50146, ARC2_THETH; Q9YBY8, ARGC_AERPE; DR Q8UG00, ARGC_AGRT5; P54894, ARGC_ANASP; O67724, ARGC_AQUAE; DR O28208, ARGC_ARCFU; Q9K8V2, ARGC_BACHD; Q07906, ARGC_BACST; DR P23715, ARGC_BACSU; P59305, ARGC_BIFLO; Q8YGI8, ARGC_BRUME; DR P59314, ARGC_BRUSU; P57156, ARGC_BUCAI; Q8KA61, ARGC_BUCAP; DR Q9PIS0, ARGC_CAMJE; Q9A8H5, ARGC_CAUCR; Q8KDE3, ARGC_CHLTE; DR Q97GH7, ARGC_CLOAB; Q59279, ARGC_CORGL; Q9RY72, ARGC_DEIRA; DR Q8X732, ARGC_ECO57; P59306, ARGC_ECOL6; P11446, ARGC_ECOLI; DR Q9CHD5, ARGC_LACLA; P59307, ARGC_LEPIN; Q92BB7, ARGC_LISIN; DR Q8Y6U1, ARGC_LISMO; Q8TK53, ARGC_METAC; Q58496, ARGC_METJA; DR Q8TWF8, ARGC_METKA; Q8PZL6, ARGC_METMA; O26934, ARGC_METTH; DR Q9K4Z1, ARGC_MORS3; Q9K4Z6, ARGC_MORS4; Q9CC15, ARGC_MYCLE; DR P94987, ARGC_MYCTU; Q9JVU6, ARGC_NEIMA; Q9JY18, ARGC_NEIMB; DR O87890, ARGC_NOSEL; P57907, ARGC_PASMU; Q9I5Q9, ARGC_PSEAE; DR P59308, ARGC_PSEPK; Q9V1I6, ARGC_PYRAB; Q8ZUA0, ARGC_PYRAE; DR Q8U0B6, ARGC_PYRFU; O59397, ARGC_PYRHO; Q8Y339, ARGC_RALSO; DR Q9AKR8, ARGC_RHIET; Q982X3, ARGC_RHILO; Q92QR7, ARGC_RHIME; DR Q9LA02, ARGC_RHOCA; Q8Z309, ARGC_SALTI; Q8ZKL8, ARGC_SALTY; DR P59309, ARGC_SHEON; P59310, ARGC_SHIFL; Q99X37, ARGC_STAAM; DR Q8NYM6, ARGC_STAAW; P54896, ARGC_STRCL; P54895, ARGC_STRCO; DR P59311, ARGC_STRMU; Q980X1, ARGC_SULSO; Q976J5, ARGC_SULTO; DR P59312, ARGC_SYNEL; P54899, ARGC_SYNY3; Q9X2A2, ARGC_THEMA; DR Q9Z4S2, ARGC_THENE; P96136, ARGC_THETH; Q8R7B8, ARGC_THETN; DR Q9KNT6, ARGC_VIBCH; P59313, ARGC_VIBVU; Q8PK31, ARGC_XANAC; DR Q8P8J8, ARGC_XANCP; Q9PEM6, ARGC_XYLFA; Q87EL1, ARGC_XYLFT; DR Q8ZA86, ARGC_YERPE; // ID 1.2.1.39 DE Phenylacetaldehyde dehydrogenase. CA Phenylacetaldehyde + NAD(+) + H(2)O = phenylacetate + NADH. PR PROSITE; PDOC00068; DR P80668, FEAB_ECOLI; // ID 1.2.1.40 DE 3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-oxidoreductase. AN 3-alpha,7-alpha,12-alpha-trihydroxycholestan-26-al 26-dehydrogenase. CA 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-al + NAD(+) + CA H(2)O = 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestan-26-oate + CA NADH. // ID 1.2.1.41 DE Glutamate-5-semialdehyde dehydrogenase. AN Gamma-glutamylphosphate reductase. AN Beta-glutamylphosphate reductase. AN Glutamyl-gamma-semialdehyde dehydrogenase. CA L-glutamate 5-semialdehyde + phosphate + NADP(+) = L-gamma- CA glutamyl 5-phosphate + NADPH. PR PROSITE; PDOC00940; DR P54887, P5C1_ARATH; P54888, P5C2_ARATH; O04015, P5CS_ACTCH; DR P54889, P5CS_CAEEL; P54886, P5CS_HUMAN; Q96480, P5CS_LYCES; DR O65361, P5CS_MESCR; Q9Z110, P5CS_MOUSE; O04226, P5CS_ORYSA; DR P32296, P5CS_VIGAC; Q8UBS1, PROA_AGRT5; Q8YV15, PROA_ANASP; DR O67166, PROA_AQUAE; Q9KCR5, PROA_BACHD; P39821, PROA_BACSU; DR Q8YJ78, PROA_BRUME; P53000, PROA_CAMJE; Q9A2X6, PROA_CAUCR; DR Q97E62, PROA_CLOAB; Q8XHA7, PROA_CLOPE; P45638, PROA_CORGL; DR Q9RTD9, PROA_DEIRA; Q8X7N4, PROA_ECO57; P07004, PROA_ECOLI; DR P45121, PROA_HAEIN; Q9CF73, PROA_LACLA; P94872, PROA_LEPIN; DR Q92CE5, PROA_LISIN; Q93Q55, PROA_LISMO; O86053, PROA_MEIRU; DR Q9HHA1, PROA_METAC; Q8PYP2, PROA_METMA; Q9CBZ7, PROA_MYCLE; DR P71921, PROA_MYCTU; Q9JUK8, PROA_NEIMA; Q9JZG3, PROA_NEIMB; DR Q9CM98, PROA_PASMU; Q9HX20, PROA_PSEAE; Q8XVT6, PROA_RALSO; DR Q98EZ5, PROA_RHILO; Q92LB2, PROA_RHIME; Q8Z932, PROA_SALTI; DR P40861, PROA_SALTY; P17857, PROA_SERMA; Q9RDK1, PROA_STRCO; DR Q8K6C2, PROA_STRP3; Q8NZX9, PROA_STRP8; Q97R94, PROA_STRPN; DR Q99YJ8, PROA_STRPY; P96489, PROA_STRTR; P54902, PROA_SYNY3; DR Q9WYC9, PROA_THEMA; P54903, PROA_THETH; Q8RAE5, PROA_THETN; DR P74935, PROA_TREPA; Q9KPT9, PROA_VIBCH; Q87RU9, PROA_VIBPA; DR Q8DF94, PROA_VIBVU; Q8PK35, PROA_XANAC; Q8P8K3, PROA_XANCP; DR Q9PEM3, PROA_XYLFA; Q87EK9, PROA_XYLFT; P54885, PROA_YEAST; DR Q8ZC09, PROA_YERPE; // ID 1.2.1.42 DE Hexadecanal dehydrogenase (acylating). AN Fatty acyl-CoA reductase. CA Hexadecanal + CoA + NAD(+) = hexadecanoyl-CoA + NADH. CC -!- Also acts, more slowly, on octadecanoyl-CoA. // ID 1.2.1.43 DE Formate dehydrogenase (NADP+). CA Formate + NADP(+) = CO(2) + NADPH. CF Selenium; Tungsten; Iron. // ID 1.2.1.44 DE Cinnamoyl-CoA reductase. CA Cinnamaldehyde + CoA + NADP(+) = cinnamoyl-CoA + NADPH. CC -!- Also acts on a number of substituted cinnamoyl esters of coenzyme A. // ID 1.2.1.45 DE 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase. CA 4-carboxy-2-hydroxy-cis,cis-muconate 6-semialdehyde + NADP(+) = CA 4-carboxy-2-hydroxy-cis,cis-muconate + NADPH. CC -!- Does not act on unsubstituted aliphatic or aromatic aldehydes or CC glucose. CC -!- NAD(+) can replace NADP(+), but with lower affinity. // ID 1.2.1.46 DE Formaldehyde dehydrogenase. CA Formaldehyde + NAD(+) + H(2)O = formate + NADH. CC -!- Unlike EC 1.2.1.1, this enzyme from Pseudomonas does not need CC reduced glutathione. PR PROSITE; PDOC00058; DR P46154, FADH_PSEPU; // ID 1.2.1.47 DE 4-trimethylammoniobutyraldehyde dehydrogenase. CA 4-trimethylammoniobutanal + NAD(+) + H(2)O = 4-trimethylammoniobutanoate CA + NADH. // ID 1.2.1.48 DE Long-chain-aldehyde dehydrogenase. CA A long-chain aldehyde + NAD(+) + H(2)O = a long-chain acid anion + NADH. CC -!- The best substrate is dodecylaldehyde. // ID 1.2.1.49 DE 2-oxoaldehyde dehydrogenase (NADP+). AN Alpha-ketoaldehyde dehydrogenase. AN Methylglyoxal dehydrogenase. CA A 2-oxoaldehyde + NADP(+) + H(2)O = a 2-oxo acid + NADPH. CC -!- Not identical with EC 1.2.1.23. // ID 1.2.1.50 DE Long-chain-fatty-acyl-CoA reductase. AN Acyl-CoA reductase. CA A long-chain aldehyde + CoA + NADP(+) = a long-chain acyl-CoA + NADPH. CC -!- Together with EC 6.2.1.19 forms a fatty acid reductase system which CC produces the substrate of EC 1.14.14.3, thus being part of the CC bacterial luciferase system. DR P23113, LUXC_PHOLU; P19841, LUXC_PHOPO; P12748, LUXC_VIBFI; DR P08639, LUXC_VIBHA; Q03324, LXC1_PHOLE; P29236, LXC2_PHOLE; // ID 1.2.1.51 DE Pyruvate dehydrogenase (NADP+). CA Pyruvate + CoA + NADP(+) = acetyl-CoA + CO(2) + NADPH. CC -!- The Euglena enzyme can also use FAD or methyl viologen as acceptor, CC more slowly. CC -!- Inhibited by oxygen. // ID 1.2.1.52 DE Oxoglutarate dehydrogenase (NADP+). CA 2-oxoglutarate + CoA + NADP(+) = succinyl-CoA + CO(2) + NADPH. CC -!- The Euglena enzyme can also use NAD(+) as acceptor, more slowly. // ID 1.2.1.53 DE 4-hydroxyphenylacetaldehyde dehydrogenase. CA 4-hydroxyphenylacetaldehyde + NAD(+) + H(2)O = 4-hydroxyphenylacetate + CA NADH. CC -!- With EC 4.2.1.87, brings about the metabolism of octopamine in CC Pseudomonas. // ID 1.2.1.54 DE Gamma-guanidinobutyraldehyde dehydrogenase. CA 4-guanidinobutanal + NAD(+) + H(2)O = 4-guanidinobutanoate + NADH. CC -!- Involved in the degradation of arginine in Pseudomonas putida CC (cf. EC 1.2.1.19). // ID 1.2.1.55 DE (R)-3-hydroxyacid ester dehydrogenase. CA Ethyl (R)-3-hydroxyhexanoate + NADP(+) = ethyl 3-oxohexanoate + NADPH. CC -!- Also acts on ethyl (R)-3-oxobutanoate and some other (R)-3-hydroxy CC acid esters. The (R)- symbol is allotted on the assumption that no CC substituents change the order of priority from O-3>C-2>C-4. CC -!- A subunit of yeast EC 2.3.1.86 (cf. EC 1.2.1.56). // ID 1.2.1.56 DE (S)-3-hydroxyacid ester dehydrogenase. CA Ethyl (S)-3-hydroxyhexanoate + NADP(+) = ethyl 3-oxohexanoate + NADPH. CC -!- Also acts on 4-oxo- and 5-oxo-fatty acids and their esters (cf. CC EC 1.2.1.55). // ID 1.2.1.57 DE Butanal dehydrogenase. CA Butanal + CoA + NAD(P)(+) = butanoyl-CoA + NAD(P)H. CC -!- Also acts on acetaldehyde, more slowly. // ID 1.2.1.58 DE Phenylglyoxylate dehydrogenase (acylating). CA Phenylglyoxylate + NAD(+) + CoA = benzoyl-S-CoA + CO(2) + NADH. CF Thiamine pyrophosphate; FAD. CC -!- The enzyme from Azoarcus evansii is specific for phenylglyoxylate. CC -!- 2-oxoisovalerate is oxidized at 15% of the rate for phenylglyoxylate. CC -!- Also reduces viologen dyes. // ID 1.2.1.59 DE Glyceraldehyde 3-phosphate dehydrogenase (NAD(P)) (phosphorylating). AN NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase. AN Triosephosphate dehydrogenase (NAD(P)). CA D-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D- CA glyceroyl phosphate + NAD(P)H. CC -!- NAD and NADP can be used as cofactors with similar efficiency, unlike CC EC 1.2.1.12 and EC 1.2.1.13, which are NAD- and NADP-dependent, CC respectively. PR PROSITE; PDOC00069; DR P58837, G3P1_METAC; O34425, G3P2_BACSU; P58838, G3P2_METAC; DR P80505, G3P2_SYNY3; O09452, G3PA_GUITH; Q9YFS9, G3P_AERPE ; DR O28542, G3P_ARCFU ; Q9HSS7, G3P_HALN1 ; Q48335, G3P_HALVA ; DR P19314, G3P_METBR ; P10618, G3P_METFE ; P19315, G3P_METFO ; DR Q58546, G3P_METJA ; P58839, G3P_METKA ; Q8PTD3, G3P_METMA ; DR O27090, G3P_METTH ; Q9V1P1, G3P_PYRAB ; Q8ZWK7, G3P_PYRAE ; DR P20286, G3P_PYRFU ; O59494, G3P_PYRHO ; P39460, G3P_SULSO ; DR Q971K2, G3P_SULTO ; Q9HJ69, G3P_THEAC ; Q97BJ8, G3P_THEVO ; // ID 1.2.1.60 DE 5-carboxymethyl-2-hydroxymuconic-semialdehyde dehydrogenase. AN Carboxymethylhydroxymuconic semialdehyde dehydrogenase. CA 5-carboxymethyl-2-hydroxymuconate semialdehyde + H(2)O + NAD(+) = CA 5-carboxymethyl-2-hydroxymuconate + NADH. CC -!- Involved in the tyrosine degradation pathway in Arthrobacter sp. // ID 1.2.1.61 DE 4-hydroxymuconic-semialdehyde dehydrogenase. CA 4-hydroxymuconic semialdehyde + NAD(+) + H(2)O = maleylacetate + NADH. CC -!- Involved in the 4-nitrophenol degradation pathway. // ID 1.2.1.62 DE 4-formylbenzenesulfonate dehydrogenase. CA 4-formylbenzenesulfonate + NAD(+) + H(2)O = 4-sulfobenzoate + NADH. CC -!- Involved in the toluene-4-sulfonate degradation pathway. // ID 1.2.1.63 DE 6-oxohexanoate dehydrogenase. CA 6-oxohexanoate + NADP(+) + H(2)O = adipate + NADPH. CC -!- Last step in the cyclohexanol degradation pathway in CC Acinetobacter sp. // ID 1.2.1.64 DE 4-hydroxybenzaldehyde dehydrogenase. AN p-hydroxybenzaldehyde dehydrogenase. CA 4-hydroxybenzaldehyde + NAD(+) + H(2)O = 4-hydroxybenzoate + NADH. CC -!- Involved in the toluene degradation pathway in Pseudomonas CC mendocina. // ID 1.2.1.65 DE Salicylaldehyde dehydrogenase. CA Salicylaldehyde + NAD(+) + H(2)O = salicylate + NADH. CC -!- Involved in the naphthalene degradation pathway in some bacteria. PR PROSITE; PDOC00068; DR Q52460, NAHF_PSESP; // ID 1.2.1.66 DE Mycothiol-dependent formaldehyde dehydrogenase. AN NAD/factor-dependent formaldehyde dehydrogenase. CA Formaldehyde + mycothiol + NAD(+) = S-formylmycothiol + NADH. CF Zinc. CC -!- A similar reaction to that of EC 1.2.1.1, except that mycothiol CC {1-O-[2-(N-acetyl-L-cysteinamido)-2-deoxy-alpha-D-glucopyranosyl]- CC D-myo-inositol} replaces glutathione. The S-formylmycothiol formed CC hydrolyzes to mycothiol and formate. PR PROSITE; PDOC00058; DR P80094, FADH_AMYME; // ID 1.2.1.67 DE Vanillin dehydrogenase. CA Vanillin + NAD(+) + H(2)O = vanillate + NADH. // ID 1.2.1.68 DE Coniferyl-aldehyde dehydrogenase. CA Coniferyl aldehyde + H(2)O + NAD(P)(+) = ferulate + NAD(P)H. CC -!- The enzyme also oxidizes other aromatic aldehydes, but not CC aliphatic aldehydes. DR Q9A777, CALB_CAUCR; Q9I6C8, CALB_PSEAE; O86447, CALB_PSESP; // ID 1.2.2.1 DE Formate dehydrogenase (cytochrome). CA Formate + ferricytochrome b1 = CO(2) + ferrocytochrome b1. // ID 1.2.2.2 DE Pyruvate dehydrogenase (cytochrome). AN Pyruvate dehydrogenase. AN Pyruvic dehydrogenase. CA Pyruvate + ferricytochrome b1 + H(2)O = CO(2) + acetate + CA ferrocytochrome b1. CF Thiamine pyrophosphate. DI Ataxia with lactic acidosis I; MIM:208800. PR PROSITE; PDOC00166; DR P07003, POXB_ECOLI; // ID 1.2.2.3 DE Formate dehydrogenase (cytochrome c-553). CA Formate + ferricytochrome c-553 = CO(2) + ferrocytochrome c-553. CC -!- Yeast cytochrome c, ferricyanide and phenazine methosulfate can act CC as acceptors. // ID 1.2.2.4 DE Carbon monoxide oxygenase (cytochrome b-561). CA CO + H(2)O + ferrocytochrome b-561 = CO(2) + 2 H(+) + ferricytochrome CA b-561. CF FAD; Iron-molybdenum. CC -!- Methylene blue and iodonitrotetrazolium chloride can act as CC artificial electron acceptors. // ID 1.2.3.1 DE Aldehyde oxidase. AN Quinoline oxidase. CA An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2). CF FAD; Molybdenum; Heme. CC -!- Also oxidizes quinoline and pyridine derivatives. CC -!- May be identical with EC 1.2.3.11. PR PROSITE; PDOC00484; DR P48034, ADO_BOVIN ; Q06278, ADO_HUMAN ; O54754, ADO_MOUSE ; DR P80456, ADO_RABIT ; Q9Z0U5, ADO_RAT ; // ID 1.2.3.2 DE Transferred entry: 1.1.3.22. // ID 1.2.3.3 DE Pyruvate oxidase. AN Pyruvic oxidase. CA Pyruvate + phosphate + O(2) + H(2)O = acetyl phosphate + CO(2) + CA H(2)O(2). CF Thiamine pyrophosphate; FAD. PR PROSITE; PDOC00166; DR P37063, POXB_LACPL; Q54970, POXB_STRPN; // ID 1.2.3.4 DE Oxalate oxidase. CA Oxalate + O(2) = 2 CO(2) + H(2)O(2). CF Flavoprotein. PR PROSITE; PDOC00597; DR P15290, GER2_WHEAT; P26759, GER3_WHEAT; P45850, OXO1_HORVU; DR P45851, OXO2_HORVU; // ID 1.2.3.5 DE Glyoxylate oxidase. CA Glyoxylate + H(2)O + O(2) = oxalate + H(2)O(2). // ID 1.2.3.6 DE Pyruvate oxidase (CoA-acetylating). CA Pyruvate + CoA + O(2) = acetyl-CoA + CO(2) + H(2)O(2). CF FAD. CC -!- May be identical with EC 1.2.7.1. // ID 1.2.3.7 DE Indole-3-acetaldehyde oxidase. CA 2 indole-3-acetaldehyde + O(2) = 2 indole-3-acetate + 2 H(2)O. CF Heme. CC -!- Also oxidizes indole-3-aldehyde and acetaldehyde, more slowly. // ID 1.2.3.8 DE Pyridoxal oxidase. CA Pyridoxal + H(2)O + O(2) = 4-pyridoxate + H(2)O(2). CF Molybdenum. // ID 1.2.3.9 DE Aryl-aldehyde oxidase. CA An aromatic aldehyde + O(2) + H(2)O = an aromatic carboxylic acid CA + H(2)O(2). CC -!- Acts on benzaldehyde, vanillin and a number of other aromatic CC aldehydes, but not on aliphatic aldehydes or sugars. // ID 1.2.3.10 DE Carbon-monoxide oxidase. CA CO + H(2)O + O(2) = CO(2) + H(2)O(2). CF Iron-sulfur; Flavoprotein; Molybdenum. CC -!- Methylene blue can act as acceptor. // ID 1.2.3.11 DE Retinal oxidase. AN Retinene oxidase. CA Retinal + O(2) + H(2)O = retinoate + H(2)O(2). CC -!- May be the same as EC 1.2.3.1. // ID 1.2.3.12 DE Vanillate demethylase. AN 4-hydroxy-3-methoxybenzoate demethylase. CA Vanillate + O(2) + NADH = 3,4-dihydroxybenzoate + NAD(+) + H(2)O + CA formaldehyde. CF Iron-sulfur. CC -!- Forms part of the vanillin degradation pathway in Arthrobacter sp. PR PROSITE; PDOC00493; DR P12609, VANA_PSES9; O05616, VANA_PSESP; // ID 1.2.3.13 DE 4-hydroxyphenylpyruvate oxidase. CA 4-hydroxyphenylpyruvate + 1/2 O(2) = 4-hydroxyphenylacetate + CO(2). CC -!- Involved in tyrosine degradation pathway in Arthrobacter sp. // ID 1.2.4.1 DE Pyruvate dehydrogenase (lipoamide). AN Pyruvate decarboxylase. AN Pyruvate dehydrogenase. AN Pyruvic dehydrogenase. CA Pyruvate + lipoamide = S-acetyldihydrolipoamide + CO(2). CF Thiamine pyrophosphate. CC -!- Component of the multienzyme pyruvate dehydrogenase complex. DI Ataxia with lactic acidosis I; MIM:208800. DR Q59097, ODP1_ALCEU; P10801, ODP1_AZOVI; P57301, ODP1_BUCAI; DR Q8K9T9, ODP1_BUCAP; Q89AR0, ODP1_BUCBP; P06958, ODP1_ECOLI; DR P45119, ODP1_HAEIN; Q10504, ODP1_MYCTU; Q59637, ODP1_PSEAE; DR P35485, ODPA_ACHLA; P52901, ODPA_ARATH; P26267, ODPA_ASCSU; DR P21873, ODPA_BACST; P21881, ODPA_BACSU; P52899, ODPA_CAEEL; DR P49823, ODPA_CANFA; P08559, ODPA_HUMAN; O13366, ODPA_KLULA; DR P35486, ODPA_MOUSE; P47516, ODPA_MYCGE; P75390, ODPA_MYCPN; DR P52902, ODPA_PEA ; P29804, ODPA_PIG ; P51267, ODPA_PORPU; DR P26284, ODPA_RAT ; Q9R9N5, ODPA_RHIME; Q92IS3, ODPA_RICCN; DR Q9ZDR4, ODPA_RICPR; Q10489, ODPA_SCHPO; P52900, ODPA_SMIMA; DR P52903, ODPA_SOLTU; P16387, ODPA_YEAST; O66112, ODPA_ZYMMO; DR P35488, ODPB_ACHLA; Q38799, ODPB_ARATH; P26269, ODPB_ASCSU; DR P21874, ODPB_BACST; P21882, ODPB_BACSU; P11966, ODPB_BOVIN; DR P11177, ODPB_HUMAN; Q9MUR4, ODPB_MESVI; P47515, ODPB_MYCGE; DR P75391, ODPB_MYCPN; P52904, ODPB_PEA ; P51266, ODPB_PORPU; DR P49432, ODPB_RAT ; Q9R9N4, ODPB_RHIME; Q92IS2, ODPB_RICCN; DR Q9ZDR3, ODPB_RICPR; Q09171, ODPB_SCHPO; P81419, ODPB_SOLTU; DR P32473, ODPB_YEAST; O66113, ODPB_ZYMMO; P26268, ODPT_ASCSU; DR P29803, ODPT_HUMAN; P35487, ODPT_MOUSE; Q06437, ODPT_RAT ; // ID 1.2.4.2 DE Oxoglutarate dehydrogenase (lipoamide). AN Oxoglutarate decarboxylase. AN Alpha-ketoglutaric dehydrogenase. CA 2-oxoglutarate + lipoamide = S-succinyldihydrolipoamide + CO(2). CF Thiamine pyrophosphate. CC -!- Component of the multienzyme 2-oxoglutarate dehydrogenase complex. DR Q59106, ODO1_ALCEU; P20707, ODO1_AZOVI; P23129, ODO1_BACSU; DR P57388, ODO1_BUCAI; Q8K9N3, ODO1_BUCAP; Q89AJ7, ODO1_BUCBP; DR P51056, ODO1_COXBU; P07015, ODO1_ECOLI; P45303, ODO1_HAEIN; DR Q02218, ODO1_HUMAN; Q60597, ODO1_MOUSE; Q92J42, ODO1_RICCN; DR Q9ZDY3, ODO1_RICPR; P20967, ODO1_YEAST; // ID 1.2.4.3 DE Transferred entry: 1.2.4.4. // ID 1.2.4.4 DE 3-methyl-2-oxobutanoate dehydrogenase (lipoamide). AN 2-oxoisovalerate dehydrogenase. AN Branched-chain alpha-keto acid dehydrogenase. AN Branched-chain alpha-keto acid decarboxylase. CA 3-methyl-2-oxobutanoate + lipoamide = CA S-(2-methylpropanoyl)dihydrolipoamide + CO(2). CF Thiamine pyrophosphate. CC -!- Multienzyme complex. CC -!- Also acts on (S)-3-methyl-2-oxopentanoate and 4-methyl-2- CC oxopentanoate. CC -!- Formerly EC 1.2.4.3. DI Maple syrup urine disease; MIM:248600. DR P37940, ODBA_BACSU; P11178, ODBA_BOVIN; P12694, ODBA_HUMAN; DR P50136, ODBA_MOUSE; P09060, ODBA_PSEPU; P11960, ODBA_RAT ; DR P37941, ODBB_BACSU; P21839, ODBB_BOVIN; P21953, ODBB_HUMAN; DR P09061, ODBB_PSEPU; P35738, ODBB_RAT ; // ID 1.2.7.1 DE Pyruvate synthase. AN Pyruvate synthetase. AN Pyruvic-ferredoxin oxidoreductase. AN Pyruvate oxidoreductase. CA Pyruvate + CoA + oxidized ferredoxin = acetyl-CoA + CO(2) + reduced CA ferredoxin. DR Q57715, PORA_METJA; P56810, PORA_METTH; P80900, PORA_METTM; DR Q9UYZ4, PORA_PYRAB; Q51804, PORA_PYRFU; O73986, PORA_PYRHO; DR O05651, PORA_THEMA; Q57714, PORB_METJA; O27771, PORB_METTH; DR P80901, PORB_METTM; Q9UYZ5, PORB_PYRAB; Q51805, PORB_PYRFU; DR O58417, PORB_PYRHO; Q56317, PORB_THEMA; Q57717, PORC_METJA; DR O27772, PORC_METTH; P80902, PORC_METTM; Q9UYY9, PORC_PYRAB; DR Q51799, PORC_PYRFU; O58411, PORC_PYRHO; O05650, PORC_THEMA; DR Q57716, PORD_METJA; P56815, PORD_METTH; P80903, PORD_METTM; DR Q9UYZ3, PORD_PYRAB; Q51803, PORD_PYRFU; O58415, PORD_PYRHO; DR Q56316, PORD_THEMA; P80521, PYSA_METBA; P80522, PYSB_METBA; DR P80524, PYSD_METBA; P80523, PYSG_METBA; // ID 1.2.7.2 DE 2-oxobutyrate synthase. CA 2-oxobutanoate + CoA + oxidized ferredoxin = propanoyl-CoA + CO(2) + CA reduced ferredoxin. // ID 1.2.7.3 DE 2-oxoglutarate synthase. AN 2-oxoglutarate-ferredoxin oxidoreductase. AN Alpha-ketoglutarate synthase. AN Alpha-ketoglutarate-ferredoxin oxidoreductase. CA 2-oxoglutarate + CoA + oxidized ferredoxin = succinyl-CoA + CO(2) + CA reduced ferredoxin. DR O29781, KORA_ARCFU; Q57724, KORA_METJA; O27112, KORA_METTH; DR P80904, KORA_METTM; O29782, KORB_ARCFU; Q57957, KORB_METJA; DR O27113, KORB_METTH; P80905, KORB_METTM; O29779, KORC_ARCFU; DR Q57956, KORC_METJA; O27114, KORC_METTH; P80906, KORC_METTM; // ID 1.2.99.1 DE Transferred entry: 1.1.99.19. // ID 1.2.99.2 DE Carbon-monoxide dehydrogenase. CA CO + H(2)O + acceptor = CO(2) + reduced acceptor. CF Nickel; Zinc; Iron. CC -!- Methyl viologen can act as acceptor. CC -!- The enzyme from Clostridium sp. also catalyzes an exchange reaction CC of carbon between C-1 of acetyl-CoA and CO. CC -!- Involved in the synthesis of acetyl-CoA from CO(2) and H(2). DR P31896, COOS_RHORU; Q49161, DCA1_METMA; Q49163, DCA2_METMA; DR Q49162, DCB1_METMA; Q49164, DCB2_METMA; Q57617, DCMA_METJA; DR P26692, DCMA_METSO; Q08368, DCMA_METTE; O27743, DCMA_METTH; DR P27988, DCMA_MOOTH; P26693, DCMB_METSO; P27989, DCMB_MOOTH; DR Q50538, DCMD_METTE; Q50539, DCMG_METTE; P19913, DCML_HYDPS; DR P19919, DCML_OLICA; P19916, DCML_PSECH; P19914, DCMM_HYDPS; DR P19920, DCMM_OLICA; P19917, DCMM_PSECH; P19915, DCMS_HYDPS; DR P19921, DCMS_OLICA; P19918, DCMS_PSECH; // ID 1.2.99.3 DE Aldehyde dehydrogenase (pyrroloquinoline-quinone). AN Aldehyde dehydrogenase (acceptor). CA An aldehyde + acceptor + H(2)O = a carboxylate + reduced acceptor. CF PQQ. CC -!- Wide specificity; acts on straight-chain aldehydes up to C(10), CC aromatic aldehydes, glyoxylate and glyceraldehyde. DR P80472, DHAB_AMYME; P80704, DHAB_COMTE; P80705, DHAG_COMTE; DR P17201, DHAQ_ACEPO; // ID 1.2.99.4 DE Formaldehyde dismutase. CA 2 formaldehyde + H(2)O = formate + methanol. CC -!- Formaldehyde and acetaldehyde can act as donors. CC -!- Formaldehyde, acetaldehyde and propanal can act as acceptors. // ID 1.2.99.5 DE Formylmethanofuran dehydrogenase. CA Formylmethanofuran + H(2)O + acceptor = CO(2) + methanofuran + reduced CA acceptor. CF Molybdenum. CC -!- Methyl viologen can act as acceptor. CC -!- Also oxidizes N-furfurylformamide. DR Q48943, FMDC_METBA; O27002, FMDC_METTH; P95294, FMDC_METTM; DR Q58571, FWDC_METJA; O31112, FWDC_METMP; O27600, FWDC_METTH; DR Q59579, FWDC_METTM; O74031, FWDC_METWO; Q49611, FWDG_METKA; // ID 1.2.99.6 DE Carboxylate reductase. CA An aldehyde + acceptor + H(2)O = a carboxylate + reduced acceptor. CF Tungsten. CC -!- Methyl viologen can act as acceptor. CC -!- In the reverse direction, non-activated acids are reduced by CC reduced viologens to aldehydes, but not to the corresponding CC alcohols. // ID 1.3.1.1 DE Dihydrouracil dehydrogenase (NAD+). CA 5,6-dihydrouracil + NAD(+) = uracil + NADH. // ID 1.3.1.2 DE Dihydropyrimidine dehydrogenase (NADP+). AN Dihydrouracil dehydrogenase (NADP+). AN Dihydrothymine dehydrogenase. CA 5,6-dihydrouracil + NADP(+) = uracil + NADPH. CC -!- Also acts on dihydrothymine. DI Pyrimidinemia; MIM:274270. DR Q28007, DPYD_BOVIN; Q18164, DPYD_CAEEL; Q12882, DPYD_HUMAN; DR Q28943, DPYD_PIG ; // ID 1.3.1.3 DE Cortisone beta-reductase. AN Cortisone 5-beta-reductase. AN Delta-4-3-ketosteroid 5-beta-reductase. CA 4,5-beta-dihydrocortisone + NADP(+) = cortisone + NADPH. // ID 1.3.1.4 DE Cortisone alpha-reductase. CA 4,5-alpha-dihydrocortisone + NADP(+) = cortisone + NADPH. // ID 1.3.1.5 DE Cucurbitacin delta(23) reductase. CA 23,24-dihydrocucurbitacin + NAD(P)(+) = cucurbitacin + NAD(P)H. CF Manganese. CC -!- Iron or zinc can replace manganese to some extent. CC -!- Cucurbitacin is a plant triterpenoid. // ID 1.3.1.6 DE Fumarate reductase (NADH). AN NADH-dependent fumarate reductase. CA Succinate + NAD(+) = fumarate + NADH. // ID 1.3.1.7 DE Meso-tartrate dehydrogenase. CA Meso-tartrate + NAD(+) = dihydroxyfumarate + NADH. // ID 1.3.1.8 DE Acyl-CoA dehydrogenase (NADP+). AN 2-enoyl-CoA reductase. AN Enoyl coenzyme A reductase. CA Acyl-CoA + NADP(+) = 2,3-dehydroacyl-CoA + NADPH. CC -!- The liver enzyme acts on enoyl-CoA derivatives of carbon chain CC length 4 to 16, with optimum activity on 2-hexenoyl-CoA. CC -!- In E.coli, cis-specific and trans-specific enzymes exist CC (cf. EC 1.3.1.37 and EC 1.3.1.38). // ID 1.3.1.9 DE Enoyl-[acyl-carrier protein] reductase (NADH). AN Enoyl-ACP reductase. AN NADH-enoyl acyl carrier protein reductase. AN NADH-specific enoyl-ACP reductase. CA Acyl-[acyl-carrier protein] + NAD(+) = trans-2,3-dehydroacyl-[acyl- CA carrier protein] + NADH. CC -!- Catalyzes the reduction of enoyl-acyl-[acyl-carrier protein] CC derivatives of carbon chain length from 4 to 16. DR Q05069, FABI_ANASP; O67505, FABI_AQUAE; P54616, FABI_BACSU; DR P80030, FABI_BRANA; P57353, FABI_BUCAI; Q8K9Q6, FABI_BUCAP; DR Q89AM1, FABI_BUCBP; P29132, FABI_ECOLI; P44432, FABI_HAEIN; DR Q9ZMN7, FABI_HELPJ; O24990, FABI_HELPY; Q9ZFE4, FABI_PSEAE; DR Q9X450, FABI_RHIME; Q9ZDG4, FABI_RICPR; P16657, FABI_SALTY; DR P73016, FABI_SYNY3; P58380, FAI1_RHIME; P58381, FAI2_RHIME; DR P34731, FAS1_CANAL; Q9UUG0, FAS1_SCHPO; P34229, FAS1_YARLI; DR P07149, FAS1_YEAST; O07400, INHA_MYCAV; P42829, INHA_MYCSM; DR P46533, INHA_MYCTU; Q92215, TOXC_COCCA; // ID 1.3.1.10 DE Enoyl-[acyl-carrier protein] reductase (NADPH, B-specific). AN Acyl-ACP dehydrogenase. AN NADPH 2-enoyl Co A reductase. AN Enoyl acyl-carrier-protein reductase. AN Enoyl-ACP reductase. CA Acyl-[acyl-carrier protein] + NADP(+) = trans-2,3-dehydroacyl-[acyl- CA carrier protein] + NADPH. CC -!- Catalyzes the reduction of enoyl-acyl-[acyl-carrier protein] CC derivatives of carbon chain length from 4 to 16. CC -!- The yeast and E.coli enzymes are B-specific with respect to NADP(+) CC (cf. EC 1.3.1.9). DR P12276, FAS_CHICK ; P49327, FAS_HUMAN ; P19096, FAS_MOUSE ; DR P12785, FAS_RAT ; // ID 1.3.1.11 DE Coumarate reductase. AN Melilotate dehydrogenase. CA 3-(2-hydroxyphenyl)propanoate + NAD(+) = 2-coumarate + NADH. // ID 1.3.1.12 DE Prephenate dehydrogenase. AN Hydroxyphenylpyruvate synthase. CA Prephenate + NAD(+) = 4-hydroxyphenylpyruvate + CO(2) + NADH. CC -!- This enzyme in the enteric bacteria also possesses EC 5.4.99.5 CC activity and converts chorismate into prephenate. DR P20692, TYRA_BACSU; P07023, TYRA_ECOLI; Q02287, TYRA_ERWHE; DR P43902, TYRA_HAEIN; Q9CET9, TYRA_LACLA; P43901, TYRA_LACLC; DR Q04983, TYRC_ZYMMO; // ID 1.3.1.13 DE Prephenate dehydrogenase (NADP+). CA Prephenate + NADP(+) = 4-hydroxyphenylpyruvate + CO(2) + NADPH. DR O60078, TYR1_SCHPO; P20049, TYR1_YEAST; // ID 1.3.1.14 DE Orotate reductase (NADH). CA (S)-dihydroorotate + NAD(+) = orotate + NADH. CF FAD; FMN. // ID 1.3.1.15 DE Orotate reductase (NADPH). CA (S)-dihydroorotate + NADP(+) = orotate + NADPH. CF Flavoprotein. // ID 1.3.1.16 DE Beta-nitroacrylate reductase. CA 3-nitropropanoate + NADP(+) = 3-nitroacrylate + NADPH. // ID 1.3.1.17 DE 3-methyleneoxindole reductase. CA 3-methyloxindole + NADP(+) = 3-methyleneoxindole + NADPH. // ID 1.3.1.18 DE Kynurenate-7,8-dihydrodiol dehydrogenase. CA 7,8-dihydro-7,8-dihydroxykynurenate + NAD(+) = 7,8-dihydroxykynurenate + CA NADH. // ID 1.3.1.19 DE Cis-1,2-dihydrobenzene-1,2-diol dehydrogenase. AN Cis-benzene glycol dehydrogenase. CA Cis-1,2-dihydrobenzene-1,2-diol + NAD(+) = catechol + NADH. PR PROSITE; PDOC00060; DR P08088, BNZE_PSEPU; // ID 1.3.1.20 DE Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase. CA Trans-1,2-dihydrobenzene-1,2-diol + NADP(+) = catechol + NADPH. PR PROSITE; PDOC00061; DR Q04828, AKC1_HUMAN; P52895, AKC2_HUMAN; P42330, AKC3_HUMAN; // ID 1.3.1.21 DE 7-dehydrocholesterol reductase. AN 7-DHC reductase. AN Sterol delta-7-reductase. CA Cholesterol + NADP(+) = cholesta-5,7-dien-3-beta-ol + NADPH. DI Smith-Lemli-Opitz syndrome; MIM:270400. DR Q9UBM7, DHC7_HUMAN; O88455, DHC7_MOUSE; Q9LDU6, ST7R_ARATH; // ID 1.3.1.22 DE Cholestenone 5-alpha-reductase. CA 5-alpha-cholestan-3-one + NADP(+) = cholest-4-en-3-one + NADPH. // ID 1.3.1.23 DE Cholestenone 5-beta-reductase. CA 5-beta-cholestan-3-one + NADP(+) = cholest-4-en-3-one + NADPH. // ID 1.3.1.24 DE Biliverdin reductase. CA Bilirubin + NAD(P)(+) = biliverdin + NAD(P)H. DR P53004, BIEA_HUMAN; P46844, BIEA_RAT ; P52556, FLRE_BOVIN; DR P30043, FLRE_HUMAN; // ID 1.3.1.25 DE 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate dehydrogenase. CA 1,6-dihydroxycyclohexa-2,4-diene-1-carboxylate + NAD(+) = catechol + CA CO(2) + NADH. // ID 1.3.1.26 DE Dihydrodipicolinate reductase. CA 2,3,4,5-tetrahydrodipicolinate + NAD(P)(+) = 2,3-dihydrodipicolinate + CA NAD(P)H. PR PROSITE; PDOC01000; DR P58210, DAB1_RHILO; P58326, DAB1_RHIME; P58211, DAB2_RHILO; DR O69783, DAB2_RHIME; Q8UIV8, DAPB_AGRT5; Q8YU19, DAPB_ANASP; DR O67061, DAPB_AQUAE; O29353, DAPB_ARCFU; Q9KC93, DAPB_BACHD; DR P42976, DAPB_BACSU; Q9X6Y9, DAPB_BORPE; Q8YDC8, DAPB_BRUME; DR P57246, DAPB_BUCAI; Q8K9Z5, DAPB_BUCAP; P59474, DAPB_BUCBP; DR Q9PIT2, DAPB_CAMJE; Q9A2L1, DAPB_CAUCR; Q9PK30, DAPB_CHLMU; DR Q9Z6L2, DAPB_CHLPN; O84369, DAPB_CHLTR; Q97GI8, DAPB_CLOAB; DR Q8XJ55, DAPB_CLOPE; Q8RQN0, DAPB_COREF; P40110, DAPB_CORGL; DR P24703, DAPB_COXBU; P58209, DAPB_ECO57; P04036, DAPB_ECOLI; DR P45153, DAPB_HAEIN; Q9ZLW6, DAPB_HELPJ; P94844, DAPB_HELPY; DR P45415, DAPB_KLEPN; Q9CFC0, DAPB_LACLA; Q92AA1, DAPB_LISIN; DR Q8Y5Z6, DAPB_LISMO; Q9S3W8, DAPB_MASLA; Q8THP0, DAPB_METAC; DR Q57865, DAPB_METJA; Q8TVG7, DAPB_METKA; Q8PXL6, DAPB_METMA; DR O26891, DAPB_METTH; P46829, DAPB_MYCBO; P72024, DAPB_MYCTU; DR Q9JX48, DAPB_NEIMA; Q9K1F1, DAPB_NEIMB; P57867, DAPB_PASMU; DR P38103, DAPB_PSEAE; Q52419, DAPB_PSESZ; Q8XVT2, DAPB_RALSO; DR Q92J79, DAPB_RICCN; Q9ZE14, DAPB_RICPR; Q8Z9L9, DAPB_SALTI; DR Q8ZRX8, DAPB_SALTY; Q99U88, DAPB_STAAM; Q9EZ11, DAPB_STAAU; DR Q8NWS4, DAPB_STAAW; O86836, DAPB_STRCO; Q97PP8, DAPB_STRPN; DR P72642, DAPB_SYNY3; Q9X1K8, DAPB_THEMA; Q8RBI6, DAPB_THETN; DR Q9KPH7, DAPB_VIBCH; Q8PLE0, DAPB_XANAC; Q8P9L3, DAPB_XANCP; DR Q9PEC3, DAPB_XYLFA; Q87EC0, DAPB_XYLFT; Q8ZIL6, DAPB_YERPE; // ID 1.3.1.27 DE 2-hexadecenal reductase. AN 2-alkenal reductase. CA Hexadecanal + NADP(+) = 2-trans-hexadecenal + NADPH. CC -!- Specific for long chain 2-trans- and 2-cis-alkenals, with chain CC length optimum around 14 to 16 carbon atoms. // ID 1.3.1.28 DE 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase. AN 2,3-DHB dehydrogenase. CA 2,3-dihydro-2,3-dihydroxybenzoate + NAD(+) = 2,3-dihydroxybenzoate + CA NADH. CC -!- Formerly EC 1.1.1.109. PR PROSITE; PDOC00060; DR P39071, DHBA_BACSU; P15047, ENTA_ECOLI; Q56632, VIBA_VIBCH; // ID 1.3.1.29 DE Cis-1,2-dihydro-1,2-dihydroxynaphthalene dehydrogenase. AN Cis-naphthalene dihydrodiol dehydrogenase. AN Cis-dihydrodiol naphthalene dehydrogenase. CA Cis-1,2-dihydronaphthalene-1,2-diol + NAD(+) = naphthalene-1,2-diol + CA NADH. CC -!- Also acts, at half the rate, on cis-anthracene dihydrodiol and CC cis-phenanthrene dihydrodiol. // ID 1.3.1.30 DE Progesterone 5-alpha-reductase. AN Steroid 5-alpha-reductase. CA 5-alpha-pregnane-3,20-dione + NADP(+) = progesterone + NADPH. CC -!- Testosterone and 20-alpha-hydroxy-4-pregnen-3-one can act in place CC of progesterone. // ID 1.3.1.31 DE 2-enoate reductase. AN Enoate reductase. CA Butanoate + NAD(+) = 2-butenoate + NADH. CF Iron-sulfur; FAD. CC -!- Acts, in the reverse direction, on a wide range of alkyl and aryl CC alpha,beta-unsaturated carboxylate ions. CC -!- 2-butenoate was the best substrate tested. DR P11887, 2ENR_CLOTY; // ID 1.3.1.32 DE Maleylacetate reductase. AN Maleolylacetate reductase. CA 3-oxoadipate + NAD(P)(+) = 2-maleylacetate + NAD(P)H. DR O87612, CLCE_PSEAE; O30847, CLCE_PSESB; O84992, MCA1_RHOOP; DR P56870, MCA2_RHOOP; P27101, TCBF_PSESQ; P27137, TFF1_ALCEU; DR P94135, TFF2_ALCEU; Q45072, TFTE_BURCE; // ID 1.3.1.33 DE Protochlorophyllide reductase. AN NADPH-protochlorophyllide oxidoreductase. AN Protochlorophyllide oxidoreductase. CA Chlorophyllide A + NADP(+) = protochlorophyllide + NADPH. CC -!- Catalyzes a light-dependent trans-reduction of the D-ring of CC protochlorophyllide; the product has the (7S,8S)-configuration. DR Q42536, PORA_ARATH; Q41249, PORA_CUCSA; P13653, PORA_HORVU; DR Q41578, PORA_WHEAT; P21218, PORB_ARATH; Q42850, PORB_HORVU; DR O48741, PORC_ARATH; P15904, POR_AVESA ; Q39617, POR_CHLRE ; DR Q9SDT1, POR_DAUCA ; O80333, POR_MARPA ; Q01289, POR_PEA ; DR O66148, POR_PLEBO ; Q59987, POR_SYNY3 ; // ID 1.3.1.34 DE 2,4-dienoyl-CoA reductase (NADPH). AN 4-enoyl-CoA reductase (NADPH). CA Trans-2,3-didehydroacyl-CoA + NADP(+) = trans,trans-2,3,4,5- CA tetradehydroacyl-CoA + NADPH. CC -!- Best substrates for reduction contain a 2,4-diene structure with CC chain length C(8) or C(10). PR PROSITE; PDOC00060; DR Q16698, DECR_HUMAN; Q64591, DECR_RAT ; P42593, FADH_ECOLI; // ID 1.3.1.35 DE Phosphatidylcholine desaturase. AN Oleate desaturase. AN Oleoyl-CoA desaturase. AN Linoleate synthase. CA 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + NAD(+) = CA 1-acyl-2-linoleoyl-sn-glycero-3-phosphocholine + NADH. CC -!- Also desaturates phosphatidylcholines containing the oleoyl group on CC O-2 of the glycerol residue. // ID 1.3.1.36 DE Geissoschizine dehydrogenase. CA Geissoschizine + NADP(+) = 4,21-dehydrogeissoschizine + NADPH. CC -!- Involved in the interconversion of heteroyohimbine alkaloids in CC Catharanthus roseus. // ID 1.3.1.37 DE Cis-2-enoyl-CoA reductase (NADPH). CA Acyl-CoA + NADP(+) = cis-2,3-dehydroacyl-CoA + NADPH. CC -!- Not identical with EC 1.3.1.38 (cf. EC 1.3.1.8). // ID 1.3.1.38 DE Trans-2-enoyl-CoA reductase (NADPH). CA Acyl-CoA + NADP(+) = trans-2,3-dehydroacyl-CoA + NADPH. CC -!- Not identical with EC 1.3.1.37 (cf. EC 1.3.1.8). // ID 1.3.1.39 DE Enoyl-[acyl-carrier protein] reductase (NADPH, A-specific). AN Acyl-ACP dehydrogenase. CA Acyl-[acyl-carrier protein] + NADP(+) = trans,2,3-dehydroacyl- CA [acyl-carrier protein] + NADPH. CC -!- The liver enzyme is A-specific with respect to NADP(+) (cf. CC EC 1.3.1.10). // ID 1.3.1.40 DE 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate reductase. CA 2,6-dioxo-6-phenylhexanoate + NADP(+) = 2-hydroxy-6-oxo-6-phenylhexa- CA 2,4-dienoate + NADPH. CC -!- Broad specificity; reduces a number of compounds produced by CC Pseudomonas from aromatic hydrocarbons by ring fission. // ID 1.3.1.41 DE Xanthommatin reductase. CA 5,12-dihydroxanthommatin + NAD(+) = xanthommatin + NADH. CC -!- From Drosophila melanogaster. // ID 1.3.1.42 DE 12-oxophytodienoate reductase. CA 8-[(1R,2R)-3-oxo-2-{(Z)-pent-2-enyl}cyclopentyl]octanoate + NADP(+) = CA (15Z)-12-oxophyto-10,15-dienoate + NADPH. CC -!- Involved in the conversion of linolenate into jasmonate in maize. // ID 1.3.1.43 DE Cyclohexadienyl dehydrogenase. AN Pretyrosine dehydrogenase. AN Arogenate dehydrogenase. CA L-arogenate + NAD(+) = L-tyrosine + NADH + CO(2). CC -!- Also acts on prephenate and D-prephenyllactate (cf. EC 1.3.1.12). DR Q04983, TYRC_ZYMMO; // ID 1.3.1.44 DE Trans-2-enoyl-CoA reductase (NAD+). CA Acyl-CoA + NAD(+) = trans-2,3-didehydroacyl-CoA + NADH. CC -!- The enzyme from Euglena gracilis acts on crotonoyl-CoA and, more CC slowly, on trans-hex-2-enoyl-CoA and trans-oct-2-enoyl-CoA. // ID 1.3.1.45 DE 2'-hydroxyisoflavone reductase. CA Vestitone + NADP(+) = 2'-hydroxyformononetin + NADPH. CC -!- In the reverse direction, a 2'-hydroxyisoflavone is reduced to an CC isoflavonone. CC -!- 2'-hydroxypseudobaptigenin also acts. CC -!- Involved in the biosynthesis of the pterocarpin phytoalexins CC medicarpin and maackiain. // ID 1.3.1.46 DE Biochanin-A reductase. CA Dihydrobiochanin A + NADP(+) = biochanin A + NADPH. CC -!- Some other isoflavones are reduced to the corresponding CC isoflavonones. // ID 1.3.1.47 DE Alpha-santonin 1,2-reductase. CA 1,2-dihydrosantonin + NAD(P)(+) = alpha-santonin + NAD(P)H. // ID 1.3.1.48 DE 15-oxoprostaglandin 13-reductase. CA (5Z)-(15S)-11-alpha-hydroxy-9,15-dioxoprostanoate + NAD(P)(+) = CA (5Z)-(15S)-11-alpha-hydroxy-9,15-dioxoprosta-13-enoate + NAD(P)H. CC -!- Reduces 15-oxoprostaglandins to 13,14-dihydro derivates. CC -!- The enzyme from placenta is specific for NAD(+). // ID 1.3.1.49 DE Cis-3,4-dihydrophenanthrene-3,4-diol dehydrogenase. CA (+)-cis-3,4-dihydrophenanthrene-3,4-diol + NAD(+) = phenanthrene-3,4- CA diol + NADH. // ID 1.3.1.50 DE Transferred entry: 1.1.1.252. // ID 1.3.1.51 DE 2'-hydroxydaidzein reductase. CA 2'-hydroxydihydrodaidzein + NADP(+) = 2'-hydroxydaidzein + NADPH. CC -!- The enzyme is specific to the reduction of 2'-hydroxy-5- CC deoxyisoflavones. // ID 1.3.1.52 DE 2-methyl-branched-chain-enoyl-CoA reductase. CA 2-methylbutanoyl-CoA + NAD(+) = 2-methylcrotonoyl-CoA + NADH. CF FAD. CC -!- From Ascaris suum. CC -!- The reaction proceeds only in the presence of another flavoprotein CC (ETF='Electron-Transferring Flavoprotein'). // ID 1.3.1.53 DE (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate dehydrogenase. AN (1R,2S)-dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase. AN Dihydroxy-3,5-cyclohexadiene-1,4-dicarboxylate dehydrogenase. CA (3S,4R)-3,4-dihydroxycyclohexa-1,5-diene-1,4-dicarboxylate + NAD(+) = CA 3,4-dihydroxybenzoate + CO(2) + NADH. CF Iron. // ID 1.3.1.54 DE Precorrin-6X reductase. CA Precorrin-6Y + NADP(+) = precorrin-6X + NADPH. DR Q05591, CBIJ_SALTY; O27083, COBK_METTH; Q10680, COBK_MYCTU; DR P21920, COBK_PSEDE; Q53139, COBK_RHOER; P72711, COBK_SYNY3; // ID 1.3.1.55 DE Cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate dehydrogenase. AN Cis-1,2-dihydroxy-3,4-cyclohexadiene-1-carboxylate dehydrogenase. AN 2-hydro-1,2-dihydroxybenzoate dehydrogenase. AN DHB dehydrogenase. CA Cis-1,2-dihydroxycyclohexa-3,5-diene-1-carboxylate + NAD(+) = catechol + CA NADH. PR PROSITE; PDOC00060; DR P07772, BEND_ACICA; P23102, XYLL_PSEPU; // ID 1.3.1.56 DE Cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase. AN Biphenyl-2,3-dihydro-2,3-diol dehydrogenase. AN 2,3-dihydro-2,3-dihydroxybiphenyl dehydrogenase. CA Cis-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD(+) = biphenyl-2,3-diol + CA NADH. CC -!- Catalyzes the second step in the biphenyl degradation pathway in CC bacteria. PR PROSITE; PDOC00060; DR P47227, BPHB_BURCE; Q46381, BPHB_COMTE; P08694, BPHB_PSEPS; DR P72220, BPHB_PSEPU; P50206, BPHB_PSES1; P47230, BPHB_RHOGO; // ID 1.3.1.57 DE Phloroglucinol reductase. CA Dihydrophloroglucinol + NADP(+) = phloroglucinol + NADPH. CC -!- Involved in the gallate anaerobic degradation pathway in bacteria. DR P57793, PHGR_EUBOX; // ID 1.3.1.58 DE 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase. AN Biphenyl-2,3-dihydro-2,3-diol dehydrogenase. CA Cis-5,6-dihydroxy-4-isopropylcyclohexa-1,3-dienecarboxylate + NAD(+) = CA 2,3-dihydroxy-p-cumate + NADH. CC -!- Involved in the p-cymene and p-cumate degradation pathways in CC Pseudomonas putida. PR PROSITE; PDOC00060; DR Q51977, CMTB_PSEPU; // ID 1.3.1.59 DE 1,6-dihydroxy-5-methylcyclohexa-2,4-dienecarboxylate dehydrogenase. CA 1,6-dihydroxy-5-methylcyclohexa-2,4-dienecarboxylate + NAD(+) = CA 3-methylcatechol + CO(2) + NADH. CC -!- Involved in the m-xylene degradation pathway in bacteria. // ID 1.3.1.60 DE Dibenzothiophene dihydrodiol dehydrogenase. CA Cis-1,2-dihydroxy-1,2-dihydrodibenzothiophene + NAD(+) = CA 1,2-dihydroxydibenzothiophene + NADH. CC -!- Involved in the dibenzothiophene degradation pathway in bacteria. DR Q52459, NAHB_PSEPU; // ID 1.3.1.61 DE Terephthalate 1,2-cis-dihydrodiol dehydrogenase. CA Cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,4-dicarboxylate + NAD(+) = CA 3,4-dihydroxybenzoate + CO(2) + NADH. CC -!- Involved in the terephthalate degradation pathway in bacteria. // ID 1.3.1.62 DE Pimeloyl-CoA dehydrogenase. CA Pimeloyl-CoA + NAD(+) = 6-carboxyhex-2-enoyl-CoA + NADH. CC -!- Involved in the benzoate degradation (anaerobic) pathway in CC bacteria. // ID 1.3.1.63 DE 2,4-dichlorobenzoyl-CoA reductase. CA 4-chlorobenzoyl-CoA + NADP(+) + HCl = 2,4-dichlorobenzoyl-CoA + NADPH. CC -!- Acts in the reverse direction to form part of the CC 2,4-dichlorobenzoate degradation pathway in bacteria. // ID 1.3.1.64 DE Phthalate 4,5-cis-dihydrodiol dehydrogenase. CA Cis-4,5-dihydroxycyclohexa-1(6),2-diene-1,2-dicarboxylate + NAD(+) = CA 4,5-dihydroxyphthalate + NADH. CC -!- Involved in the phthalate degradation pathway in bacteria. // ID 1.3.1.65 DE 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline DE dehydrogenase. CA 5,6-dihydroxy-3-methyl-2-oxo-1,2,5,6-tetrahydroquinoline + NAD(+) = CA 5,6-dihydroxy-3-methyl-2-oxo-1,2-dihydroquinoline + NADH. CC -!- Acts in the reverse direction to form part of the CC 3-methylquinoline degradation pathway in bacteria. // ID 1.3.1.66 DE Cis-dihydroethylcatechol dehydrogenase. CA Cis-1,2-dihydro-3-ethylcatechol + NAD(+) = 3-ethylcatechol + NADH. CC -!- Involved in the ethylbenzene degradation pathway in bacteria. // ID 1.3.1.67 DE Cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate DE dehydrogenase. CA Cis-1,2-dihydroxy-4-methylcyclohexa-3,5-diene-1-carboxylate + CA NAD(P)(+) = 4-methylcatechol + NAD(P)H + CO(2). CC -!- Involved in the p-xylene degradation pathway in bacteria. // ID 1.3.1.68 DE 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate dehydrogenase. CA 1,2-dihydroxy-6-methylcyclohexa-3,5-dienecarboxylate + NAD(+) = CA 3-methylcatechol + NADH + CO(2). CC -!- Involved in the o-xylene degradation pathway in bacteria. // ID 1.3.1.69 DE Zeatin reductase. CA Dihydrozeatin + NADP(+) = zeatin + NADPH. CC -!- Previously classified erroneously as EC 1.1.1.242. // ID 1.3.1.70 DE Delta(14)-sterol reductase. AN C-14 sterol reductase. AN Sterol C14-reductase. CA 4,4-dimethyl-5-alpha-cholesta-8,24-dien-3-beta-ol + NADP(+) = CA 4,4-dimethyl-5-alpha-cholesta-8,14,24-trien-3-beta-ol + NADPH. CC -!- This enzyme acts on a range of steroids with a 14(15)-double bond. DR Q9LDR4, ER24_ARATH; P78575, ER24_ASCIM; Q01447, ER24_FUSSO; DR O76062, ER24_HUMAN; P38670, ER24_NEUCR; Q09195, ER24_SCHPO; DR O13597, ER24_SEPLY; P32462, ER24_YEAST; // ID 1.3.1.71 DE Delta(24(24(1)))-sterol reductase. AN Sterol delta(24(28))-reductase. AN Sterol delta(24(28))-methylene reductase. AN C-24(28) sterol reductase. CA Ergosterol + NADP(+) = ergosta-5,7,22,24(24(1))-tetraen-3-beta-ol + CA NADPH. CC -!- Acts on a range of steroids with a 24(24(1))-double bond. DR P25340, ERG4_YEAST; P36209, STS1_SCHPO; // ID 1.3.1.72 DE Delta(24)-sterol reductase. AN Lanosterol delta(24)-reductase. CA 5-alpha-cholest-7-en-3-beta-ol + NADP(+) = 5-alpha-cholesta-7,24-dien- CA 3-beta-ol + NADPH. CC -!- Acts on a range of steroids with a 24(25)-double bond, including CC lanosterol, desmosterol and zymosterol. // ID 1.3.1.73 DE 1,2-dihydrovomilenine reductase. CA 17-O-acetylnorajmaline + NADP(+) = 1,2-dihydrovomilenine + NADPH. CC -!- Forms part of the ajmaline biosynthesis pathway. // ID 1.3.2.1 DE Transferred entry: 1.3.99.2. // ID 1.3.2.2 DE Transferred entry: 1.3.99.3. // ID 1.3.2.3 DE Galactonolactone dehydrogenase. AN L-galactono-gamma-lactone dehydrogenase. CA L-galactono-1,4-lactone + 2 ferricytochrome c = L-ascorbate + CA 2 ferrocytochrome c. CC -!- Cf. EC 1.1.3.24. // ID 1.3.3.1 DE Dihydroorotate oxidase. AN Dihydroorotate dehydrogenase. AN DHOdehase. AN Dihydoorotic acid dehydrogenase. CA (S)-dihydroorotate + O(2) = orotate + H(2)O(2). CF FAD; FMN. CC -!- Ferricyanide can act as acceptor. PR PROSITE; PDOC00708; DR P59626, PYDA_ENTFA; Q9CFC9, PYDA_LACLA; P54321, PYDA_LACLC; DR Q47741, PYDB_ENTFA; Q9CFW8, PYDB_LACLA; P54322, PYDB_LACLC; DR Q9YFI6, PYRD_AERPE; P28294, PYRD_AGRAE; Q8YPC6, PYRD_ANASP; DR O66461, PYRD_AQUAE; P32746, PYRD_ARATH; O29513, PYRD_ARCFU; DR P46539, PYRD_BACCL; Q9K9W1, PYRD_BACHD; P25996, PYRD_BACSU; DR P57443, PYRD_BUCAI; Q8K9I5, PYRD_BUCAP; Q8FTC6, PYRD_COREF; DR Q8NQC0, PYRD_CORGL; Q9FB59, PYRD_CORST; Q9RX14, PYRD_DEIRA; DR P32748, PYRD_DROME; Q8FJ91, PYRD_ECOL6; P05021, PYRD_ECOLI; DR Q9F1U7, PYRD_FLALU; Q8RG85, PYRD_FUSNN; P45477, PYRD_HAEIN; DR Q9ZM11, PYRD_HELPJ; O25655, PYRD_HELPY; Q02127, PYRD_HUMAN; DR P77887, PYRD_LACPL; Q92AH5, PYRD_LISIN; Q8Y667, PYRD_LISMO; DR Q8TT55, PYRD_METAC; Q58070, PYRD_METJA; Q8PW56, PYRD_METMA; DR O27281, PYRD_METTH; O35435, PYRD_MOUSE; P46727, PYRD_MYCLE; DR O06236, PYRD_MYCTU; Q9JX66, PYRD_NEIMA; Q9K1D7, PYRD_NEIMB; DR Q8CWG1, PYRD_OCEIH; P57858, PYRD_PASMU; Q08210, PYRD_PLAFA; DR Q9HZF8, PYRD_PSEAE; Q9V0Y6, PYRD_PYRAB; Q8U0P6, PYRD_PYRFU; DR O59185, PYRD_PYRHO; Q8XYY7, PYRD_RALSO; Q63707, PYRD_RAT ; DR Q8Z7S9, PYRD_SALTI; P25468, PYRD_SALTY; P32747, PYRD_SCHPO; DR Q8EDZ8, PYRD_SHEON; Q9KXR7, PYRD_STRCO; Q9X9S0, PYRD_STRPN; DR O08358, PYRD_SULAC; Q9UX04, PYRD_SULSO; Q8DLB7, PYRD_SYNEL; DR P74782, PYRD_SYNY3; Q9HL35, PYRD_THEAC; Q9WYG8, PYRD_THEMA; DR Q8R9R7, PYRD_THETN; Q979G6, PYRD_THEVO; Q9KRZ2, PYRD_VIBCH; DR Q87PB7, PYRD_VIBPA; Q8D9G5, PYRD_VIBVU; Q8PLJ2, PYRD_XANAC; DR Q8P9R0, PYRD_XANCP; Q9PAE7, PYRD_XYLFA; Q87A77, PYRD_XYLFT; DR P28272, PYRD_YEAST; Q8ZG91, PYRD_YERPE; // ID 1.3.3.2 DE Lathosterol oxidase. AN Lathosterol 5-desaturase. AN Delta-7-sterol delta-5-dehydrogenase. AN Delta-7-sterol 5-desaturase. CA 5-alpha-cholest-7-en-3-beta-ol + O(2) = cholesta-5,7-dien-3-beta-ol + CA H(2)O(2). DI Lathosterolosis; MIM:607330. DR O75845, SC5D_HUMAN; O88822, SC5D_MOUSE; // ID 1.3.3.3 DE Coproporphyrinogen oxidase. AN Coproporphyrinogenase. AN Coproporphyrinogen-III oxidase. AN Coprogen oxidase. CA Coproporphyrinogen-III + O(2) = protoporphyrinogen-IX + 2 CO(2). CF Iron. DI Coproporphyria; MIM:121300. PR PROSITE; PDOC00783; DR Q8UD80, HEM6_AGRT5; Q8YX58, HEM6_ANASP; Q9LR75, HEM6_ARATH; DR Q8YIH7, HEM6_BRUME; Q9AAT8, HEM6_CAUCR; Q9V3D2, HEM6_DROME; DR Q8XBI4, HEM6_ECO57; Q8FFA3, HEM6_ECOL6; P36553, HEM6_ECOLI; DR Q42840, HEM6_HORVU; P36551, HEM6_HUMAN; P36552, HEM6_MOUSE; DR P43898, HEM6_PSEAE; Q8XXC3, HEM6_RALSO; Q92PD8, HEM6_RHIME; DR Q92FV8, HEM6_RICCN; Q9ZC86, HEM6_RICPR; Q8Z4U8, HEM6_SALTI; DR P33771, HEM6_SALTY; Q9UTE2, HEM6_SCHPO; P35055, HEM6_SOYBN; DR P72848, HEM6_SYNY3; Q42946, HEM6_TOBAC; Q9KVT4, HEM6_VIBCH; DR Q87KE3, HEM6_VIBPA; Q8DDD5, HEM6_VIBVU; Q8D1X2, HEM6_WIGBR; DR Q8PF76, HEM6_XANAC; Q8P3Q0, HEM6_XANCP; Q9PHC7, HEM6_XYLFA; DR Q87FB2, HEM6_XYLFT; P11353, HEM6_YEAST; Q8ZCF9, HEM6_YERPE; // ID 1.3.3.4 DE Protoporphyrinogen oxidase. AN Protoporphyrinogen-IX oxidase. AN Protoporphyrinogenase. CA Protoporphyrinogen-IX + O(2) = protoporphyrin-IX + H(2)O(2). CF FAD. CC -!- Also slowly oxidizes mesoporphyrinogen-IX. DI Porphyria variegata; MIM:176200. DR P27863, HEMG_ECOLI; Q9L6L1, HEMG_SALTY; P55826, PPOC_ARATH; DR O24163, PPOC_TOBAC; O24164, PPOM_TOBAC; P32397, PPOX_BACSU; DR P56602, PPOX_BOVIN; P50336, PPOX_HUMAN; P51175, PPOX_MOUSE; DR Q50008, PPOX_MYCLE; O53230, PPOX_MYCTU; P56601, PPOX_MYXXA; DR O32434, PPOX_PROFR; P40012, PPOX_YEAST; // ID 1.3.3.5 DE Bilirubin oxidase. CA Bilirubin + O(2) = biliverdin + H(2)O. DR Q12737, BLRO_MYRVE; // ID 1.3.3.6 DE Acyl-CoA oxidase. CA Acyl-CoA + O(2) = trans-2,3-dehydroacyl-CoA + H(2)O(2). CF FAD. CC -!- Acts on CoA derivatives of fatty acids with chain length from C(8) CC to C(18). DR P08790, CAO1_CANTR; Q9Z1N0, CAO1_CAVPO; Q15067, CAO1_HUMAN; DR Q9R0H0, CAO1_MOUSE; P07872, CAO1_RAT ; Q00468, CAO2_CANMA; DR P06598, CAO2_CANTR; Q99424, CAO2_HUMAN; Q9QXD1, CAO2_MOUSE; DR O02767, CAO2_RABIT; P97562, CAO2_RAT ; P11355, CAO3_CANTR; DR O15254, CAO3_HUMAN; Q9EPL9, CAO3_MOUSE; Q63448, CAO3_RAT ; DR P05335, CAO4_CANMA; P11356, CAO4_CANTR; P34355, CAOP_CAEEL; DR P13711, CAO_YEAST ; // ID 1.3.3.7 DE Dihydrouracil oxidase. CA 5,6-dihydrouracil + O(2) = uracil + H(2)O(2). CF FMN. CC -!- Also oxidizes dihydrothymine to thymine. // ID 1.3.3.8 DE Tetrahydroberberine oxidase. AN THB oxidase. CA (S)-tetrahydroberberine + 2 O(2) = berberine + 2 H(2)O(2). CF Flavoprotein. CC -!- (R)-tetrahydroberberines are not oxidized. CC -!- Formerly EC 1.5.3.8. // ID 1.3.3.9 DE Secologanin synthase. CA Loganin + NADPH + O(2) = secologanin + NADP(+) + 2 H(2)O. CF Heme-thiolate. CC -!- Secologanin is the precursor of the monoterpenoid indole alkaloids CC and ipecac alkaloids. PR PROSITE; PDOC00081; DR Q05047, CP72_CATRO; // ID 1.3.5.1 DE Succinate dehydrogenase (ubiquinone). AN Succinic dehydrogenase. CA Succinate + ubiquinone = fumarate + ubiquinol. CF FAD; Iron-sulfur. CC -!- The complex, present in mitochondria, can be degraded to form CC EC 1.3.99.1, which no longer reacts with ubiquinone. PR PROSITE; PDOC00393; DR O82663, DHSA_ARATH; P31039, DHSA_BOVIN; Q09508, DHSA_CAEEL; DR Q94523, DHSA_DROME; P31040, DHSA_HUMAN; Q9UTJ7, DHSA_SCHPO; DR Q00711, DHSA_YEAST; Q09545, DHSB_CAEEL; P48932, DHSB_CHOCR; DR P48933, DHSB_CYACA; P21914, DHSB_DROME; P21912, DHSB_HUMAN; DR O42772, DHSB_MYCGR; P80477, DHSB_PORPU; P21913, DHSB_RAT ; DR P80480, DHSB_RECAM; P21911, DHSB_SCHPO; P32420, DHSB_USTMA; DR P21801, DHSB_YEAST; P47052, DHSX_YEAST; // ID 1.3.7.1 DE 6-hydroxynicotinate reductase. AN 6-oxotetrahydro-nicotinate dehydrogenase. AN 6-hydroxynicotinic reductase. AN HNA reductase. CA 1,4,5,6-tetrahydro-6-oxonicotinate + oxidized ferredoxin = CA 6-hydroxynicotinate + reduced ferredoxin. // ID 1.3.7.2 DE 15,16-dihydrobiliverdin:ferredoxin oxidoreductase. CA 15,16-dihydrobiliverdin + oxidized ferredoxin = biliverdin IXa + CA reduced ferredoxin. CC -!- Catalyzes the two-electron reduction of biliverdin IXa at the CC C15 methine bridge. CC -!- It has been proposed that this enzyme and EC 1.3.7.3 function as a CC dual enzyme complex in the conversion of biliverdin IXa into CC phycoerythrobilin. DR Q93TL6, PEBA_NOSPU; Q9K4U6, PEBA_PROMA; Q93SN8, PEBA_PROS1; DR Q02189, PEBA_SYNPY; // ID 1.3.7.3 DE Phycoerythrobilin:ferredoxin oxidoreductase. CA (3Z)-phycoerythrobilin + oxidized ferredoxin = 15,16-dihydrobiliverdin CA + reduced ferredoxin. CC -!- Catalyzes the two-electron reduction of the C2 and C3(1) diene CC system of 15,16-dihydrobiliverdin. CC -!- Specific for 15,16-dihydrobiliverdin. CC -!- It has been proposed that this enzyme and EC 1.3.7.2 function as a CC dual enzyme complex in the conversion of biliverdin IXa into CC phycoerythrobilin. DR Q93TM8, PEBB_NOSPU; Q9K4U5, PEBB_PROMA; Q93SN7, PEBB_PROS1; DR Q02190, PEBB_SYNPY; // ID 1.3.7.4 DE Phytochromobilin:ferredoxin oxidoreductase. AN Phytochromobilin synthase. AN PPhiB synthase. AN PFB synthase. CA (3Z)-phytochromobilin + oxidized ferredoxin = biliverdin IXa + reduced CA ferredoxin. CC -!- Catalyzes the two-electron reduction of biliverdin IXa. CC -!- Can use 2Fe-2S ferredoxins from a number of sources as acceptor but CC not the 4Fe-4S ferredoxin from Clostridium pasteurianum. CC -!- The isomerization of (3Z)-phytochromobilin to (3E)-phytochromobilin CC is thought to occur prior to covalent attachment to apophytochrome CC in the plant cell cytoplasm. CC -!- Flavodoxins can be used instead of ferredoxin. DR Q9SR43, PFBS_ARATH; // ID 1.3.7.5 DE Phycocyanobilin:ferredoxin oxidoreductase. CA (3Z)-phycocyanobilin + oxidized ferredoxin = biliverdin IXa + reduced CA ferredoxin. CC -!- Catalyzes the four-electron reduction of biliverdin IXa (2-electron CC reduction at both the A and D rings). CC -!- Reaction proceeds via an isolatable 2-electron intermediate, CC 181,182-dihydrobiliverdin. CC -!- Flavodoxins can be used instead of ferredoxin. CC -!- The direct conversion of biliverdin IXa (BV) to (3Z)- CC phycocyanolbilin (PCB) in the cyanobacteria Synechocystis sp PCC CC 6803, Anabaena sp PCC7120 and Nostoc punctiforme is in contrast to CC the proposed pathways of PCB biosynthesis in the red alga Cyanidium CC caldarium, which involves (3Z)-phycoerythrobilin (PEB) as an CC intermediate and in the green alga Mesotaenium caldariorum, in CC which PCB is an isolable intermediate. DR Q93TN0, PCYA_ANASP; Q93TM9, PCYA_NOSPU; Q93TL5, PCYA_PROS1; DR P59288, PCYA_SYNEL; Q8KPS9, PCYA_SYNP7; Q55891, PCYA_SYNY3; // ID 1.3.99.1 DE Succinate dehydrogenase. AN Succinic dehydrogenase. AN Fumarate reductase. AN Fumarate dehydrogenase. AN Fumaric hydrogenase. CA Succinate + acceptor = fumarate + reduced acceptor. CF FAD. PR PROSITE; PDOC00393; DR P08065, DHSA_BACSU; P51054, DHSA_COXBU; P10444, DHSA_ECOLI; DR Q59661, DHSA_PARDE; Q92J97, DHSA_RICCN; P31038, DHSA_RICPR; DR Q8ZQU3, DHSA_SALTY; P08066, DHSB_BACSU; P51053, DHSB_COXBU; DR P07014, DHSB_ECOLI; Q59662, DHSB_PARDE; Q92JJ8, DHSB_RICCN; DR Q9ZEA1, DHSB_RICPR; Q8ZQU2, DHSB_SALTY; Q9Z4P0, FRD2_SHEFR; DR P00363, FRDA_ECOLI; P44894, FRDA_HAEIN; Q9ZMP0, FRDA_HELPJ; DR O06913, FRDA_HELPY; Q10760, FRDA_MYCTU; P20922, FRDA_PROVU; DR Q02469, FRDA_SHEFR; P83223, FRDA_SHEON; P17412, FRDA_WOLSU; DR P00364, FRDB_ECOLI; P44893, FRDB_HAEIN; Q9ZMP1, FRDB_HELPJ; DR O06914, FRDB_HELPY; Q10761, FRDB_MYCTU; P20921, FRDB_PROVU; DR P17596, FRDB_WOLSU; // ID 1.3.99.2 DE Butyryl-CoA dehydrogenase. AN Short-chain acyl-CoA dehydrogenase. AN Unsaturated acyl-CoA reductase. AN Butyryl dehydrogenase. CA Butanoyl-CoA + ETF = 2-butenoyl-CoA + reduced ETF. CF FAD. CC -!- Forms with another flavoprotein (ETF = 'Electron-Transferring CC Flavoprotein') and EC 1.5.5.1 a system reducing ubiquinone and CC other acceptors. CC -!- Formerly EC 1.3.2.1. DI Deficiency of short-chain acyl-CoA dehydrogenase; MIM:201470. PR PROSITE; PDOC00070; DR P52042, ACDS_CLOAB; P16219, ACDS_HUMAN; Q06319, ACDS_MEGEL; DR Q07417, ACDS_MOUSE; P79273, ACDS_PIG ; P15651, ACDS_RAT ; // ID 1.3.99.3 DE Acyl-CoA dehydrogenase. AN Medium-chain acyl-CoA dehydrogenase. AN Acyl dehydrogenase. CA Acyl-CoA + ETF = 2,3-dehydroacyl-CoA + reduced ETF. CF FAD. CC -!- Forms with another flavoprotein (ETF = 'Electron-Transferring CC Flavoprotein') and EC 1.5.5.1 a system reducing ubiquinone and CC other acceptors. CC -!- Formerly EC 1.3.2.2. DI Deficiency of medium-chain acyl-CoA dehydrogenase; MIM:201450. PR PROSITE; PDOC00070; DR Q22347, ACDM_CAEEL; Q9VSA3, ACDM_DROME; P11310, ACDM_HUMAN; DR P45952, ACDM_MOUSE; P41367, ACDM_PIG ; P08503, ACDM_RAT ; // ID 1.3.99.4 DE 3-oxosteroid 1-dehydrogenase. CA A 3-oxosteroid + acceptor = a 3-oxo-delta(1)-steroid + reduced acceptor. DR Q06401, 3O1D_COMTE; Q04616, 3O1D_RHOOP; // ID 1.3.99.5 DE 3-oxo-5-alpha-steroid 4-dehydrogenase. AN Steroid 5-alpha-reductase. CA A 3-oxo-5-alpha-steroid + acceptor = a 3-oxo-delta(4)-steroid + reduced CA acceptor. DI Male pseudohermaphroditism (pseudovaginal perineoscrotal); MIM:264600. DR P18405, S5A1_HUMAN; Q28891, S5A1_MACFA; P24008, S5A1_RAT ; DR P31213, S5A2_HUMAN; Q28892, S5A2_MACFA; Q99N99, S5A2_MOUSE; DR O18765, S5A2_PIG ; P31214, S5A2_RAT ; // ID 1.3.99.6 DE 3-oxo-5-beta-steroid 4-dehydrogenase. AN Delta(4)-3-ketosteroid 5-beta-reductase. CA A 3-oxo-5-beta-steroid + acceptor = a 3-oxo-delta(4)-steroid + reduced CA acceptor. PR PROSITE; PDOC00061; DR P51857, AKD1_HUMAN; P31210, AKD1_RAT ; // ID 1.3.99.7 DE Glutaryl-CoA dehydrogenase. CA Glutaryl-CoA + acceptor = crotonoyl-CoA + CO(2) + reduced acceptor. CF FAD. DI Glutaricaciduria I; MIM:231670. PR PROSITE; PDOC00070; DR Q20772, GCDH_CAEEL; Q92947, GCDH_HUMAN; Q60759, GCDH_MOUSE; DR P81140, GCDH_PIG ; // ID 1.3.99.8 DE 2-furoyl-CoA dehydrogenase. AN Furoyl-CoA hydroxylase. CA 2-furoyl-CoA + H(2)O + acceptor = S-(5-hydroxy-2-furoyl)-CoA + reduced CA acceptor. CF Copper. CC -!- The oxygen atom of the -OH produced is derived from water, not O(2). CC -!- The actual oxidative step is probably dehydrogenation of a hydrated CC form -CHOH-CH(2)- TO -C(OH)=CH-, which tautomerizes non-enzymically CC to -CO-CH(2)-, giving (5-oxo-4,5-dihydro-2-furoyl)-CoA. CC -!- Methylene blue, nitro blue tetrazolium and a membrane fraction from CC P.putida can act as acceptors. // ID 1.3.99.9 DE Transferred entry: 1.21.99.1. // ID 1.3.99.10 DE Isovaleryl-CoA dehydrogenase. CA 3-methylbutanoyl-CoA + ETF = 3-methylbut-2-enoyl-CoA + reduced ETF. CF FAD. CC -!- Forms with another flavoprotein (ETF = 'Electron-Transferring CC Flavoprotein') and EC 1.5.5.1 a system reducing ubiquinone and CC other acceptors. CC -!- N-pentanoate can act as donor. CC -!- Not identical with EC 1.3.99.2, EC 1.3.99.3 or EC 1.3.99.12. DI Isovalericacidemia; MIM:243500. PR PROSITE; PDOC00070; DR Q9FS88, IVD1_SOLTU; Q9FS87, IVD2_SOLTU; Q9SWG0, IVD_ARATH ; DR P34275, IVD_CAEEL ; P26440, IVD_HUMAN ; P12007, IVD_RAT ; // ID 1.3.99.11 DE Dihydroorotate dehydrogenase. CA (S)-dihydroorotate + acceptor = orotate + reduced acceptor. CF Iron; Zinc. CC -!- Oxygen can act as acceptor, but much more slowly than CC 2,6-dichloroindophenol or 1,10-phenanthroline. DR P07670, DHDO_DICDI; // ID 1.3.99.12 DE 2-methylacyl-CoA dehydrogenase. AN Branched-chain acyl-CoA dehydrogenase. CA 2-methylbutanoyl-CoA + acceptor = 2-methylbut-2-enoyl-CoA + reduced CA acceptor. CF FAD. CC -!- Also oxidizes 2-methylpropanoyl-CoA. CC -!- Not identical with EC 1.3.99.2, EC 1.3.99.3, EC 1.3.99.10 or CC EC 1.3.99.13. PR PROSITE; PDOC00070; // ID 1.3.99.13 DE Long-chain acyl-CoA dehydrogenase. CA Acyl-CoA + ETF = 2,3-dehydroacyl-CoA + reduced ETF. CF FAD. CC -!- Forms with another flavoprotein (ETF = 'Electron-Transferring CC Flavoprotein') and EC 1.5.5.1 a system reducing ubiquinone and CC other acceptors. CC -!- Not identical with EC 1.3.99.2, EC 1.3.99.3, EC 1.3.99.10 or CC EC 1.3.99.12. DI Deficiency of long-chain acyl-coa dehydrogenase; MIM:201460. PR PROSITE; PDOC00070; DR P28330, ACDL_HUMAN; P51174, ACDL_MOUSE; P79274, ACDL_PIG ; DR P15650, ACDL_RAT ; // ID 1.3.99.14 DE Cyclohexanone dehydrogenase. CA Cyclohexanone + acceptor = cyclohex-2-enone + reduced acceptor. CC -!- 2,6-dichloroindophenol can act as acceptor. CC -!- The corresponding ketones of cyclopentane cannot act as donors. // ID 1.3.99.15 DE Benzoyl-CoA reductase. AN Benzoyl-CoA reductase (dearomatizing). CA Benzoyl-CoA + reduced acceptor + 2 ATP = cyclohexa-1,5-diene-1-carbonyl- CA CoA + acceptor + 2 ADP + 2 phosphate. CF Manganese or Magnesium. CC -!- Reduced methyl viologen can act as electron donor. CC -!- Inactive towards aromatic acids that are not CoA esters but will also CC catalyze the reaction: ammonia + acceptor + 2 ADP + 2 phosphate + CC H(2)O = hydroxylamine + reduced acceptor + 2 ATP. CC -!- In the presence of reduced acceptor, but in the absence of oxidizable CC substrate, the enzyme catalyzes the hydrolysis of ATP to ADP plus CC phosphate. // ID 1.3.99.16 DE Isoquinoline 1-oxidoreductase. CA Isoquinoline + acceptor + H(2)O = isoquinolin-1(2H)-one + reduced CA acceptor. CC -!- The enzyme from Pseudomonas diminuta is specific towards N-containing CC N-heterocyclic substrates, including isoquinoline, isoquinolin-5-ol, CC phthalazine and quinazoline. CC -!- Electron acceptors include 1,2-benzoquinone, cytochrome c, CC ferricyanide, iodonitrotetrazolium chloride (INT), nitroblue CC tetrazolium (NBT), Meldola blue and phenazine methosulfate. DR Q51697, IORA_BREDI; Q51698, IORB_BREDI; // ID 1.3.99.17 DE Quinoline 2-oxidoreductase. CA Quinoline + acceptor + H(2)O = isoquinolin-1(2H)-one + reduced acceptor. CF FAD; Molybdenum; Iron-sulfur. CC -!- In addition to quinoline, quinolin-2-ol, quinolin-7-ol, CC quinolin-8-ol, 3-, 4- and 8-methylquinolines and 8-chloroquinoline CC are substrates. CC -!- Iodonitrotetrazolium chloride (INT) can act as an electron acceptor. DR P80464, Q2OA_COMTE; P80465, Q2OB_COMTE; P80466, Q2OG_COMTE; // ID 1.3.99.18 DE Quinaldate 4-oxidoreductase. AN Quinaldic acid 4-oxidoreductase. CA Quinaldate + acceptor + H(2)O = kynurenate + reduced acceptor. CC -!- The enzyme from Pseudomonas sp. AK2 also acts on quinoline-8- CC carboxylate, whereas that from Serratia marcescens 2CC-1 will oxidize CC nicotinate; quinaldate is a substrate for both of these enzymes. CC -!- 2,4,6-Trinitrobenzene sulfonate acid, 1,4-benzoquinone, 1,2- CC naphthoquinone, nitroblue tetrazolium (NBT), thionine and menadione CC will serve as an electron acceptor for the former enzyme and CC ferricyanide for the latter; Meldola blue, iodonitrotetrazolium CC chloride (INT), phenazine methosulfate (PMS), 2,6- CC dichlorophenolindophenol (DCPIP) and cytochrome c will act as CC electron acceptors for both. // ID 1.3.99.19 DE Quinoline-4-carboxylate 2-oxidoreductase. AN Quinoline-4-carboxylic acid 2-oxidoreductase. AN Quinaldic acid 4-oxidoreductase. CA Quinoline-4-carboxylate + acceptor + H(2)O = quinolin-2(1H)-one + reduced CA acceptor. CC -!- Quinoline-4-carboxylate, quinoline, 4-methyl quinoline and 4- CC chloroquinoline will also serve as substrates for the enzyme from CC Agrobacterium sp. 1B. CC -!- 1,4-Benzoquinone, iodonitrotetrazolium chloride (INT), thionine, CC menadione and 2,6-dichlorophenolindophenol (DCPIP) will act as CC electron acceptors. // ID 1.3.99.20 DE 4-hydroxybenzoyl-CoA reductase. CA 4-hydroxybenzoyl-CoA + acceptor = benzoyl-CoA + reduced acceptor. CC -!- Involved in the anaerobic pathway of phenol metabolism in CC bacteria. DR O33819, HCRA_THAAR; O33820, HCRB_THAAR; O33818, HCRC_THAAR; // ID 1.4.1.1 DE Alanine dehydrogenase. CA L-alanine + H(2)O + NAD(+) = pyruvate + NH(3) + NADH. PR PROSITE; PDOC00654; DR P17556, DHA_BACSH ; P17557, DHA_BACST ; Q08352, DHA_BACSU ; DR P30234, DHA_MYCTU ; // ID 1.4.1.2 DE Glutamate dehydrogenase. AN Glutamic dehydrogenase. CA L-glutamate + H(2)O + NAD(+) = 2-oxoglutarate + NH(3) + NADH. PR PROSITE; PDOC00071; DR P41755, DHE2_ACHKL; P94316, DHE2_BACFR; P39633, DHE2_BACSU; DR P27346, DHE2_CLODI; P24295, DHE2_CLOSY; P00365, DHE2_NEUCR; DR P28997, DHE2_PEPAS; Q03578, DHE2_PORGI; P20016, DHE2_THUTH; DR P33327, DHE2_YEAST; P50735, GUDB_BACSU; // ID 1.4.1.3 DE Glutamate dehydrogenase (NAD(P)+). AN Glutamic dehydrogenase. CA L-glutamate + H(2)O + NAD(P)(+) = 2-oxoglutarate + NH(3) + NAD(P)H. PR PROSITE; PDOC00071; DR Q43314, DHE1_ARATH; Q38946, DHE2_ARATH; P80053, DHE2_SULSO; DR Q9YC65, DHE3_AERPE; Q9S7A0, DHE3_ARATH; P94598, DHE3_BACTN; DR P00366, DHE3_BOVIN; P82264, DHE3_CHAAC; P00368, DHE3_CHICK; DR P54385, DHE3_DROME; P28270, DHE3_ELEEL; P00367, DHE3_HUMAN; DR P93541, DHE3_LYCES; Q43260, DHE3_MAIZE; P26443, DHE3_MOUSE; DR P42174, DHE3_PIG ; Q47950, DHE3_PYRAB; Q47951, DHE3_PYREN; DR P80319, DHE3_PYRFU; O52310, DHE3_PYRHO; O59650, DHE3_PYRKO; DR Q09115, DHE3_PYRWO; P10860, DHE3_RAT ; Q53199, DHE3_RHISN; DR Q56304, DHE3_THELI; P96110, DHE3_THEMA; O74024, DHE3_THEPR; DR P52596, DHE3_VITVI; P49448, DHE4_HUMAN; O04937, DHEA_NICPL; DR Q9LEC8, DHEB_NICPL; // ID 1.4.1.4 DE Glutamate dehydrogenase (NADP+). AN Glutamic dehydrogenase. CA L-glutamate + H(2)O + NADP(+) = 2-oxoglutarate + NH(3) + NADPH. PR PROSITE; PDOC00071; DR P54387, DHE4_AGABI; P28998, DHE4_CHLSO; Q8RQP4, DHE4_COREF; DR P31026, DHE4_CORGL; P29507, DHE4_DEBOC; P00370, DHE4_ECOLI; DR P18819, DHE4_EMENI; P28724, DHE4_GIALA; P43793, DHE4_HAEIN; DR Q9HSM4, DHE4_HALN1; P29051, DHE4_HALSA; Q9ZKD8, DHE4_HELPJ; DR P55990, DHE4_HELPY; P54388, DHE4_LACBI; P00369, DHE4_NEUCR; DR P95544, DHE4_PRERU; Q9S1F9, DHE4_PSYT1; Q8Z6F6, DHE4_SALTI; DR P15111, DHE4_SALTY; P39475, DHE4_SULSH; P54386, DHE4_SYNY3; DR P14657, DHE4_UNKP ; P07262, DHE4_YEAST; P39708, DHE5_YEAST; // ID 1.4.1.5 DE L-amino-acid dehydrogenase. CA An L-amino acid + H(2)O + NAD(+) = a 2-oxo acid + NH(3) + NADH. CC -!- Acts on aliphatic amino acids. // ID 1.4.1.6 DE Transferred entry: 1.21.4.1. // ID 1.4.1.7 DE Serine dehydrogenase. CA L-serine + H(2)O + NAD(+) = 3-hydroxypyruvate + NH(3) + NADH. // ID 1.4.1.8 DE Valine dehydrogenase (NADP+). CA L-valine + H(2)O + NADP(+) = 3-methyl-2-oxobutanoate + NH(3) + NADPH. // ID 1.4.1.9 DE Leucine dehydrogenase. AN LeuDH. CA L-leucine + H(2)O + NAD(+) = 4-methyl-2-oxopentanoate + NH(3) + NADH. CC -!- Also acts on isoleucine, valine, norvaline and norleucine. PR PROSITE; PDOC00071; DR Q59194, DHLE_BACCR; Q53560, DHLE_BACLI; P13154, DHLE_BACST; DR P54531, DHLE_BACSU; Q60030, DHLE_THEIN; // ID 1.4.1.10 DE Glycine dehydrogenase. CA Glycine + H(2)O + NAD(+) = glyoxylate + NH(3) + NADH. // ID 1.4.1.11 DE L-erythro-3,5-diaminohexanoate dehydrogenase. CA L-erythro-3,5-diaminohexanoate + H(2)O + NAD(+) = (S)-5-amino-3- CA oxohexanoate + NH(3) + NADH. // ID 1.4.1.12 DE 2,4-diaminopentanoate dehydrogenase. CA 2,4-diaminopentanoate + H(2)O + NAD(P)(+) = 2-amino-4-oxopentanoate + CA NH(3) + NAD(P)H. CC -!- Also acts, more slowly, on 2,5-diaminohexanoate forming 2-amino-5- CC oxohexanoate, which then cyclizes non-enzymically to 1-pyrroline-2- CC methyl-5-carboxylate. // ID 1.4.1.13 DE Glutamate synthase (NADPH). AN GOGAT. AN L-glutamate synthase. AN L-glutamate synthetase. AN NADPH-glutamate synthase. AN Glutamate (reduced nicotinamide adenine dinucleotide phosphate) synthase. AN Glutamate synthetase (NADP). AN NADPH-dependent glutamate synthase. AN Glutamine-ketoglutaric aminotransferase. AN Glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP). AN L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing. CA 2 L-glutamate + NADP(+) = L-glutamine + 2-oxoglutarate + NADPH. CF Iron-sulfur; FAD; FMN. CC -!- Formerly EC 2.6.1.53. DR Q12680, GLT1_YEAST; Q05755, GLTB_AZOBR; P39812, GLTB_BACSU; DR P09831, GLTB_ECOLI; Q05756, GLTD_AZOBR; P09832, GLTD_ECOLI; // ID 1.4.1.14 DE Glutamate synthase (NADH). AN L-glutamate synthase. AN L-glutamate synthetase. AN NADH-glutamate synthase. AN NADH-dependent glutamate synthase. CA 2 L-glutamate + NAD(+) = L-glutamine + 2-oxoglutarate + NADH. CF FMN. DR Q03460, GLSN_MEDSA; // ID 1.4.1.15 DE Lysine dehydrogenase. CA L-lysine + NAD(+) = 1,2-didehydropiperidine-2-carboxylate + NH(3) + NADH. // ID 1.4.1.16 DE Diaminopimelate dehydrogenase. AN Meso-diaminopimelate D-dehydrogenase. CA Meso-2,6-diaminoheptanedioate + H(2)O + NADP(+) = L-2-amino-6- CA oxoheptanedioate + NH(3) + NADPH. DR P04964, DDH_CORGL ; // ID 1.4.1.17 DE N-methylalanine dehydrogenase. CA N-methyl-L-alanine + H(2)O + NADP(+) = pyruvate + methylamine + NADPH. // ID 1.4.1.18 DE Lysine 6-dehydrogenase. CA L-lysine + NAD(+) = allysine + NADH. CC -!- The product is spontaneously converted into 1,6-didehydropiperidine- CC 2-carboxylate. // ID 1.4.1.19 DE Tryptophan dehydrogenase. AN L-tryptophan dehydrogenase. AN L-Trp-dehydrogenase. AN TrpDH. CA L-tryptophan + NAD(P)(+) = (indol-3-yl)pyruvate + NH(3) + NAD(P)H. CF Calcium. // ID 1.4.1.20 DE Phenylalanine dehydrogenase. AN L-phenylalanine dehydrogenase. AN PheDH. CA L-phenylalanine + H(2)O + NAD(+) = phenylpyruvate + NH(3) + NADH. CC -!- The enzyme from Bacillus badius and Sporosarcina ureae are highly CC specific for L-phenylalanine, that from Bacillus sphaericus also CC acts on L-tyrosine. PR PROSITE; PDOC00071; DR Q59224, DHPH_BACBA; P23307, DHPH_BACSH; P97014, DHPH_SPOUR; DR P22823, DHPH_THEIN; // ID 1.4.2.1 DE Glycine dehydrogenase (cytochrome). AN Glycine-cytochrome c reductase. CA Glycine + H(2)O + 2 ferricytochrome c = glyoxylate + NH(3) + CA 2 ferrocytochrome c. // ID 1.4.3.1 DE D-aspartate oxidase. AN Aspartic oxidase. CA D-aspartate + H(2)O + O(2) = oxaloacetate + NH(3) + H(2)O(2). CF FAD. PR PROSITE; PDOC00573; DR P31228, OXDD_BOVIN; Q99489, OXDD_HUMAN; // ID 1.4.3.2 DE L-amino acid oxidase. AN Ophio-amino-acid oxidase. CA An L-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2). CF FAD. DR P81382, OXLA_AGKRH; O93364, OXLA_CROAD; P56742, OXLA_CROAT; DR P23623, OXLA_NEUCR; P81383, OXLA_OPHHA; P81375, OXLA_VIPLE; // ID 1.4.3.3 DE D-amino acid oxidase. CA A D-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2). CF FAD. CC -!- Wide specificity for D-amino acids. CC -!- Also acts on glycine. PR PROSITE; PDOC00573; DR Q19564, OXDA_CAEEL; P24552, OXDA_FUSSO; P14920, OXDA_HUMAN; DR P18894, OXDA_MOUSE; P00371, OXDA_PIG ; P22942, OXDA_RABIT; DR O35078, OXDA_RAT ; P80324, OXDA_RHOTO; Q99042, OXDA_TRIVR; // ID 1.4.3.4 DE Amine oxidase (flavin-containing). AN Monoamine oxidase. AN Tyramine oxidase. AN Tyraminase. AN Amine oxidase. AN Adrenalin oxidase. CA RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2). CF FAD. CC -!- Acts on primary amines, and usually also on secondary and tertiary CC amines. CC -!- Formerly EC 1.4.3.9. DR P21398, AOFA_BOVIN; P58027, AOFA_CANFA; P21397, AOFA_HUMAN; DR Q64133, AOFA_MOUSE; P21396, AOFA_RAT ; O18851, AOFA_SHEEP; DR P56560, AOFB_BOVIN; P58028, AOFB_CAVPO; P27338, AOFB_HUMAN; DR P19643, AOFB_RAT ; P46882, AOFN_ASPNG; P49253, AOF_ONCMY ; // ID 1.4.3.5 DE Pyridoxamine-phosphate oxidase. AN Pyridoxamine 5'-phosphate oxidase. CA Pyridoxamine 5'-phosphate + H(2)O + O(2) = pyridoxal 5'-phosphate + CA NH(3) + H(2)O(2). CF FMN. CC -!- Also oxidizes pyridoxine 5-phosphate and pyridoxine. PR PROSITE; PDOC00815; DR Q9UTQ1, PDX3_SCHPO; P38075, PDX3_YEAST; Q20939, PDXH_CAEEL; DR P28225, PDXH_ECOLI; P44909, PDXH_HAEIN; O33065, PDXH_MYCLE; DR O06207, PDXH_MYCTU; P21159, PDXH_MYXXA; P74211, PDXH_SYNY3; // ID 1.4.3.6 DE Amine oxidase (copper-containing). AN Diamine oxidase. AN DAO. AN Diamino oxhydrase. AN Histaminase. CA RCH(2)NH(2) + H(2)O + O(2) = RCHO + NH(3) + H(2)O(2). CF Topaquinone; Copper. CC -!- A group of enzymes including those oxidizing primary amines, diamines CC and histamine. CC -!- One form of EC 1.3.1.15 from rat kidney also catalyzes this CC reaction. PR PROSITE; PDOC00895; DR P19801, ABP_HUMAN ; Q9TRC7, ABP_PIG ; P36633, ABP_RAT ; DR Q07121, AMO1_ARTS1; Q12556, AMO1_ASPNG; Q07123, AMO2_ARTS1; DR Q59118, AMOH_ARTGO; P46883, AMO_ECOLI ; P49250, AMO_KLEAE ; DR P80695, AMO_KLEOX ; P49252, AMO_LENCU ; Q43077, AMO_PEA ; DR P12807, AMO_PICAN ; O75106, AOC2_HUMAN; Q16853, AOC3_HUMAN; DR O70423, AOC3_MOUSE; O08590, AOC3_RAT ; Q29437, AOCX_BOVIN; DR O46406, AOCY_BOVIN; P46881, PAOX_ARTGO; // ID 1.4.3.7 DE D-glutamate oxidase. AN D-glutamic oxidase. CA D-glutamate + H(2)O + O(2) = 2-oxoglutarate + NH(3) + H(2)O(2). // ID 1.4.3.8 DE Ethanolamine oxidase. CA Ethanolamine + H(2)O + O(2) = glycolaldehyde + NH(3) + H(2)O(2). CF Cobalt. // ID 1.4.3.9 DE Transferred entry: 1.4.3.4. // ID 1.4.3.10 DE Putrescine oxidase. CA Putrescine + O(2) + H(2)O = 4-aminobutanal + NH(3) + H(2)O(2). CF FAD. CC -!- 4-aminobutanal condenses non-enzymically to 1-pyrroline. DR P40974, PUO_MICRU ; // ID 1.4.3.11 DE L-glutamate oxidase. CA L-glutamate + O(2) + H(2)O = 2-oxoglutarate + NH(3) + H(2)O(2). CF FAD. CC -!- The enzyme from Azotobacter previously listed under this number, CC which did not produce H(2)O(2), was a crude cell-free extract which CC probably contained catalase. // ID 1.4.3.12 DE Cyclohexylamine oxidase. CA Cyclohexylamine + O(2) + H(2)O = cyclohexanone + NH(3) + H(2)O(2). CF FAD. CC -!- Some other cyclic amines can act instead of cyclohexylamine, but not CC simple aliphatic and aromatic amides. // ID 1.4.3.13 DE Protein-lysine 6-oxidase. AN Lysyl oxidase. CA Peptidyl-L-lysyl-peptide + H(2)O + O(2) = peptidyl-allysyl-peptide + CA NH(3) + H(2)O(2). CC -!- Also acts on protein 5-hydroxylysine. DI Cutis laxa (Ehlers-Danlos syndrome IX); MIM:304150. PR PROSITE; PDOC00716; DR P33072, LYOX_BOVIN; Q05063, LYOX_CHICK; P28300, LYOX_HUMAN; DR P28301, LYOX_MOUSE; P45845, LYOX_PIG ; P16636, LYOX_RAT ; // ID 1.4.3.14 DE L-lysine oxidase. CA L-lysine + O(2) + H(2)O = 6-amino-2-oxo-hexanoate + NH(3) + H(2)O(2). CF FAD. CC -!- Also acts, more slowly, on L-ornithine, L-phenylalanine, L-arginine, CC and L-histidine. DI Lysine intolerance; MIM:247900. // ID 1.4.3.15 DE D-glutamate(D-aspartate) oxidase. CA D-glutamate + H(2)O + O(2) = 2-oxoglutarate + NH(3) + H(2)O(2). CF FAD. CC -!- D-glutamate and D-aspartate are oxidized at the same rate. Other CC D-monoaminodicarboxylates, and other D- and L-amino acids, are not CC oxidized. // ID 1.4.3.16 DE L-aspartate oxidase. CA L-aspartate + H(2)O + O(2) = oxaloacetate + NH(3) + H(2)O(2). CF FAD. CC -!- A component of the bacterial quinolinate synthase system. DR Q8XWM7, NAB1_RALSO; Q8XQG4, NAB2_RALSO; Q8U8J4, NADB_AGRT5; DR Q8YXJ6, NADB_ANASP; O66973, NADB_AQUAE; Q9KDJ5, NADB_BACHD; DR P38032, NADB_BACSU; Q9A4C3, NADB_CAUCR; Q97K95, NADB_CLOAB; DR Q8XNE2, NADB_CLOPE; Q8XA23, NADB_ECO57; P10902, NADB_ECOLI; DR Q9HNZ0, NADB_HALN1; Q929Z2, NADB_LISIN; Q8Y5N4, NADB_LISMO; DR Q49617, NADB_MYCLE; O06595, NADB_MYCTU; Q9JSX4, NADB_NEIMA; DR Q9K107, NADB_NEIMB; Q51363, NADB_PSEAE; Q9V2R0, NADB_PYRAB; DR Q8TZL4, NADB_PYRFU; O57765, NADB_PYRHO; Q98AV8, NADB_RHILO; DR Q92R32, NADB_RHIME; Q59767, NADB_RHORU; Q8Z4K0, NADB_SALTI; DR Q8ZMX9, NADB_SALTY; Q9X8N8, NADB_STRCO; Q97ZC5, NADB_SULSO; DR Q972D2, NADB_SULTO; P74562, NADB_SYNY3; Q9KPA4, NADB_VIBCH; DR Q9PC57, NADB_XYLFA; Q87D19, NADB_XYLFT; Q8ZD80, NADB_YERPE; // ID 1.4.3.17 DE Tryptophan alpha,beta-oxidase. AN L-tryptophan alpha,beta-dehydrogenase. AN L-tryptophan 2',3'-oxidase. CA L-tryptophan + O(2) = alpha,beta-didehydrotryptophan + H(2)O(2). CF Heme. CC -!- The enzyme from Chromobacterium violaceum is specific for CC tryptophan derivatives possessing its carboxyl group free or as CC an amide or ester, and an unsubstituted indole ring. CC -!- The enzyme also catalyzes the alpha,beta dehydrogenation of CC L-tryptophan side chains in peptides. // ID 1.4.3.18 DE Deleted entry. // ID 1.4.3.19 DE Glycine oxidase. CA (1) glycine + H(2)O + O(2) = glyoxylate + NH(3) + H(2)O(2). CA (2) D-alanine + H(2)O + O(2) = pyruvate + NH(3) + H(2)O(2). CA (3) sarcosine + H(2)O + O(2) = glyoxylate + methylamine + H(2)O(2). CA (4) N-ethylglycine + H(2)O + O(2) = glyoxylate + ethylamine + H(2)O(2). CF FAD. CC -!- The enzyme from Bacillus subtilis is active with glycine, CC sarcosine, N-ethylglycine, D-alanine, D-a-aminobutyrate, D-proline, CC D-pipecolate and N-methyl-D-alanine. CC -!- It differs from EC 1.4.3.3 due to its activity on sarcosine and CC D-pipecolate. DR O31616, GLOX_BACSU; // ID 1.4.4.1 DE Transferred entry: 1.21.4.1. // ID 1.4.4.2 DE Glycine dehydrogenase (decarboxylating). AN Glycine decarboxylase. AN Glycine cleavage system P-protein. CA Glycine + lipoylprotein = S-aminomethyldihydrolipoylprotein + CO(2). CF Pyridoxal-phosphate. CC -!- Lipoamide can also act as acceptor. CC -!- A component, with EC 2.1.2.10, of the glycine cleavage system, CC previously known as glycine synthase. DI Nonketotic hyperglycinemia type II; MIM:238310. DR P54376, GCS1_BACSU; P54377, GCS2_BACSU; P49361, GCSA_FLAPR; DR P49362, GCSB_FLAPR; O80988, GCSP_ARATH; P15505, GCSP_CHICK; DR P33195, GCSP_ECOLI; O49850, GCSP_FLAAN; O49852, GCSP_FLATR; DR P23378, GCSP_HUMAN; Q50601, GCSP_MYCTU; P26969, GCSP_PEA ; DR Q09785, GCSP_SCHPO; O49954, GCSP_SOLTU; P49095, GCSP_YEAST; // ID 1.4.7.1 DE Glutamate synthase (ferredoxin). AN Ferredoxin-dependent glutamate synthase. CA 2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + CA 2 reduced ferredoxin. CF Iron-sulfur; Flavoprotein. DR Q9ZNZ7, GLS1_ARATH; Q9T0P4, GLS2_ARATH; Q06434, GLSF_ANTSP; DR O19906, GLSF_CYACA; Q08258, GLSF_HORVU; P23225, GLSF_MAIZE; DR P51375, GLSF_PORPU; Q43155, GLSF_SPIOL; P55037, GLTB_SYNY3; DR P55038, GLTS_SYNY3; // ID 1.4.99.1 DE D-amino-acid dehydrogenase. CA A D-amino acid + H(2)O + acceptor = a 2-oxo acid + NH(3) + reduced CA acceptor. CF FAD. CC -!- Acts to some extent on all D-amino acids except D-aspartate and CC D-glutamate. DR Q9HTQ0, DAD1_PSEAE; Q8Y0W7, DAD1_RALSO; Q98F08, DAD1_RHILO; DR Q9HU99, DAD2_PSEAE; Q8XX54, DAD2_RALSO; Q98B75, DAD2_RHILO; DR Q981X2, DAD3_RHILO; P58739, DADA_AGRT5; Q8YD04, DADA_BRUME; DR P29011, DADA_ECOLI; O30745, DADA_KLEAE; Q9JX24, DADA_NEIMA; DR Q9K1H5, DADA_NEIMB; Q9RAE6, DADA_RHILV; Q8Z687, DADA_SALTI; DR Q8ZP17, DADA_SALTY; Q9KTV1, DADA_VIBCH; Q8PGC9, DADA_XANAC; DR Q8P4Q9, DADA_XANCP; Q9PF27, DADA_XYLFA; Q87AK0, DADA_XYLFT; DR Q8ZEL7, DADA_YERPE; // ID 1.4.99.2 DE Taurine dehydrogenase. CA Taurine + H(2)O + acceptor = sulfoacetaldehyde + NH(3) + reduced CA acceptor. // ID 1.4.99.3 DE Amine dehydrogenase. AN Methylamine dehydrogenase. AN Primary-amine dehydrogenase. AN MADH. CA RCH(2)NH(2) + H(2)O + acceptor = RCHO + NH(3) + reduced acceptor. CF Tryptophan tryptophylquinone (TTQ). DR Q49124, DHMH_METEX; Q50420, DHMH_METFL; Q59542, DHMH_METME; DR P29894, DHMH_PARDE; P23006, DHMH_PARVE; P00372, DHML_METEX; DR Q50425, DHML_METFL; Q59543, DHML_METME; P22619, DHML_PARDE; DR P22641, DHML_PARVE; // ID 1.4.99.4 DE Aralkylamine dehydrogenase. AN Aromatic amine dehydrogenase. CA RCH(2)NH(2) + H(2)O + acceptor = RCHO + NH(3) + reduced acceptor. CC -!- Phenazine methosulfate can act as acceptor. CC -!- Acts on aromatic amines and, more slowly, on some long-chain CC aliphatic amines, but not on methylamine or ethylamine (cf. CC EC 1.4.99.3). // ID 1.4.99.5 DE Glycine dehydrogenase (cyanide-forming). AN Hydrogen cyanide synthase. AN HCN synthase. CA Glycine + 2 A = HCN + CO(2) + 2 AH(2). CF FAD. CC -!- The enzyme is membrane-bound, and the 2-electron acceptor is a CC component of the respiratory chain. CC -!- The enzyme can act with various artificial electron acceptors, CC including phenazine methosulfate. // ID 1.5.1.1 DE Pyrroline-2-carboxylate reductase. CA L-proline + NAD(P)(+) = 1-pyrroline-2-carboxylate + NAD(P)H. CC -!- Reduces 1-pyrroline-2-carboxylate to L-proline and also CC 1,2-didehydropiperidine-2-carboxylate to L-pipecolate. // ID 1.5.1.2 DE Pyrroline-5-carboxylate reductase. AN P5CR. CA L-proline + NAD(P)(+) = 1-pyrroline-5-carboxylate + NAD(P)H. CC -!- Also reduces 1-pyrroline-3-hydroxy-5-carboxylate to L-hydroxyproline. PR PROSITE; PDOC00451; DR O04016, PROC_ACTCH; O66553, PROC_AQUAE; P54904, PROC_ARATH; DR Q20848, PROC_CAEEL; P46540, PROC_CORGL; P00373, PROC_ECOLI; DR P43869, PROC_HAEIN; Q9ZK56, PROC_HELPJ; O25773, PROC_HELPY; DR P32322, PROC_HUMAN; Q9HH99, PROC_METAC; P22350, PROC_METSM; DR P46725, PROC_MYCLE; Q11141, PROC_MYCTU; Q12641, PROC_NEUCR; DR Q9CPE8, PROC_PASMU; Q04708, PROC_PEA ; P22008, PROC_PSEAE; DR Q9P7Y7, PROC_SCHPO; P17817, PROC_SOYBN; P74572, PROC_SYNY3; DR P54893, PROC_THETH; P27771, PROC_TREPA; P52053, PROC_VIBAL; DR P32263, PROC_YEAST; Q12740, PROC_ZALAR; Q00777, PROG_BACSU; DR P14383, PROH_BACSU; P54552, PROI_BACSU; // ID 1.5.1.3 DE Dihydrofolate reductase. AN Tetrahydrofolate dehydrogenase. CA 5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH. CC -!- The enzyme from animals and some micro-organisms also slowly reduces CC folate to 5,6,7,8-tetrahydrofolate. CC -!- Formerly EC 1.5.1.4. PR PROSITE; PDOC00072; DR Q05762, DRT1_ARATH; Q05763, DRT2_ARATH; Q23695, DRTS_CRIFA; DR P45350, DRTS_DAUCA; P16126, DRTS_LEIAM; P07382, DRTS_LEIMA; DR O81395, DRTS_MAIZE; Q27828, DRTS_PARTE; Q27713, DRTS_PLABA; DR P20712, DRTS_PLACH; P13922, DRTS_PLAFK; O02604, DRTS_PLAVI; DR P46103, DRTS_PLAVN; P51820, DRTS_SOYBN; Q07422, DRTS_TOXGO; DR Q27783, DRTS_TRYBB; Q27793, DRTS_TRYCR; P00383, DY21_ECOLI; DR P00384, DY22_ECOLI; P05794, DY23_ECOLI; P00382, DYR1_ECOLI; DR P12833, DYR3_SALTY; P11731, DYR5_ECOLI; P95524, DYR6_PROMI; DR P27422, DYR7_ECOLI; Q57452, DYR8_ECOLI; Q59397, DYR9_ECOLI; DR Q04515, DYRA_ECOLI; P13955, DYRA_STAAU; P10167, DYRB_STAAM; DR Q59408, DYRC_ECOLI; P78218, DYRF_ECOLI; P28019, DYR_AEDAL ; DR P11045, DYR_BACSU ; P00376, DYR_BOVIN ; P04382, DYR_BPT4 ; DR P57243, DYR_BUCAI ; Q8K9Z8, DYR_BUCAP ; Q93341, DYR_CAEEL ; DR P22906, DYR_CANAL ; P00378, DYR_CHICK ; P31073, DYR_CITFR ; DR Q07801, DYR_CRYNE ; P17719, DYR_DROME ; P00379, DYR_ECOLI ; DR O62583, DYR_ENCCU ; P31074, DYR_ENTAE ; P00380, DYR_ENTFC ; DR P43791, DYR_HAEIN ; P15093, DYR_HALVO ; Q9U8B8, DYR_HELVI ; DR P27421, DYR_HSVS7 ; P09503, DYR_HSVSA ; P22573, DYR_HSVSC ; DR P00374, DYR_HUMAN ; P27498, DYR_KLEAE ; P00381, DYR_LACCA ; DR Q59487, DYR_LACLA ; P04753, DYR_MESAU ; P00375, DYR_MOUSE ; DR P47470, DYR_MYCGE ; Q9CBW1, DYR_MYCLE ; P78028, DYR_MYCPN ; DR Q98Q32, DYR_MYCPU ; O33305, DYR_MYCTU ; P04174, DYR_NEIGO ; DR Q9JSQ9, DYR_NEIMA ; Q9K168, DYR_NEIMB ; P00377, DYR_PIG ; DR P16184, DYR_PNECA ; P36591, DYR_SCHPO ; Q59908, DYR_STAEP ; DR Q54277, DYR_STAHA ; Q54801, DYR_STRPN ; Q60034, DYR_THEMA ; DR Q9PR30, DYR_UREPA ; P07807, DYR_YEAST ; // ID 1.5.1.4 DE Transferred entry: 1.5.1.3. // ID 1.5.1.5 DE Methylenetetrahydrofolate dehydrogenase (NADP+). CA 5,10-methylenetetrahydrofolate + NADP(+) = CA 5,10-methenyltetrahydrofolate + NADPH. PR PROSITE; PDOC00616; DR P11586, C1TC_HUMAN; P27653, C1TC_RAT ; P07245, C1TC_YEAST; DR P09440, C1TM_YEAST; P54382, FOLD_BACSU; P57557, FOLD_BUCAI; DR Q8K979, FOLD_BUCAP; Q9PKW1, FOLD_CHLMU; Q9Z8K3, FOLD_CHLPN; DR O84081, FOLD_CHLTR; P24186, FOLD_ECOLI; P44313, FOLD_HAEIN; DR Q9ZLQ4, FOLD_HELPJ; P56467, FOLD_HELPY; P47259, FOLD_MYCGE; DR P75096, FOLD_MYCPN; P51696, FOLD_PHOPO; Q9ZD32, FOLD_RICPR; DR Q60006, FOLD_SALTI; P58688, FOLD_SALTY; P96050, FOLD_STRTR; DR Q05213, FOLD_THEAC; P55818, MTDA_METEX; // ID 1.5.1.6 DE Formyltetrahydrofolate dehydrogenase. AN 10-formyltetrahydrofolate dehydrogenase. CA 10-formyltetrahydrofolate + NADP(+) + H(2)O = tetrahydrofolate + CO(2) + CA NADPH. PR PROSITE; PDOC00068; DR O75891, FTDH_HUMAN; Q8R0Y6, FTDH_MOUSE; P28037, FTDH_RAT ; // ID 1.5.1.7 DE Saccharopine dehydrogenase (NAD+, L-lysine forming). AN Lysine--2-oxoglutarate reductase. CA N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD(+) + H(2)O = L-lysine + CA 2-oxoglutarate + NADH. DI Saccharopinuria; MIM:268700. DR P43065, LYS1_CANAL; Q09694, LYS1_SCHPO; P38997, LYS1_YARLI; DR P38998, LYS1_YEAST; // ID 1.5.1.8 DE Saccharopine dehydrogenase (NADP+, L-lysine forming). CA N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP(+) + H(2)O = L-lysine + CA 2-oxoglutarate + NADPH. // ID 1.5.1.9 DE Saccharopine dehydrogenase (NAD+, L-glutamate forming). CA N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NAD(+) + H(2)O = L-glutamate + CA 2-aminoadipate 6-semialdehyde + NADH. // ID 1.5.1.10 DE Saccharopine dehydrogenase (NADP+, L-glutamate forming). AN Saccharopine reductase. CA N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP(+) + H(2)O = L-glutamate + CA 2-aminoadipate 6-semialdehyde + NADPH. DR Q9P4R4, LYS9_MAGGR; P38999, LYS9_YEAST; // ID 1.5.1.11 DE D-octopine dehydrogenase. AN D-octopine synthase. CA N(2)-(D-1-carboxyethyl)-L-arginine + NAD(+) + H(2)O = L-arginine + CA pyruvate + NADH. CC -!- Also acts, in the reverse direction, on L-ornithine, L-lysine and CC L-histidine. DR P00385, DHLO_AGRT4; P94210, DHLO_AGRVI; // ID 1.5.1.12 DE 1-pyrroline-5-carboxylate dehydrogenase. CA 1-pyrroline-5-carboxylate + NAD(+) + H(2)O = L-glutamate + NADH. CC -!- Oxidizes other 1-pyrrolines, e.g. 3-hydroxy-1-pyrroline-5- CC carboxylate forms 4-hydroxyglutamate. DI Hyperprolinemia II; MIM:239510. PR PROSITE; PDOC00068; DR P78568, PUT2_AGABI; Q9P8I0, PUT2_EMENI; P30038, PUT2_HUMAN; DR O74766, PUT2_SCHPO; P07275, PUT2_YEAST; P09546, PUTA_ECOLI; DR O52485, PUTA_KLEAE; P23725, PUTA_KLEPN; P95629, PUTA_RHIME; DR P10503, PUTA_SALTY; P39634, ROCA_BACSU; // ID 1.5.1.13 DE Nicotinate dehydrogenase. CA Nicotinate + H(2)O + NADP(+) = 6-hydroxynicotinate + NADPH. CF Flavoprotein; Iron. CC -!- Also oxidizes NADPH. // ID 1.5.1.14 DE Transferred entry: 1.5.1.21. // ID 1.5.1.15 DE Methylenetetrahydrofolate dehydrogenase (NAD+). CA 5,10-methylenetetrahydrofolate + NAD(+) = CA 5,10-methenyltetrahydrofolate + NADH. PR PROSITE; PDOC00616; DR Q02046, MTD1_YEAST; Q04448, MTDC_DROME; P13995, MTDC_HUMAN; DR P18155, MTDC_MOUSE; // ID 1.5.1.16 DE D-lysopine dehydrogenase. AN D-lysopine synthase. CA N(2)-(D-1-carboxyethyl)-L-lysine + NADP(+) + H(2)O = L-lysine + pyruvate CA + NADPH. CC -!- In the reverse reaction, a number of L-amino acids can act instead of CC L-lysine, and 2-oxobutanoate and, to a lesser extent, glyoxylate, can CC act instead of pyruvate. DR P00385, DHLO_AGRT4; P94210, DHLO_AGRVI; // ID 1.5.1.17 DE Alanopine dehydrogenase. CA 2,2'-iminodipropanoate + NAD(+) + H(2)O = L-alanine + pyruvate + NADH. CC -!- In the reverse reaction, L-alanine can be replaced by L-cysteine, CC L-serine, or L-threonine; glycine acts very slowly (cf. EC 1.5.1.22). // ID 1.5.1.18 DE Ephedrine dehydrogenase. CA (-)-ephedrine + NAD(+) = (R)-2-methylimino-1-phenylpropan-1-ol + NADH. CC -!- The product immediately hydrolyzes to methylamine and 1-hydroxy-1- CC phenylpropan-2-one. CC -!- Acts on a number of related compounds including (-)-sympatol, CC (+)-pseudoephedrine and (+)-norephedrine. // ID 1.5.1.19 DE D-nopaline dehydrogenase. AN D-nopaline synthase. AN Nopaline synthase. CA N(2)-(D-1,3-dicarboxypropyl)-L-arginine + NADP(+) + H(2)O = L-arginine + CA 2-oxoglutarate + NADPH. CC -!- In the reverse direction, forms D-nopaline from L-arginine and CC D-ornaline from L-ornithine. DR P00386, DHNO_AGRT7; Q44524, DHNO_AGRVI; // ID 1.5.1.20 DE Methylenetetrahydrofolate reductase (NADPH). AN MTHFR. CA 5-methyltetrahydrofolate + NADP(+) = 5,10-methylenetetrahydrofolate + CA NADPH. CF FAD. CC -!- Formerly EC 1.1.1.171. DI Homocystinuria II (MTHFR deficiency); MIM:236250. DR O80585, MTHR_ARATH; Q17693, MTHR_CAEEL; P42898, MTHR_HUMAN; DR Q9WU20, MTHR_MOUSE; Q10258, MTHR_SCHPO; P46151, MTHR_YEAST; DR O74927, MTHS_SCHPO; P53128, MTHS_YEAST; // ID 1.5.1.21 DE Delta(1)-piperideine-2-carboxylate reductase. CA L-pipecolate + NADP(+) = delta(1)-piperideine-2-carboxylate + NADPH. CC -!- Formerly EC 1.5.1.14. // ID 1.5.1.22 DE Strombine dehydrogenase. CA N-(carboxymethyl)-D-alanine + NAD(+) + H(2)O = glycine + pyruvate + NADH. CC -!- Catalyzes the reaction of EC 1.5.1.17, more slowly. CC -!- Does not act on L-strombine. // ID 1.5.1.23 DE Tauropine dehydrogenase. CA Tauropine + NAD(+) + H(2)O = taurine + pyruvate + NADH. CC -!- In the reverse reaction, alanine can act instead of taurine, more CC slowly, and 2-oxobutanoate and 2-oxopentanoate can act instead of CC pyruvate. // ID 1.5.1.24 DE N(5)-(carboxyethyl)ornithine synthase. CA N(5)-(L-1-carboxyethyl)-L-ornithine + NADP(+) + H(2)O = L-ornithine + CA pyruvate + NADPH. CC -!- In the reverse direction L-lysine can act instead of L-ornithine, CC more slowly. Acts on the amino group (cf. EC 1.5.1.16). DR Q9CG73, CEO1_LACLA; P15244, CEO2_LACLA; // ID 1.5.1.25 DE Thiomorpholine-carboxylate dehydrogenase. AN Ketimine reductase. CA Thiomorpholine-3-carboxylate + NAD(P)(+) = 3,4-dehydro-1,4- CA thiomorpholine-3-carboxylate + NAD(P)H. CC -!- The product is the cyclic imine of the 2-oxoacid corresponding to CC S-(2-aminoethyl)cysteine. CC -!- In the reverse direction, a number of other cyclic unsaturated CC compounds can act as substrates, more slowly. // ID 1.5.1.26 DE Beta-alanopine dehydrogenase. CA Beta-alanopine + NAD(+) + H(2)O = beta-alanine + pyruvate + NADH. // ID 1.5.1.27 DE 1,2-dehydroreticulinium reductase (NADPH). AN 1,2-dehydroreticulinium ion reductase. CA 1,2-dehydroreticulinium + NADPH = (R)-reticuline + NADP(+). CC -!- Stereospecifically reduces the 1,2-dehydroreticulinium ion to CC (R)-reticuline, which is a direct precursor of morphinan alkaloids CC in the poppy plant, papaver somniferum. CC -!- The enzyme does not catalyze the reverse reaction to any significant CC extent under physiological conditions. // ID 1.5.1.28 DE Opine dehydrogenase. CA (2S)-2-{[1-(R)-carboxyethyl]amino}pentanoate + NAD(+) + H(2)O = L-2- CA aminopentanoic acid + pyruvate + NADH. CC -!- In the forward direction, the enzyme from Arthrobacter sp. acts also CC on secondary amine dicarboxylates such as N-(1- CC carboxyethyl)methionine and N-(1-carboxyethyl)phenylalanine. CC -!- Dehydrogenation forms an imine, which dissociates to the amino acid CC and pyruvate. CC -!- In the reverse direction, the enzyme acts also on neutral amino acids CC as an amino donor. They include L-amino acids such as CC 2-aminopentanoic acid, 2-aminobutyric acid, 2-aminohexanoic acid, CC 3-chloroalanine, O-acetylserine, methionine, isoleucine, valine, CC phenylalanine, leucine and alanine. CC -!- The amino acceptors include 2-oxoacids such as pyruvate, CC oxaloacetate, glyoxylate and 2-oxobutyrate. DR Q44297, ODH_ARTSP ; // ID 1.5.1.29 DE FMN reductase. AN NAD(P)H dehydrogenase (FMN). AN NAD(P)H:flavin oxidoreductase. AN Riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide AN (phosphate)) reductase. AN Flavin mononucleotide reductase. AN Flavine mononucleotide reductase. AN NAD(P)H-FMN reductase. AN NAD(P)H:FMN oxidoreductase. AN Riboflavin mononucleotide reductase. AN Riboflavine mononucleotide reductase. AN NAD(P)H:FMN oxidoreductase. AN NAD(P)H-dependent FMN reductase. AN NAD(P)H:flavin oxidoreductase. AN NAD(P)H(2) dehydrogenase (FMN). AN NAD(P)H(2):FMN oxidoreductase. CA FMNH(2) + NAD(P)(+) = FMN + NAD(P)H. CC -!- The enzyme from luminescent bacteria and the SsuE enzyme from CC Escherichia coli also reduce riboflavin and FAD, but more slowly. CC -!- In E. coli, this enzyme, in conjunction with EC 1.14.14.5, forms CC a two-component alkanesulfonate monooxygenase, which allows for CC utilization of alkanesulfonates as sulfur sources under conditions CC of sulfate and cysteine starvation. CC -!- Formerly EC 1.6.8.1. DR P23486, FRE_ECOLI ; Q9L6L9, FRE_SALTY ; O31038, MSUE_PSEAE; DR P80644, SSUE_ECOLI; O85762, SSUE_PSEPU; // ID 1.5.1.30 DE Flavin reductase. AN NADPH dehydrogenase (flavin). AN NADPH:flavin oxidoreductase. AN Riboflavin mononucleotide (reduced nicotinamide adenine dinucleotide AN phosphate) reductase. AN Flavin mononucleotide reductase. AN Flavine mononucleotide reductase. AN FMN reductase (NADPH). AN NADPH-dependent FMN reductase. AN NADPH-flavin reductase. AN NADPH-FMN reductase. AN NADPH-specific FMN reductase. AN Riboflavin mononucleotide reductase. AN Riboflavine mononucleotide reductase. AN NADPH dehydrogenase (flavin). AN NADPH:riboflavin oxidoreductase. CA Reduced riboflavin + NADP(+) = riboflavin + NADPH. CC -!- The enzyme from Entamoeba histolytica reduces riboflavin and CC galactoflavin, and, more slowly, FMN and FAD. CC -!- NADH is oxidized more slowly than NADPH. CC -!- Formerly EC 1.6.8.2. DR P52556, FLRE_BOVIN; P30043, FLRE_HUMAN; // ID 1.5.1.31 DE Berberine reductase. AN (R)-canadine synthase. CA (R)-canadine + 2 NADP(+) = berberine + 2 NADPH. CC -!- Involved in alkaloid biosynthesis in Corydalis cava to give (R)- CC canadine with the opposite configuration to the precursor of CC berberine (see EC 1.3.3.8). CC -!- Also acts on 7,8-dihydroberberine. // ID 1.5.1.32 DE Vomilenine reductase. CA 1,2-dihydrovomilenine + NADP(+) = vomilenine + NADPH. CC -!- Forms part of the ajmaline biosynthesis pathway. // ID 1.5.3.1 DE Sarcosine oxidase. CA Sarcosine + H(2)O + O(2) = glycine + formaldehyde + H(2)O(2). CF FAD. CC -!- The flavin is both covalently and non-covalently bound in a molar CC ratio of 1:1. DR P40873, MSOX_ARTSP; P23342, MSOX_BACSN; P40859, MSOX_BACSP; DR P40854, MSOX_STRSQ; Q46337, SOXA_CORS1; O87386, SOXA_RHIME; DR P40875, SOXB_CORS1; O87388, SOXB_RHIME; Q52671, SOXB_RHOCA; DR Q46336, SOXD_CORS1; O87387, SOXD_RHIME; Q46338, SOXG_CORS1; DR Q9SJA7, SOX_ARATH ; Q18006, SOX_CAEEL ; Q9P0Z9, SOX_HUMAN ; DR Q9D826, SOX_MOUSE ; P79371, SOX_RABIT ; // ID 1.5.3.2 DE N-methyl-L-amino-acid oxidase. CA An N-methyl-L-amino acid + H(2)O + O(2) = an L-amino acid + formaldehyde CA + H(2)O(2). CF Flavoprotein. // ID 1.5.3.3 DE Deleted entry. // ID 1.5.3.4 DE N(6)-methyl-lysine oxidase. CA N(6)-methyl-L-lysine + H(2)O + O(2) = L-lysine + formaldehyde + CA H(2)O(2). // ID 1.5.3.5 DE (S)-6-hydroxynicotine oxidase. CA (S)-6-hydroxynicotine + H(2)O + O(2) = 1-(6-hydroxypyrid-3-yl)-4- CA (methylamino)butan-1-one + H(2)O(2). CF FAD. // ID 1.5.3.6 DE (R)-6-hydroxynicotine oxidase. CA (R)-6-hydroxynicotine + H(2)O + O(2) = 1-(6-hydroxypyrid-3-yl)-4- CA (methylamino)butan-1-one + H(2)O(2). CF FAD. PR PROSITE; PDOC00674; DR P08159, HDNO_ARTOX; // ID 1.5.3.7 DE L-pipecolate oxidase. CA L-pipecolate + O(2) = 2,3,4,5-tetrahydropyridine-2-carboxylate + CA H(2)O(2). CC -!- The product reacts with water to form 2-aminoadipate 6-semialdehyde, CC i.e. 2-amino-6-oxohexanoate. DR Q9P0Z9, SOX_HUMAN ; Q9D826, SOX_MOUSE ; P79371, SOX_RABIT ; // ID 1.5.3.8 DE Transferred entry: 1.3.3.8. // ID 1.5.3.9 DE Transferred entry: 1.21.3.3. // ID 1.5.3.10 DE Dimethylglycine oxidase. CA N,N-dimethylglycine + H(2)O + O(2) = sarcosine + formaldehyde + CA H(2)O(2). CF FAD. CC -!- Does not oxidize sarcosine. // ID 1.5.3.11 DE Polyamine oxidase. CA N(1)-acetylspermine + O(2) + H(2)O = N(1)-acetylspermidine + 3-amino- CA propanal + H(2)O(2). CF Iron; FAD. CC -!- Also acts on N(1)-acetylspermidine and N(1),N(12)- CC diacetylspermine. DR O64411, PAO_MAIZE ; // ID 1.5.3.12 DE Dihydrobenzophenanthridine oxidase. CA Dihydrosanguinarine + O(2) = sanguinarine + H(2)O(2). CF Copper. CC -!- Also catalyzes: dihydrochelirubine + O(2) = chelirubine + H(2)O(2). CC -!- Also catalyzes: dihydromacarpine + O(2) = macarpine + H(2)O(2). CC -!- Found in higher plants. CC -!- Produces oxidized forms of the benzophenanthridine alkaloids. // ID 1.5.4.1 DE Pyrimidodiazepine synthase. CA A pyrimidodiazepine + oxidized glutathione = 6-pyruvoyltetrahydropterin CA + 2 glutathione. CC -!- In the reverse direction of reaction, the reduction of CC 6-pyruvoyltetrahydropterin is accompanied by the opening of the CC 6-membered pyrazine ring and the formation of the 7-membered CC diazepine ring. The pyrimidodiazepine involved is an acetyldihydro CC derivative. CC -!- Involved in the formation of the eye pigment drosopterin in CC Drosophila melanogaster. // ID 1.5.5.1 DE Electron-transferring-flavoprotein dehydrogenase. AN Electron transfer flavoprotein-ubiquinone oxidoreductase. AN ETF-QO. AN ETF-ubiquinone oxidoreductase. AN ETF dehydrogenase. CA Reduced ETF + ubiquinone = ETF + ubiquinol. CF Iron-sulfur; FAD. CC -!- Forms part of the mitochondrial electron-transfer system. DR P94132, ETFD_ACICA; Q11190, ETFD_CAEEL; Q16134, ETFD_HUMAN; DR P55932, ETFD_PARDE; P55931, ETFD_PIG ; P87111, ETFD_SCHPO; DR Q08822, ETFD_YEAST; // ID 1.5.8.1 DE Dimethylamine dehydrogenase. AN DMADh. CA Dimethylamine + H(2)O + electron-transferring flavoprotein = CA methylamine + formaldehyde + reduced electron-transferring flavoprotein. CF FAD; Iron-sulfur. CC -!- Formerly EC 1.5.99.10. DR Q48303, DHDM_HYPSX; // ID 1.5.8.2 DE Trimethylamine dehydrogenase. AN TMADh. CA Trimethylamine + H(2)O + electron-transferring flavoprotein = CA dimethylamine + formaldehyde + reduced electron-transferring CA flavoprotein. CF FMN. CC -!- A number of alkyl-substituted derivatives of trimethylamine can also CC act as electron donors. CC -!- Phenazine methosulfate and 2,6-dichloroindophenol can act as CC electron acceptors. CC -!- Formerly EC 1.5.99.7. DR P16099, DHTM_METME; // ID 1.5.99.1 DE Sarcosine dehydrogenase. CA Sarcosine + acceptor + H(2)O = glycine + formaldehyde + reduced CA acceptor. CF FMN. DI Sarcosinemia; MIM:268900. // ID 1.5.99.2 DE Dimethylglycine dehydrogenase. CA N,N-dimethylglycine + acceptor + H(2)O = sarcosine + formaldehyde + CA reduced acceptor. CF FAD. DR Q9UI17, M2GD_HUMAN; Q63342, M2GD_RAT ; // ID 1.5.99.3 DE L-pipecolate dehydrogenase. CA L-pipecolate + acceptor = 2,3,4,5-tetrahydropyridine-2-carboxylate + CA reduced acceptor. CC -!- The product reacts with water to form 2-aminoadipate 6-semialdehyde, CC i.e. 2-amino-6-oxohexanoate. // ID 1.5.99.4 DE Nicotine dehydrogenase. CA Nicotine + acceptor + H(2)O = (S)-6-hydroxynicotine + reduced acceptor. CF FMN. CC -!- Acts on both (R)- and (S)-isomers. // ID 1.5.99.5 DE Methylglutamate dehydrogenase. CA N-methyl-L-glutamate + acceptor + H(2)O = L-glutamate + formaldehyde + CA reduced acceptor. CC -!- A number of N-methyl-substituted amino acids can act as donors. CC -!- 2,6-dichloroindophenol is the best acceptor. // ID 1.5.99.6 DE Spermidine dehydrogenase. CA Spermidine + acceptor + H(2)O = 1,3-diaminopropane + 4-aminobutanal + CA reduced acceptor. CF FAD; Heme. CC -!- Ferricyanide, 2,6-dichloroindophenol and cytochrome c can act as CC acceptor. CC -!- 4-aminobutanal condenses non-enzymically to 1-pyrroline. // ID 1.5.99.7 DE Transferred entry: 1.5.8.2. // ID 1.5.99.8 DE Proline dehydrogenase. CA L-proline + acceptor + H(2)O = (S)-1-pyrroline-5-carboxylate + reduced CA acceptor. CF FAD. PR PROSITE; PDOC00068; DR P09546, PUTA_ECOLI; O52485, PUTA_KLEAE; P23725, PUTA_KLEPN; DR P95629, PUTA_RHIME; P10503, PUTA_SALTY; // ID 1.5.99.9 DE Methylenetetrahydromethanopterin dehydrogenase. CA 5,10-methylenetetrahydromethanopterin + coenzyme F420 = CA 5,10-methenyltetrahydromethanopterin + reduced coenzyme F420. CC -!- Coenzyme F420 is a 7,8-didemethyl-8-hydroxy-5-deazariboflavin CC derivative; methanopterin is a pterin analog. CC -!- Involved in the formation of methane from CO(2) in Methanobacterium CC Thermoautotrophicum. DR O29544, MTD_ARCFU ; Q58441, MTD_METJA ; P94951, MTD_METKA ; DR Q50501, MTD_METTH ; P55300, MTD_METTM ; // ID 1.5.99.10 DE Transferred entry: 1.5.8.1. // ID 1.5.99.11 DE Coenzyme F420-dependent N(5),N(10)-methenyltetrahydromethanopterin DE reductase. AN H(2)-forming N(5),N(10)-methylenetetrahydromethanopterin AN dehydrogenase. AN H2-dependent methylene-H4MPT dehydrogenase. AN Methylene-H(4)MPT reductase. CA N(5),N(10)-methylenetetrahydromethanopterin + reduced coenzyme F420 = CA 5-methyl-5,6,7,8-tetrahydromethanopterin + coenzyme F420. CF Zinc. CC -!- Catalyzes an intermediate step in methanogenesis from CO(2) and CC H(2) in bacteria. DR Q58194, HMD_METJA ; Q02394, HMD_METKA ; Q50758, HMD_METTF ; DR O27211, HMD_METTH ; Q50759, HMD_METTL ; P32440, HMD_METTM ; DR P81221, HMD_METTW ; Q50840, HMD_METVO ; P32441, HMD_METWO ; // ID 1.5.99.12 DE Cytokinin dehydrogenase. CA N(6)-dimethylallyladenine + electron acceptor = adenine + CA 3-methylbut-2-enal + reduced electron acceptor + H(2)O. CF FAD. CC -!- Converts zeatin and related cytokinins. CC -!- Catalyzes the oxidation of cytokinins, a family of N(6)-substituted CC adenine derivatives that are plant hormones, where the substituent CC is a dimethylallyl or other prenyl group. CC -!- Although this activity was previously thought to be catalyzed by a CC hydrogen-peroxide-forming oxidase, this enzyme does not require CC oxygen for activity and does not form hydrogen peroxide. CC -!- 2,6-Dichloroindophenol, methylene blue, nitroblue tetrazolium, CC phenazine methosulfate and Cu(2+) in the presence of imidazole can CC act as acceptors. // ID 1.6.1.1 DE NAD(P)(+) transhydrogenase (B-specific). AN Pyridine nucleotide transhydrogenase. AN Nicotinamide nucleotide transhydrogenase. CA NADPH + NAD(+) = NADP(+) + NADH. CF FAD. CC -!- B-specific with respect to both NAD(+) and NADP(+). CC -!- Also acts with deamino coenzymes. PR PROSITE; PDOC00073; DR Q9XBQ9, STHA_AZOVI; Q8X727, STHA_ECO57; P27306, STHA_ECOLI; DR P71317, STHA_ERWCA; O07212, STHA_MYCTU; P57112, STHA_PSEAE; DR O05139, STHA_PSEFL; Q8XFP5, STHA_SALTY; P50529, STHA_VIBCH; DR Q8ZA97, STHA_YERPE; // ID 1.6.1.2 DE NAD(P)(+) transhydrogenase (AB-specific). AN Pyridine nucleotide transhydrogenase. AN Transhydrogenase. CA NADPH + NAD(+) = NADP(+) + NADH. CC -!- The enzyme from heart mitochondria is A-specific with respect to CC NAD(+) and B-specific with respect to NADP(+) (cf. EC 1.6.1.1.). PR PROSITE; PDOC00654; DR P11024, NNTM_BOVIN; Q13423, NNTM_HUMAN; Q61941, NNTM_MOUSE; DR Q60164, PNAA_RHORU; P41077, PNAA_RICPR; Q59764, PNAB_RHORU; DR P51995, PNAB_RICPR; P07001, PNTA_ECOLI; P43842, PNTA_HAEIN; DR P07002, PNTB_ECOLI; P43010, PNTB_HAEIN; Q59765, PNTB_RHORU; // ID 1.6.2.1 DE Transferred entry: 1.6.99.3. // ID 1.6.2.2 DE Cytochrome-b5 reductase. CA NADH + 2 ferricytochrome b5 = NAD(+) + 2 ferrocytochrome b5. CF FAD. DI Methemoglobinemia enzymopathic forms I, II, III; MIM:250800. DR P36060, MCR1_YEAST; P07514, NC5R_BOVIN; P00387, NC5R_HUMAN; DR P20070, NC5R_RAT ; P38626, NC5R_YEAST; // ID 1.6.2.3 DE Deleted entry. // ID 1.6.2.4 DE NADPH--ferrihemoprotein reductase. AN NADPH--cytochrome p450 reductase. AN TPNH(2) cytochrome c reductase. AN Ferrihemoprotein p450 reductase. CA NADPH + 2 ferricytochrome = NADP(+) + 2 ferrocytochrome. CF FMN; FAD. CC -!- Catalyzes the reduction of heme-thiolate-dependent monooxygenases CC such as EC 1.14.14.1, and is part of the microsomal hydroxylating CC system. CC -!- Also reduces cytochrome b5 and cytochrome c. DR Q9Y8G7, C505_FUSOX; P14779, CPXB_BACME; O08394, CYPD_BACSU; DR O08336, CYPE_BACSU; Q00141, NCPR_ASPNG; P50126, NCPR_CANMA; DR P37201, NCPR_CANTR; Q05001, NCPR_CATRO; P37039, NCPR_CAVPO; DR Q27597, NCPR_DROME; P16435, NCPR_HUMAN; P37040, NCPR_MOUSE; DR Q07994, NCPR_MUSDO; P37116, NCPR_PHAAU; P04175, NCPR_PIG ; DR P00389, NCPR_RABIT; P00388, NCPR_RAT ; P19618, NCPR_SALTR; DR P36587, NCPR_SCHPO; P16603, NCPR_YEAST; // ID 1.6.2.5 DE NADPH--cytochrome c2 reductase. CA NADPH + 2 ferricytochrome c2 = NADP(+) + 2 ferrocytochrome c2. CF FAD. // ID 1.6.2.6 DE Leghemoglobin reductase. CA NAD(P)H + 2 ferrileghemoglobin = NAD(P)(+) + 2 ferroleghemoglobin. // ID 1.6.4.1 DE Transferred entry: 1.8.1.6. // ID 1.6.4.2 DE Transferred entry: 1.8.1.7. // ID 1.6.4.3 DE Transferred entry: 1.8.1.4. // ID 1.6.4.4 DE Transferred entry: 1.8.1.8. // ID 1.6.4.5 DE Transferred entry: 1.8.1.9. // ID 1.6.4.6 DE Transferred entry: 1.8.1.10. // ID 1.6.4.7 DE Transferred entry: 1.8.1.11. // ID 1.6.4.8 DE Transferred entry: 1.8.1.12. // ID 1.6.4.9 DE Transferred entry: 1.8.1.13. // ID 1.6.4.10 DE Transferred entry: 1.8.1.14. // ID 1.6.5.1 DE Deleted entry. // ID 1.6.5.2 DE Transferred entry: 1.6.99.2. // ID 1.6.5.3 DE NADH dehydrogenase (ubiquinone). AN Ubiquinone reductase. AN Type 1 dehydrogenase. AN Complex 1 dehydrogenase. AN Coenzyme Q reductase. AN Complex I (electron transport chain). AN Complex I (mitochondrial electron transport). AN Complex I (NADH:Q1 oxidoreductase). AN Dihydronicotinamide adenine dinucleotide-coenzyme Q reductase. AN DPNH-coenzyme Q reductase. AN DPNH-ubiquinone reductase. AN Mitochondrial electron transport complex 1. AN Mitochondrial electron transport complex I. AN NADH coenzyme Q1 reductase. AN NADH-coenzyme Q oxidoreductase. AN NADH-coenzyme Q reductase. AN NADH-CoQ oxidoreductase. AN NADH-CoQ reductase. AN NADH-ubiquinone reductase. AN NADH-ubiquinone oxidoreductase. AN NADH-ubiquinone-1 reductase. AN Reduced nicotinamide adenine dinucleotide-coenzyme Q reductase. AN NADH:ubiquinone oxidoreductase complex. AN NADH-Q6 oxidoreductase. AN Electron transfer complex I. CA NADH + ubiquinone = NAD(+) + ubiquinol. CF FAD; Iron-sulfur. CC -!- The complex, present in mitochondria, can be degraded to form CC EC 1.6.99.3. PR PROSITE; PDOC00570; PR PROSITE; PDOC00858; PR PROSITE; PDOC00843; PR PROSITE; PDOC00468; PR PROSITE; PDOC00521; PR PROSITE; PDOC00555; PR PROSITE; PDOC00554; DR Q05752, N4AM_BOVIN; O95182, N4AM_HUMAN; Q02827, N4BM_BOVIN; DR O95298, N4BM_HUMAN; Q9M9M9, N7BM_ARATH; O97725, N7BM_BOVIN; DR Q9N2W7, N7BM_CAEEL; Q9UI09, N7BM_HUMAN; Q02365, NB2M_BOVIN; DR O43676, NB2M_HUMAN; Q02366, NB4M_BOVIN; P56556, NB4M_HUMAN; DR P42114, NB4M_NEUCR; P48305, NB5M_BOVIN; P48306, NB5M_CHICK; DR O95168, NB5M_HUMAN; Q95KV7, NB6M_BOVIN; Q9P0J0, NB6M_HUMAN; DR Q9ERS2, NB6M_MOUSE; Q02367, NB7M_BOVIN; O95139, NB7M_HUMAN; DR Q29259, NB7M_PIG ; Q02368, NB8M_BOVIN; P90789, NB8M_CAEEL; DR P17568, NB8M_HUMAN; P32340, NDI1_YEAST; Q02369, NI2M_BOVIN; DR Q9Y6M9, NI2M_HUMAN; Q02370, NI8M_BOVIN; O43678, NI8M_HUMAN; DR Q07842, NI8M_NEUCR; Q02371, NI9M_BOVIN; O95167, NI9M_HUMAN; DR Q9CQ91, NI9M_MOUSE; P42117, NI9M_NEUCR; Q02372, NIAM_BOVIN; DR O95169, NIAM_HUMAN; Q02373, NIDM_BOVIN; O96000, NIDM_HUMAN; DR Q02374, NIGM_BOVIN; Q20412, NIGM_CAEEL; O95178, NIGM_HUMAN; DR Q02376, NIKM_BOVIN; O43677, NIKM_HUMAN; Q02377, NIMM_BOVIN; DR O15239, NIMM_HUMAN; O35683, NIMM_MOUSE; Q02378, NINM_BOVIN; DR O75438, NINM_HUMAN; Q02379, NIPM_BOVIN; O43920, NIPM_HUMAN; DR Q02380, NISM_BOVIN; O43674, NISM_HUMAN; Q37381, NU1M_ACACA; DR P48897, NU1M_ALBCO; O47868, NU1M_ALLMI; P50658, NU1M_ANAPL; DR P34846, NU1M_ANOGA; P33502, NU1M_ANOQU; P34847, NU1M_APILI; DR Q33756, NU1M_ARBLI; P19040, NU1M_ARTSA; Q37714, NU1M_ARTSF; DR P24875, NU1M_ASCSU; P23649, NU1M_ASTFO; P23650, NU1M_ASTPE; DR O78693, NU1M_ATEPA; P41296, NU1M_BALMU; P24967, NU1M_BALPH; DR P03887, NU1M_BOVIN; O21000, NU1M_BRALA; Q9MIZ0, NU1M_BRARE; DR O78701, NU1M_BRAVA; O78700, NU1M_CABUN; P24887, NU1M_CAEEL; DR P92604, NU1M_CANFA; O78679, NU1M_CARAU; O78695, NU1M_CEBAP; DR O03850, NU1M_CERSI; P18936, NU1M_CHICK; P11658, NU1M_CHLRE; DR P48898, NU1M_CHOCR; P08834, NU1M_CITLA; P24968, NU1M_COTJA; DR P34186, NU1M_CROLA; P48899, NU1M_CYACA; P24969, NU1M_CYPCA; DR O63623, NU1M_DALCH; O21325, NU1M_DASNO; Q37313, NU1M_DICDI; DR P41304, NU1M_DIDMA; O79546, NU1M_DINSE; P51926, NU1M_DROAI; DR P51927, NU1M_DROAL; P51928, NU1M_DROAM; P51930, NU1M_DROBF; DR P51931, NU1M_DROGU; P51932, NU1M_DROMD; P18929, NU1M_DROME; DR P51933, NU1M_DROMI; P51938, NU1M_DROSS; P51937, NU1M_DROSU; DR P07710, NU1M_DROYA; Q8W9N6, NU1M_DUGDU; P92475, NU1M_EQUAS; DR P48900, NU1M_FELCA; P55779, NU1M_GADMO; P38598, NU1M_HALGR; DR P48901, NU1M_HANWI; Q9ZZZ1, NU1M_HIPAM; Q9MP77, NU1M_HIPDI; DR P48652, NU1M_HORSE; P03886, NU1M_HUMAN; Q96126, NU1M_HYLLA; DR O21069, NU1M_LAMFL; O03847, NU1M_LATCH; P15576, NU1M_LEITA; DR O78696, NU1M_LEMCA; P09045, NU1M_LOCMI; O47479, NU1M_LOLBL; DR Q37546, NU1M_LUMTE; O78704, NU1M_MACEU; P92659, NU1M_MACRO; DR O78705, NU1M_MACRU; O78702, NU1M_MANTE; P26845, NU1M_MARPO; DR Q37556, NU1M_METSE; O78703, NU1M_MONDO; P03888, NU1M_MOUSE; DR Q00860, NU1M_MYTED; O21077, NU1M_MYXGL; P08774, NU1M_NEUCR; DR O78709, NU1M_NOTTY; O78697, NU1M_NYCCO; O80003, NU1M_NYCNO; DR P31839, NU1M_OENBE; P48174, NU1M_ONCMY; Q37717, NU1M_ORNAN; DR Q9ZXY4, NU1M_PAPHA; P12772, NU1M_PARLI; P05513, NU1M_PARTE; DR Q96186, NU1M_PECMA; O79670, NU1M_PELSU; O78710, NU1M_PERGU; DR Q01300, NU1M_PETHY; Q37603, NU1M_PETMA; O78706, NU1M_PHACI; DR Q00505, NU1M_PHOVI; O79874, NU1M_PIG ; P24995, NU1M_PISOC; DR P19041, NU1M_PODAN; Q96182, NU1M_POLOR; P92690, NU1M_PONPA; DR P92718, NU1M_PONPP; O79427, NU1M_RABIT; P16672, NU1M_RANCA; DR P03889, NU1M_RAT ; O99824, NU1M_RHISA; Q96189, NU1M_RHIUN; DR O78694, NU1M_SAGOE; Q37676, NU1M_SALSA; O78711, NU1M_SARHA; DR O21408, NU1M_SCYCA; O78747, NU1M_SHEEP; P50659, NU1M_SIMVI; DR O78715, NU1M_SMICR; O78712, NU1M_SMIMA; Q9ZZ54, NU1M_SQUAC; DR O21397, NU1M_STRCA; P15548, NU1M_STRPU; O78714, NU1M_TACAC; DR O78698, NU1M_TAMSI; O78699, NU1M_TAMTE; O48358, NU1M_THYAR; DR Q9ZZ38, NU1M_TRIRU; O78707, NU1M_TRIVU; O78708, NU1M_VOMUR; DR Q01148, NU1M_WHEAT; P03890, NU1M_XENLA; O78713, NU1M_ZAGBR; DR Q37376, NU2M_ACACA; P48902, NU2M_ALBCO; O63767, NU2M_ANAAC; DR O63794, NU2M_ANAAM; O63796, NU2M_ANACA; O63797, NU2M_ANAFA; DR O63775, NU2M_ANAFO; O63798, NU2M_ANAPE; Q33636, NU2M_ANOAL; DR P34848, NU2M_ANOGA; P33503, NU2M_ANOQU; P34849, NU2M_APILI; DR P19042, NU2M_ARTSA; Q37704, NU2M_ARTSF; P24877, NU2M_ASCSU; DR Q33819, NU2M_ASTPE; P41297, NU2M_BALMU; P24970, NU2M_BALPH; DR P15688, NU2M_BETVU; P03892, NU2M_BOVIN; O47434, NU2M_BRAFL; DR O21001, NU2M_BRALA; Q9MIY9, NU2M_BRARE; P24889, NU2M_CAEEL; DR Q9ZZ65, NU2M_CANFA; Q36346, NU2M_CAPHI; O78680, NU2M_CARAU; DR O03197, NU2M_CERSI; P18937, NU2M_CHICK; P08740, NU2M_CHLRE; DR P48903, NU2M_CHOCR; P24971, NU2M_COTJA; P34187, NU2M_CROLA; DR P48904, NU2M_CYACA; P24972, NU2M_CYPCA; O21326, NU2M_DASNO; DR P41305, NU2M_DIDMA; O79547, NU2M_DINSE; P29867, NU2M_DROMA; DR P03896, NU2M_DROME; P29868, NU2M_DROSE; P29869, NU2M_DROSI; DR P03895, NU2M_DROYA; Q8W9N5, NU2M_DUGDU; P92476, NU2M_EQUAS; DR P48905, NU2M_FELCA; P55780, NU2M_GADMO; P38599, NU2M_HALGR; DR P48906, NU2M_HANWI; Q9ZZZ0, NU2M_HIPAM; P48653, NU2M_HORSE; DR P03891, NU2M_HUMAN; Q95704, NU2M_HYLLA; Q34799, NU2M_HYLSY; DR O21070, NU2M_LAMFL; O03166, NU2M_LATCH; Q36426, NU2M_LOCMI; DR Q34951, NU2M_LUMTE; P92660, NU2M_MACRO; P26846, NU2M_MARPO; DR O47495, NU2M_METSE; P03893, NU2M_MOUSE; Q00229, NU2M_MYTED; DR O21078, NU2M_MYXGL; Q35140, NU2M_NEUCR; P93401, NU2M_OENBE; DR P48175, NU2M_ONCMY; Q36451, NU2M_ORNAN; O21798, NU2M_PANTR; DR Q9ZXY3, NU2M_PAPHA; P12771, NU2M_PARLI; P15577, NU2M_PARTE; DR O79671, NU2M_PELSU; Q35535, NU2M_PETMA; Q00540, NU2M_PHOVI; DR O79875, NU2M_PIG ; P24996, NU2M_PISOC; P15578, NU2M_PODAN; DR Q95910, NU2M_POLOR; P92691, NU2M_PONPA; O79428, NU2M_RABIT; DR P16673, NU2M_RANCA; P11662, NU2M_RAT ; O99817, NU2M_RHISA; DR Q96061, NU2M_RHIUN; Q35924, NU2M_SALSA; O21409, NU2M_SCYCA; DR O78748, NU2M_SHEEP; Q9ZZ53, NU2M_SQUAC; O21398, NU2M_STRCA; DR P15549, NU2M_STRPU; P03894, NU2M_XENLA; Q37382, NU3M_ACACA; DR P48907, NU3M_ALBCO; Q96007, NU3M_ALLCE; Q37399, NU3M_ALLMA; DR O47874, NU3M_ALLMI; P34850, NU3M_ANOGA; P33509, NU3M_ANOQU; DR P34851, NU3M_APILI; P92533, NU3M_ARATH; P19043, NU3M_ARTSA; DR Q37709, NU3M_ARTSF; P24883, NU3M_ASCSU; P11991, NU3M_ASTPE; DR P24973, NU3M_BALPH; P03898, NU3M_BOVIN; O47429, NU3M_BRALA; DR P48908, NU3M_BRANA; Q9MIY3, NU3M_BRARE; P24895, NU3M_CAEEL; DR Q9ZZ60, NU3M_CANFA; P48909, NU3M_CANPA; O78686, NU3M_CARAU; DR O03202, NU3M_CERSI; P18938, NU3M_CHICK; P48910, NU3M_CHOCR; DR P34192, NU3M_CROLA; P48911, NU3M_CYACA; P24974, NU3M_CYPCA; DR O21332, NU3M_DASNO; Q37312, NU3M_DICDI; P41306, NU3M_DIDMA; DR O79553, NU3M_DINSE; P18930, NU3M_DROME; P51940, NU3M_DROSU; DR P07705, NU3M_DROYA; Q8W9M9, NU3M_DUGDU; P15956, NU3M_EMENI; DR P92482, NU3M_EQUAS; Q34522, NU3M_FASHE; P48912, NU3M_FELCA; DR P15957, NU3M_GADMO; P38600, NU3M_HALGR; P48913, NU3M_HANWI; DR Q9ZZY4, NU3M_HIPAM; P48654, NU3M_HORSE; P03897, NU3M_HUMAN; DR Q95708, NU3M_HYLLA; O03171, NU3M_LATCH; Q36422, NU3M_LOCMI; DR O47476, NU3M_LOLBL; Q34950, NU3M_LUMTE; P92666, NU3M_MACRO; DR P16265, NU3M_MAIZE; P26847, NU3M_MARPO; Q35100, NU3M_METSE; DR O21519, NU3M_MICPE; P03899, NU3M_MOUSE; Q00568, NU3M_MYTED; DR Q9G2X1, NU3M_MYXGL; Q35141, NU3M_NEUCR; P18630, NU3M_OENBE; DR P20686, NU3M_ONCGO; Q35262, NU3M_ONCKE; P20687, NU3M_ONCKI; DR Q37108, NU3M_ONCMA; P11629, NU3M_ONCMY; P20688, NU3M_ONCNE; DR P25707, NU3M_ONCTS; Q36456, NU3M_ORNAN; P27062, NU3M_PANGI; DR Q9ZXX7, NU3M_PAPHA; P12774, NU3M_PARLI; P92817, NU3M_PAROL; DR P15579, NU3M_PARTE; Q95881, NU3M_PERGO; Q95891, NU3M_PERMA; DR Q95897, NU3M_PERME; Q95921, NU3M_PERPL; Q35540, NU3M_PETMA; DR O21513, NU3M_PHOSU; Q00541, NU3M_PHOVI; O79880, NU3M_PIG ; DR Q36664, NU3M_PINSY; P24997, NU3M_PISOC; Q36518, NU3M_PLASU; DR P15580, NU3M_PODAN; Q95915, NU3M_POLOR; P92697, NU3M_PONPA; DR O99978, NU3M_PORPU; Q37625, NU3M_PROWI; O79434, NU3M_RABIT; DR P05506, NU3M_RAT ; O21273, NU3M_RECAM; O99823, NU3M_RHISA; DR Q96066, NU3M_RHIUN; Q35929, NU3M_SALSA; O03252, NU3M_SALTR; DR O63850, NU3M_SARGL; O79408, NU3M_SCYCA; O78753, NU3M_SHEEP; DR O21566, NU3M_SIGHI; O99869, NU3M_SOLTU; Q9ZZ47, NU3M_SQUAC; DR O79102, NU3M_STRCA; P15550, NU3M_STRPU; P18903, NU3M_WHEAT; DR P03900, NU3M_XENLA; Q37375, NU4M_ACACA; P92623, NU4M_AGKAC; DR P92492, NU4M_AGKCO; O03726, NU4M_AGKHA; O03727, NU4M_AGKIN; DR P92503, NU4M_AGKPI; P92613, NU4M_AGKRH; P48914, NU4M_ALBCO; DR P51898, NU4M_ANOAR; P34852, NU4M_ANOGA; P33511, NU4M_ANOQU; DR P34853, NU4M_APILI; P34941, NU4M_ARBLI; P19046, NU4M_ARTSA; DR Q37711, NU4M_ARTSF; P24880, NU4M_ASCSU; P03913, NU4M_ASPAM; DR P11992, NU4M_ASTPE; O03692, NU4M_ATRNM; O03695, NU4M_ATRPI; DR P92494, NU4M_AZEFE; P41298, NU4M_BALMU; P24975, NU4M_BALPH; DR O03697, NU4M_BOTAS; O03698, NU4M_BOTBI; O03699, NU4M_BOTER; DR O03700, NU4M_BOTLA; O03701, NU4M_BOTSC; P03910, NU4M_BOVIN; DR Q04050, NU4M_BRACM; O47423, NU4M_BRAFL; O79421, NU4M_BRALA; DR Q9MIY1, NU4M_BRARE; P24892, NU4M_CAEEL; Q34076, NU4M_CAICR; DR Q9ZZ58, NU4M_CANFA; O78687, NU4M_CARAU; O03707, NU4M_CAURH; DR Q34048, NU4M_CERCA; O03703, NU4M_CERGO; O03204, NU4M_CERSI; DR P18939, NU4M_CHICK; P20113, NU4M_CHLRE; P48915, NU4M_CHOCR; DR O03702, NU4M_CROAD; P34194, NU4M_CROLA; O03704, NU4M_CROLE; DR O03710, NU4M_CROVC; O21334, NU4M_DASNO; P41308, NU4M_DIDMA; DR O79555, NU4M_DINSE; P18931, NU4M_DROME; P07707, NU4M_DROYA; DR Q8W9M7, NU4M_DUGDU; P03914, NU4M_EMENI; P92484, NU4M_EQUAS; DR P48916, NU4M_FELCA; P55781, NU4M_GADMO; P03907, NU4M_GORGO; DR P38601, NU4M_HALGR; P48917, NU4M_HANWI; Q9ZZY2, NU4M_HIPAM; DR P48655, NU4M_HORSE; P03905, NU4M_HUMAN; P03909, NU4M_HYLLA; DR O03733, NU4M_HYPHY; P92649, NU4M_LACMU; O03173, NU4M_LATCH; DR Q34878, NU4M_LEMCA; Q36424, NU4M_LOCMI; Q34949, NU4M_LUMTE; DR P50664, NU4M_MACFA; P92668, NU4M_MACRO; P26848, NU4M_MARPO; DR O47497, NU4M_METSE; O21521, NU4M_MICPE; P03911, NU4M_MOUSE; DR Q00231, NU4M_MYTED; Q9G2W9, NU4M_MYXGL; P11631, NU4M_ONCMY; DR Q36458, NU4M_ORNAN; P03906, NU4M_PANTR; P12775, NU4M_PARLI; DR P15581, NU4M_PARTE; O79677, NU4M_PELSU; Q35542, NU4M_PETMA; DR O21515, NU4M_PHOSU; Q00506, NU4M_PHOVI; O79881, NU4M_PIG ; DR P24998, NU4M_PISOC; P15582, NU4M_PODAN; Q95917, NU4M_POLOR; DR P92698, NU4M_PONPA; P03908, NU4M_PONPY; O03763, NU4M_PORHY; DR O03772, NU4M_PORNA; O03773, NU4M_POROP; Q37617, NU4M_PROWI; DR O79436, NU4M_RABIT; P05508, NU4M_RAT ; O99825, NU4M_RHISA; DR Q96068, NU4M_RHIUN; Q9ZZM4, NU4M_SALSA; O79410, NU4M_SCYCA; DR O78755, NU4M_SHEEP; P50660, NU4M_SIMVI; O03778, NU4M_SISMI; DR Q9ZZ45, NU4M_SQUAC; O21406, NU4M_STRCA; P15551, NU4M_STRPU; DR Q36150, NU4M_TARSY; O03780, NU4M_TRIAB; O03792, NU4M_TRICN; DR P92793, NU4M_TRIEL; P92794, NU4M_TRIFL; P92681, NU4M_TRIOK; DR Q36834, NU4M_TRIRU; P92759, NU4M_TRIST; O03807, NU4M_TRIWA; DR P27572, NU4M_WHEAT; P03912, NU4M_XENLA; Q37372, NU5M_ACACA; DR P48918, NU5M_ALBCO; P50365, NU5M_ALLMA; P51899, NU5M_ANOAR; DR P34854, NU5M_ANOGA; Q31696, NU5M_ANOQN; P33510, NU5M_ANOQU; DR Q31651, NU5M_ANSCE; P34855, NU5M_APILI; P29388, NU5M_ARATH; DR Q33753, NU5M_ARBLI; P19047, NU5M_ARTSA; Q37710, NU5M_ARTSF; DR P24884, NU5M_ASCSU; P11993, NU5M_ASTPE; P41299, NU5M_BALMU; DR P24978, NU5M_BALPH; P03920, NU5M_BOVIN; O47430, NU5M_BRAFL; DR O79422, NU5M_BRALA; Q9MIY0, NU5M_BRARE; P24896, NU5M_CAEEL; DR Q9ZZ57, NU5M_CANFA; P48919, NU5M_CANPA; O78688, NU5M_CARAU; DR Q34052, NU5M_CERCA; O03205, NU5M_CERSI; P18940, NU5M_CHICK; DR Q94RJ2, NU5M_CHIMO; P08739, NU5M_CHLRE; P48920, NU5M_CHOCR; DR P34195, NU5M_CROLA; P24979, NU5M_CYPCA; O21335, NU5M_DASNO; DR Q34313, NU5M_DICDI; P41309, NU5M_DIDMA; O79556, NU5M_DINSE; DR P18932, NU5M_DROME; P07706, NU5M_DROYA; Q8W9M6, NU5M_DUGDU; DR P11628, NU5M_EMENI; P92485, NU5M_EQUAS; P48921, NU5M_FELCA; DR P55782, NU5M_GADMO; P03917, NU5M_GORGO; P38602, NU5M_HALGR; DR Q9ZZY1, NU5M_HIPAM; P48656, NU5M_HORSE; P03915, NU5M_HUMAN; DR P03919, NU5M_HYLLA; O03174, NU5M_LATCH; P15583, NU5M_LEITA; DR Q34879, NU5M_LEMCA; Q36428, NU5M_LOCMI; Q34947, NU5M_LUMTE; DR P50665, NU5M_MACFA; P92669, NU5M_MACRO; Q36284, NU5M_MAIZE; DR P26849, NU5M_MARPO; Q35099, NU5M_METSE; P03921, NU5M_MOUSE; DR O63908, NU5M_MYOGL; Q00232, NU5M_MYTED; Q9G2W8, NU5M_MYXGL; DR P05510, NU5M_NEUCR; P10330, NU5M_OENBE; P48176, NU5M_ONCMY; DR Q36459, NU5M_ORNAN; P03916, NU5M_PANPA; Q35648, NU5M_PANTR; DR Q95885, NU5M_PAPHA; P12776, NU5M_PARLI; P15584, NU5M_PARTE; DR Q35639, NU5M_PEA ; O79678, NU5M_PELSU; Q35543, NU5M_PETMA; DR Q00542, NU5M_PHOVI; P50366, NU5M_PHYIN; Q9TDR1, NU5M_PIG ; DR P24999, NU5M_PISOC; P20679, NU5M_PODAN; Q95918, NU5M_POLOR; DR P92699, NU5M_PONPA; P03918, NU5M_PONPY; O79437, NU5M_RABIT; DR P11661, NU5M_RAT ; Q9ZYM7, NU5M_RHISA; P50367, NU5M_RHIST; DR Q96069, NU5M_RHIUN; Q9ZZM3, NU5M_SALSA; P50368, NU5M_SCHCO; DR O79411, NU5M_SCYCA; O78756, NU5M_SHEEP; Q9ZZ44, NU5M_SQUAC; DR Q35813, NU5M_STRCA; Q35832, NU5M_STRFN; P15552, NU5M_STRPU; DR Q36151, NU5M_TARSY; Q01561, NU5M_TRIRU; P04540, NU5M_TRYBB; DR Q37680, NU5M_WHEAT; P03922, NU5M_XENLA; Q37371, NU6M_ACACA; DR P43189, NU6M_AETCR; P43190, NU6M_AETPU; P43191, NU6M_AETPY; DR P48922, NU6M_ALBCO; Q08084, NU6M_ALBTU; P43193, NU6M_ALCTO; DR P43192, NU6M_ALLAL; Q06059, NU6M_ANAPL; Q33635, NU6M_ANOAL; DR P34856, NU6M_ANOGA; P33513, NU6M_ANOQU; P34857, NU6M_APILI; DR Q01825, NU6M_ARATH; P19048, NU6M_ARTSA; Q37712, NU6M_ARTSF; DR P24873, NU6M_ASCSU; Q33817, NU6M_ASTPE; P41300, NU6M_BALMU; DR P24980, NU6M_BALPH; P03924, NU6M_BOVIN; P43194, NU6M_BRABR; DR O79423, NU6M_BRALA; P43195, NU6M_BRAMA; Q9MIX9, NU6M_BRARE; DR P24885, NU6M_CAEEL; P43196, NU6M_CALMA; Q9ZZ56, NU6M_CANFA; DR P48923, NU6M_CANPA; O78689, NU6M_CARAU; P43197, NU6M_CEPCO; DR P43198, NU6M_CEPGR; Q34050, NU6M_CERCA; O03206, NU6M_CERSI; DR P18941, NU6M_CHICK; P10329, NU6M_CHLRE; P48924, NU6M_CHOCR; DR P24981, NU6M_COTJA; P34196, NU6M_CROLA; P48925, NU6M_CYACA; DR P43199, NU6M_CYCPS; P24982, NU6M_CYPCA; O21336, NU6M_DASNO; DR Q37314, NU6M_DICDI; P41315, NU6M_DIDMA; O79557, NU6M_DINSE; DR P18933, NU6M_DROME; P07709, NU6M_DROYA; Q8W9M5, NU6M_DUGDU; DR P92486, NU6M_EQUAS; P48926, NU6M_FELCA; P43200, NU6M_FRAAR; DR P43201, NU6M_FRACR; P55783, NU6M_GADMO; Q34573, NU6M_GORGO; DR P38603, NU6M_HALGR; P48927, NU6M_HANWI; Q9ZZY0, NU6M_HIPAM; DR P48657, NU6M_HORSE; P03923, NU6M_HUMAN; Q95710, NU6M_HYLLA; DR P41322, NU6M_LARCA; O03175, NU6M_LATCH; Q36425, NU6M_LOCMI; DR O47478, NU6M_LOLBL; Q34944, NU6M_LUMTE; P43202, NU6M_LUNCI; DR P92670, NU6M_MACRO; P26850, NU6M_MARPO; O47498, NU6M_METSE; DR P03925, NU6M_MOUSE; Q00570, NU6M_MYTED; Q9G2W7, NU6M_MYXGL; DR P48177, NU6M_ONCMY; Q36460, NU6M_ORNAN; Q9ZXX5, NU6M_PAPHA; DR P12777, NU6M_PARLI; O79679, NU6M_PELSU; Q35544, NU6M_PETMA; DR Q00543, NU6M_PHOVI; O79882, NU6M_PIG ; P15959, NU6M_PODAN; DR Q95919, NU6M_POLOR; P92700, NU6M_PONPA; Q37626, NU6M_PROWI; DR P43203, NU6M_PTYAL; O79438, NU6M_RABIT; P03926, NU6M_RAT ; DR O99827, NU6M_RHISA; Q96070, NU6M_RHIUN; Q9ZZM2, NU6M_SALSA; DR O63849, NU6M_SARGL; O79412, NU6M_SCYCA; O78757, NU6M_SHEEP; DR Q9ZZ43, NU6M_SQUAC; O21407, NU6M_STRCA; P15553, NU6M_STRPU; DR P43204, NU6M_SYNAN; P43205, NU6M_SYNHY; P43206, NU6M_SYNWU; DR Q36836, NU6M_TRIRU; P43207, NU6M_URIAL; P43208, NU6M_URILO; DR Q02500, NU6M_WHEAT; P03927, NU6M_XENLA; Q37373, NUAM_ACACA; DR Q9FGI6, NUAM_ARATH; P15690, NUAM_BOVIN; Q94511, NUAM_DROME; DR P28331, NUAM_HUMAN; P24918, NUAM_NEUCR; O21241, NUAM_RECAM; DR Q43644, NUAM_SOLTU; Q92406, NUBM_ASPNG; P25708, NUBM_BOVIN; DR P49821, NUBM_HUMAN; P24917, NUBM_NEUCR; Q37384, NUCM_ACACA; DR P93306, NUCM_ARATH; P17694, NUCM_BOVIN; Q93873, NUCM_CAEEL; DR Q9TAJ7, NUCM_CAFRO; Q23883, NUCM_DICDI; O75306, NUCM_HUMAN; DR Q9TC96, NUCM_NEPOL; P22142, NUCM_NEUCR; Q36450, NUCM_NICSY; DR P15689, NUCM_PARTE; Q37619, NUCM_PROWI; Q37720, NUCM_PYLLI; DR O21270, NUCM_RECAM; P80264, NUCM_SOLTU; P21301, NUCM_TRYBB; DR P34942, NUDM_BOVIN; P54713, NUDM_CANFA; P91929, NUDM_DROME; DR O95299, NUDM_HUMAN; P34943, NUEM_BOVIN; Q16795, NUEM_HUMAN; DR P25284, NUEM_NEUCR; P80265, NUEM_SOLTU; Q9FLX7, NUFM_ARATH; DR P23935, NUFM_BOVIN; Q18359, NUFM_CAEEL; Q16718, NUFM_HUMAN; DR P24919, NUFM_NEUCR; Q63362, NUFM_RAT ; P80266, NUFM_SOLTU; DR Q37383, NUGM_ACACA; Q95748, NUGM_ARATH; Q33994, NUGM_BETTR; DR Q37787, NUGM_BETVU; Q34011, NUGM_BETWE; P23709, NUGM_BOVIN; DR Q00673, NUGM_CANMA; P22237, NUGM_DICDI; O75489, NUGM_HUMAN; DR P34944, NUGM_MARPO; Q9DCT2, NUGM_MOUSE; P23710, NUGM_NEUCR; DR Q35322, NUGM_ORYSA; P15601, NUGM_PARPR; P15600, NUGM_PARTE; DR Q37622, NUGM_PROWI; O21271, NUGM_RECAM; P80261, NUGM_SOLTU; DR O22769, NUHM_ARATH; P04394, NUHM_BOVIN; Q20719, NUHM_CAEEL; DR P49820, NUHM_CANFA; P19404, NUHM_HUMAN; Q9D6J6, NUHM_MOUSE; DR P40915, NUHM_NEUCR; P19234, NUHM_RAT ; O13691, NUHM_SCHPO; DR Q42599, NUIM_ARATH; P42028, NUIM_BOVIN; Q22619, NUIM_CAEEL; DR O00217, NUIM_HUMAN; Q12644, NUIM_NEUCR; O21233, NUIM_RECAM; DR P80269, NUIM_SOLTU; O24143, NUIM_TOBAC; P30826, NUIM_TRYBB; DR P25710, NUJM_NEUCR; Q42577, NUKM_ARATH; P42026, NUKM_BOVIN; DR P42027, NUKM_BRAOL; Q94360, NUKM_CAEEL; O75251, NUKM_HUMAN; DR O47950, NUKM_NEUCR; P15602, NUKM_PARTE; O21272, NUKM_RECAM; DR Q43844, NUKM_SOLTU; Q26783, NUKM_TRYBB; Q37379, NULM_ACACA; DR P48928, NULM_ALBCO; P34858, NULM_ANOGA; P33512, NULM_ANOQU; DR P34859, NULM_APILI; Q04614, NULM_ARATH; P19049, NULM_ARTSA; DR Q37751, NULM_ARTSF; P24874, NULM_ASCSU; Q33821, NULM_ASTPE; DR P41301, NULM_BALMU; P24976, NULM_BALPH; P03902, NULM_BOVIN; DR O79420, NULM_BRALA; Q9MIY2, NULM_BRARE; Q8HEB9, NULM_CAEBR; DR P24886, NULM_CAEEL; Q9ZZ59, NULM_CANFA; P48929, NULM_CANPA; DR Q34049, NULM_CERCA; O03203, NULM_CERSI; P18942, NULM_CHICK; DR P48930, NULM_CHOCR; P34193, NULM_CROLA; P24977, NULM_CYPCA; DR O21333, NULM_DASNO; P41307, NULM_DIDMA; O79554, NULM_DINSE; DR P18934, NULM_DROME; P07708, NULM_DROYA; Q8W9M8, NULM_DUGDU; DR P92483, NULM_EQUAS; P48931, NULM_FELCA; P23633, NULM_GADMO; DR Q34572, NULM_GORGO; Q9ZZY3, NULM_HIPAM; P48658, NULM_HORSE; DR P03901, NULM_HUMAN; Q95709, NULM_HYLLA; O03172, NULM_LATCH; DR Q36423, NULM_LOCMI; Q34948, NULM_LUMTE; P92667, NULM_MACRO; DR P26851, NULM_MARPO; O47492, NULM_METSE; O21520, NULM_MICPE; DR P03903, NULM_MOUSE; Q00230, NULM_MYTED; Q9G2X0, NULM_MYXGL; DR P05509, NULM_NEUCR; Q37131, NULM_ONCMA; P11630, NULM_ONCMY; DR Q36457, NULM_ORNAN; Q35588, NULM_PANPA; Q37809, NULM_PANTR; DR Q9ZXX6, NULM_PAPHA; P12773, NULM_PARLI; Q35541, NULM_PETMA; DR O21514, NULM_PHOSU; Q00544, NULM_PHOVI; Q37598, NULM_PHYIN; DR P56632, NULM_PIG ; P25000, NULM_PISOC; P20680, NULM_PODAN; DR Q95916, NULM_POLOR; Q35585, NULM_PONPY; Q37627, NULM_PROWI; DR O79435, NULM_RABIT; P05507, NULM_RAT ; O99826, NULM_RHISA; DR Q96067, NULM_RHIUN; Q9ZZM5, NULM_SALSA; O63851, NULM_SARGL; DR O79409, NULM_SCYCA; O78754, NULM_SHEEP; O21567, NULM_SIGHI; DR Q9ZZ46, NULM_SQUAC; O21405, NULM_STRCA; P15554, NULM_STRPU; DR Q01562, NULM_TRIRU; P03904, NULM_XENLA; Q01321, NUML_BOVIN; DR O00483, NUML_HUMAN; Q62425, NUML_MOUSE; P23934, NUMM_BOVIN; DR Q19724, NUMM_CAEEL; O75380, NUMM_HUMAN; P52503, NUMM_MOUSE; DR Q03015, NUMM_NEUCR; P52504, NUMM_RAT ; P80267, NUO1_SOLTU; DR P80268, NUO2_SOLTU; P80263, NUO3_SOLTU; P80262, NUO5_SOLTU; DR P80729, NUO6_SOLTU; P80730, NUO7_SOLTU; P80731, NUO8_SOLTU; DR P25712, NUOM_BOVIN; P56181, NUOM_HUMAN; P42029, NUPM_BOVIN; DR P51970, NUPM_HUMAN; P21976, NUPM_NEUCR; P42116, NURM_NEUCR; DR Q02854, NUXM_NEUCR; Q02375, NUYM_BOVIN; O43181, NUYM_HUMAN; DR P25711, NUYM_NEUCR; P19968, NUZM_NEUCR; // ID 1.6.5.4 DE Monodehydroascorbate reductase (NADH). CA NADH + 2 monodehydroascorbate = NAD(+) + 2 ascorbate. // ID 1.6.5.5 DE NADPH:quinone reductase. AN Quinone oxidoreductase. AN Zeta-crystallin. CA NADPH + quinone = NADP(+) + semiquinone. CF Zinc. CC -!- Specific for NADPH. CC -!- Catalyzes the one electron reduction of certain quinones; CC orthoquinones are the best substrates. CC -!- Dicoumarol (cf. EC 1.6.99.2) and nitrofurantoin are competitive CC inhibitors with respect to the quinone substrate. CC -!- Abundant in the lens of the eye of some mammalian species. PR PROSITE; PDOC00058; DR P11415, QOR_CAVPO ; P28304, QOR_ECOLI ; Q08257, QOR_HUMAN ; DR Q28452, QOR_LAMGU ; P42865, QOR_LEIAM ; P47199, QOR_MOUSE ; DR P43903, QOR_PSEAE ; P40783, QOR_SALTY ; P38230, QOR_YEAST ; // ID 1.6.5.6 DE p-benzoquinone reductase (NADPH). CA NADPH + p-benzoquinone = NADP(+) + hydroquinone. CC -!- Involved in the 4-nitrophenol degradation pathway in bacteria. // ID 1.6.5.7 DE 2-hydroxy-1,4-benzoquinone reductase. AN Hydroxybenzoquinone reductase. CA 1,2,4-trihydroxybenzene + NAD(+) = hydroxybenzoquinone + NADH. CF FMN. CC -!- The enzyme differs in substrate speificity from other quinone reductases. CC -!- The enzyme in Burkholderia cepacia is inducible by CC 2,4,5-trichlorophenoxyacetate. // ID 1.6.6.1 DE Transferred entry: 1.7.1.1. // ID 1.6.6.2 DE Transferred entry: 1.7.1.2. // ID 1.6.6.3 DE Transferred entry: 1.7.1.3. // ID 1.6.6.4 DE Transferred entry: 1.7.1.4. // ID 1.6.6.5 DE Transferred entry: 1.7.2.1. // ID 1.6.6.6 DE Transferred entry: 1.7.1.5. // ID 1.6.6.7 DE Transferred entry: 1.7.1.6. // ID 1.6.6.8 DE Transferred entry: 1.7.1.7. // ID 1.6.6.9 DE Trimethylamine-N-oxide reductase. AN Trimethylamine oxidase. CA NADH + trimethylamine-N-oxide = NAD(+) + trimethylamine + H(2)O. DI Trimethylaminuria; MIM:275700. PR PROSITE; PDOC00392; // ID 1.6.6.10 DE Transferred entry: 1.7.1.9. // ID 1.6.6.11 DE Transferred entry: 1.7.1.10. // ID 1.6.6.12 DE Transferred entry: 1.7.1.11. // ID 1.6.6.13 DE Transferred entry: 1.7.1.12. // ID 1.6.7.1 DE Transferred entry: 1.18.1.2. // ID 1.6.7.2 DE Transferred entry: 1.18.1.1. // ID 1.6.8.1 DE Transferred entry: 1.5.1.29. // ID 1.6.8.2 DE Transferred entry: 1.5.1.30. // ID 1.6.99.1 DE NADPH dehydrogenase. AN NADPH diaphorase. CA NADPH + acceptor = NADP(+) + reduced acceptor. CF FMN or FAD. CC -!- FMN in yeast; FAD in plants. DR P43084, EBP1_CANAL; P55736, FLRE_RANCA; P40952, KYE1_KLULA; DR Q02899, OYE1_YEAST; Q03558, OYE2_YEAST; P41816, OYE3_YEAST; DR Q09670, OYEA_SCHPO; Q09671, OYEB_SCHPO; // ID 1.6.99.2 DE NAD(P)H dehydrogenase (quinone). AN Quinone reductase. AN DT-diaphorase. AN Azoreductase. AN Phylloquinone reductase. AN Menadione reductase. CA NAD(P)H + acceptor = NAD(P)(+) + reduced acceptor. CF FAD. CC -!- Inhibited by dicoumarol. CC -!- Formerly EC 1.6.5.2. DR P15559, NQO1_HUMAN; Q64669, NQO1_MOUSE; P05982, NQO1_RAT ; DR P16083, NQO2_HUMAN; Q9JI75, NQO2_MOUSE; // ID 1.6.99.3 DE NADH dehydrogenase. AN Cytochrome c reductase. AN Type 1 dehydrogenase. AN Type I dehydrogenase. AN Beta-NADH dehydrogenase dinucleotide. AN Diaphorase. AN Dihydrocodehydrogenase I dehydrogenase. AN Dihydronicotinamide adenine dinucleotide dehydrogenase. AN Diphosphopyrinase. AN DPNH diaphorase. AN NADH diaphorase. AN NADH hydrogenase. AN NADH oxidoreductase. AN NADH-menadione oxidoreductase. AN Reduced diphosphopyridine nucleotide diaphorase. AN NADH:cytochrome c oxidoreductase. CA NADH + acceptor = NAD(+) + reduced acceptor. CF Flavoprotein; Iron-sulfur. CC -!- After preparations have been subjected to certain treatments CC cytochrome c may act as acceptor. CC -!- Under normal conditions, two protons are extruded from the CC cytoplasm or the intramitochondrial or stromal compartment. CC -!- Present in a mitochondrial complex as EC 1.6.5.3. CC -!- Formerly EC 1.6.2.1. PR PROSITE; PDOC00496; DR P26829, DHNA_BACSP; P42974, DHNA_BACSU; P00393, DHNA_ECOLI; DR P44856, DHNA_HAEIN; Q05752, N4AM_BOVIN; O95182, N4AM_HUMAN; DR Q02827, N4BM_BOVIN; O95298, N4BM_HUMAN; Q9M9M9, N7BM_ARATH; DR O97725, N7BM_BOVIN; Q9N2W7, N7BM_CAEEL; Q9UI09, N7BM_HUMAN; DR P37061, NAOX_ENTFA; Q58065, NAOX_METJA; Q49408, NAOX_MYCGE; DR P75389, NAOX_MYCPN; Q02365, NB2M_BOVIN; O43676, NB2M_HUMAN; DR Q02366, NB4M_BOVIN; P56556, NB4M_HUMAN; P42114, NB4M_NEUCR; DR P48305, NB5M_BOVIN; P48306, NB5M_CHICK; O95168, NB5M_HUMAN; DR Q95KV7, NB6M_BOVIN; Q9P0J0, NB6M_HUMAN; Q9ERS2, NB6M_MOUSE; DR Q02367, NB7M_BOVIN; O95139, NB7M_HUMAN; Q29259, NB7M_PIG ; DR Q02368, NB8M_BOVIN; P90789, NB8M_CAEEL; P17568, NB8M_HUMAN; DR Q02369, NI2M_BOVIN; Q9Y6M9, NI2M_HUMAN; Q02370, NI8M_BOVIN; DR O43678, NI8M_HUMAN; Q07842, NI8M_NEUCR; Q02371, NI9M_BOVIN; DR O95167, NI9M_HUMAN; Q9CQ91, NI9M_MOUSE; P42117, NI9M_NEUCR; DR Q02372, NIAM_BOVIN; O95169, NIAM_HUMAN; Q02373, NIDM_BOVIN; DR O96000, NIDM_HUMAN; Q02374, NIGM_BOVIN; Q20412, NIGM_CAEEL; DR O95178, NIGM_HUMAN; Q02376, NIKM_BOVIN; O43677, NIKM_HUMAN; DR Q02377, NIMM_BOVIN; O15239, NIMM_HUMAN; O35683, NIMM_MOUSE; DR Q02378, NINM_BOVIN; O75438, NINM_HUMAN; Q02379, NIPM_BOVIN; DR O43920, NIPM_HUMAN; Q02380, NISM_BOVIN; O43674, NISM_HUMAN; DR Q60049, NOX_THETH ; Q37373, NUAM_ACACA; Q9FGI6, NUAM_ARATH; DR P15690, NUAM_BOVIN; Q94511, NUAM_DROME; P28331, NUAM_HUMAN; DR P24918, NUAM_NEUCR; O21241, NUAM_RECAM; Q43644, NUAM_SOLTU; DR Q92406, NUBM_ASPNG; P25708, NUBM_BOVIN; P49821, NUBM_HUMAN; DR P24917, NUBM_NEUCR; Q37384, NUCM_ACACA; P93306, NUCM_ARATH; DR P17694, NUCM_BOVIN; Q93873, NUCM_CAEEL; Q9TAJ7, NUCM_CAFRO; DR Q23883, NUCM_DICDI; O75306, NUCM_HUMAN; Q9TC96, NUCM_NEPOL; DR P22142, NUCM_NEUCR; Q36450, NUCM_NICSY; P15689, NUCM_PARTE; DR Q37619, NUCM_PROWI; Q37720, NUCM_PYLLI; O21270, NUCM_RECAM; DR P80264, NUCM_SOLTU; P34942, NUDM_BOVIN; P54713, NUDM_CANFA; DR P91929, NUDM_DROME; O95299, NUDM_HUMAN; P34943, NUEM_BOVIN; DR Q16795, NUEM_HUMAN; P25284, NUEM_NEUCR; P80265, NUEM_SOLTU; DR Q9FLX7, NUFM_ARATH; P23935, NUFM_BOVIN; Q18359, NUFM_CAEEL; DR Q16718, NUFM_HUMAN; P24919, NUFM_NEUCR; Q63362, NUFM_RAT ; DR P80266, NUFM_SOLTU; Q37383, NUGM_ACACA; Q95748, NUGM_ARATH; DR Q33994, NUGM_BETTR; Q37787, NUGM_BETVU; Q34011, NUGM_BETWE; DR P23709, NUGM_BOVIN; Q00673, NUGM_CANMA; P22237, NUGM_DICDI; DR O75489, NUGM_HUMAN; P34944, NUGM_MARPO; Q9DCT2, NUGM_MOUSE; DR P23710, NUGM_NEUCR; Q35322, NUGM_ORYSA; P15601, NUGM_PARPR; DR P15600, NUGM_PARTE; Q37622, NUGM_PROWI; O21271, NUGM_RECAM; DR P80261, NUGM_SOLTU; O22769, NUHM_ARATH; P04394, NUHM_BOVIN; DR Q20719, NUHM_CAEEL; P49820, NUHM_CANFA; P19404, NUHM_HUMAN; DR Q9D6J6, NUHM_MOUSE; P40915, NUHM_NEUCR; P19234, NUHM_RAT ; DR O13691, NUHM_SCHPO; Q42599, NUIM_ARATH; P42028, NUIM_BOVIN; DR Q22619, NUIM_CAEEL; O00217, NUIM_HUMAN; Q12644, NUIM_NEUCR; DR P80269, NUIM_SOLTU; O24143, NUIM_TOBAC; P25710, NUJM_NEUCR; DR Q42577, NUKM_ARATH; P42026, NUKM_BOVIN; P42027, NUKM_BRAOL; DR Q94360, NUKM_CAEEL; O75251, NUKM_HUMAN; O47950, NUKM_NEUCR; DR Q43844, NUKM_SOLTU; Q26783, NUKM_TRYBB; Q01321, NUML_BOVIN; DR O00483, NUML_HUMAN; Q62425, NUML_MOUSE; P23934, NUMM_BOVIN; DR Q19724, NUMM_CAEEL; O75380, NUMM_HUMAN; P52503, NUMM_MOUSE; DR Q03015, NUMM_NEUCR; P52504, NUMM_RAT ; P80267, NUO1_SOLTU; DR P80268, NUO2_SOLTU; P80263, NUO3_SOLTU; P80262, NUO5_SOLTU; DR P80729, NUO6_SOLTU; P80730, NUO7_SOLTU; P80731, NUO8_SOLTU; DR P25712, NUOM_BOVIN; P56181, NUOM_HUMAN; P42029, NUPM_BOVIN; DR P51970, NUPM_HUMAN; P21976, NUPM_NEUCR; P42116, NURM_NEUCR; DR Q02854, NUXM_NEUCR; Q02375, NUYM_BOVIN; O43181, NUYM_HUMAN; DR P25711, NUYM_NEUCR; P19968, NUZM_NEUCR; // ID 1.6.99.4 DE Transferred entry: 1.18.1.2. // ID 1.6.99.5 DE NADH dehydrogenase (quinone). CA NADH + quinone = NAD(+) + quinol. CC -!- Menaquinone or other quinones can act as acceptor. CC -!- Inhibited by AMP and 2,4-dinitrophenol but not by dicoumarol or folic CC acid derivatives. DR P39755, NDHF_BACSU; P29913, NQO1_PARDE; Q56222, NQO1_THETH; DR P29914, NQO2_PARDE; Q56221, NQO2_THETH; P29915, NQO3_PARDE; DR Q56223, NQO3_THETH; P29916, NQO4_PARDE; Q56220, NQO4_THETH; DR P29917, NQO5_PARDE; Q56219, NQO5_THETH; P29918, NQO6_PARDE; DR Q56218, NQO6_THETH; P29919, NQO7_PARDE; Q56217, NQO7_THETH; DR P29920, NQO8_PARDE; Q60019, NQO8_THETH; P29921, NQO9_PARDE; DR Q56224, NQO9_THETH; P29922, NQOA_PARDE; Q56225, NQOA_THETH; DR P29923, NQOB_PARDE; Q56226, NQOB_THETH; P29924, NQOC_PARDE; DR Q56227, NQOC_THETH; P29925, NQOD_PARDE; Q56228, NQOD_THETH; DR P29926, NQOE_PARDE; Q56229, NQOE_THETH; O68852, NUA1_RHIME; DR P56895, NUA2_RHIME; O68853, NUB1_RHIME; P56897, NUB2_RHIME; DR O68854, NUC1_RHIME; P56896, NUC2_RHIME; P57254, NUCD_BUCAI; DR Q8K9Y5, NUCD_BUCAP; P33599, NUCD_ECOLI; P33902, NUCD_SALTY; DR P56907, NUD1_RHIME; P56908, NUD2_RHIME; P56909, NUE1_RHIME; DR P56910, NUE2_RHIME; P56912, NUF1_RHIME; P56913, NUF2_RHIME; DR P56914, NUG2_RHIME; P56911, NUN2_RHIME; P57252, NUOA_BUCAI; DR Q8K9Y7, NUOA_BUCAP; P33597, NUOA_ECOLI; O85273, NUOA_ERWCA; DR P95181, NUOA_MYCTU; O84969, NUOA_RHOCA; Q92ID5, NUOA_RICCN; DR Q9ZDH1, NUOA_RICPR; O67334, NUOB_AQUAE; P57253, NUOB_BUCAI; DR Q8K9Y6, NUOB_BUCAP; P33598, NUOB_ECOLI; O85274, NUOB_ERWCA; DR P95180, NUOB_MYCTU; O84970, NUOB_RHOCA; Q92ID6, NUOB_RICCN; DR Q9ZDH2, NUOB_RICPR; P95179, NUOC_MYCTU; Q9JX80, NUOC_NEIMA; DR Q9K1C1, NUOC_NEIMB; O84971, NUOC_RHOCA; Q9ZDH3, NUOC_RICPR; DR Q9PM99, NUOD_CAMJE; Q9RU89, NUOD_DEIRA; P95178, NUOD_MYCTU; DR O07310, NUOD_RHOCA; Q9ZDH4, NUOD_RICPR; O66842, NUOE_AQUAE; DR P57255, NUOE_BUCAI; Q8K9Y4, NUOE_BUCAP; P33601, NUOE_ECOLI; DR P95177, NUOE_MYCTU; Q92ID9, NUOE_RICCN; Q9ZDH5, NUOE_RICPR; DR P33903, NUOE_SALTY; O66841, NUOF_AQUAE; P57256, NUOF_BUCAI; DR Q8K9Y3, NUOF_BUCAP; P31979, NUOF_ECOLI; P95176, NUOF_MYCTU; DR O07948, NUOF_RHOCA; Q92JB2, NUOF_RICCN; Q9ZE33, NUOF_RICPR; DR P33901, NUOF_SALTY; Q9XAQ9, NUOF_STRCO; P57257, NUOG_BUCAI; DR Q8K9Y2, NUOG_BUCAP; P33602, NUOG_ECOLI; P95175, NUOG_MYCTU; DR Q92G92, NUOG_RICCN; Q9ZCF6, NUOG_RICPR; P33900, NUOG_SALTY; DR Q9XAR0, NUOG_STRCO; P57258, NUOH_BUCAI; Q8K9Y1, NUOH_BUCAP; DR P33603, NUOH_ECOLI; P95174, NUOH_MYCTU; P42032, NUOH_RHOCA; DR Q92G93, NUOH_RICCN; Q9ZCF7, NUOH_RICPR; Q60010, NUOH_SALTY; DR P57259, NUOI_BUCAI; Q8K9Y0, NUOI_BUCAP; P33604, NUOI_ECOLI; DR P95173, NUOI_MYCTU; P42031, NUOI_RHOCA; Q92G94, NUOI_RICCN; DR Q9ZCF8, NUOI_RICPR; P57260, NUOJ_BUCAI; Q8K9X9, NUOJ_BUCAP; DR P33605, NUOJ_ECOLI; P50975, NUOJ_RHOCA; Q92G99, NUOJ_RICCN; DR Q9ZCG3, NUOJ_RICPR; P57261, NUOK_BUCAI; Q8K9X8, NUOK_BUCAP; DR P33606, NUOK_ECOLI; P95171, NUOK_MYCTU; P50940, NUOK_RHOCA; DR Q92G98, NUOK_RICCN; Q9ZCG2, NUOK_RICPR; P57262, NUOL_BUCAI; DR Q8K9X7, NUOL_BUCAP; Q9PMA7, NUOL_CAMJE; P33607, NUOL_ECOLI; DR O86350, NUOL_MYCTU; Q9JX92, NUOL_NEIMA; Q9K1B0, NUOL_NEIMB; DR P50939, NUOL_RHOCA; Q92G97, NUOL_RICCN; Q9ZCG1, NUOL_RICPR; DR Q9XAR5, NUOL_STRCO; P57263, NUOM_BUCAI; Q8K9X6, NUOM_BUCAP; DR P31978, NUOM_ECOLI; O53307, NUOM_MYCTU; P50974, NUOM_RHOCA; DR Q92G96, NUOM_RICCN; Q9ZCG0, NUOM_RICPR; P57264, NUON_BUCAI; DR Q8K9X5, NUON_BUCAP; P33608, NUON_ECOLI; O53308, NUON_MYCTU; DR P50973, NUON_RHOCA; Q92HH5, NUON_RICCN; Q9ZD13, NUON_RICPR; // ID 1.6.99.6 DE NADPH dehydrogenase (quinone). CA NADPH + acceptor = NADP(+) + reduced acceptor. CF Flavoprotein. CC -!- Menaquinone can act as acceptor. CC -!- Inhibited by dicoumarol and folic acid derivatives but not by CC 2,4-dinitrophenol. // ID 1.6.99.7 DE Dihydropteridine reductase. CA NAD(P)H + 6,7-dihydropteridine = NAD(P)(+) + CA 5,6,7,8-tetrahydropteridine. CC -!- The substrate is the quinoid form of dihydropteridine. CC -!- Not identical with EC 1.5.1.3. DI Phenylketonuria with progressive neurologic disorder I; MIM:261630. PR PROSITE; PDOC00060; DR P09417, DHPR_HUMAN; P11348, DHPR_RAT ; Q03331, FHP_CANNO ; DR P24232, HMPA_ECOLI; P26353, HMPA_SALTY; P38489, NFNB_ECOLI; // ID 1.6.99.8 DE Transferred entry: 1.16.1.3. // ID 1.6.99.9 DE Transferred entry: 1.16.1.4. // ID 1.6.99.10 DE Transferred entry: 1.18.1.2. // ID 1.6.99.11 DE Transferred entry: 1.16.1.5. // ID 1.6.99.12 DE Transferred entry: 1.16.1.6. // ID 1.6.99.13 DE Transferred entry: 1.16.1.7. // ID 1.7.1.1 DE Nitrate reductase (NADH). AN Assimilatory nitrate reductase. AN NADH-nitrate reductase. AN NADH-dependent nitrate reductase. AN Assimilatory NADH:nitrate reductase. AN Nitrate reductase (NADH(2)). AN NADH:nitrate oxidoreductase. CA Nitrite + NAD(+) + H(2)O = nitrate + NADH. CF FAD or FMN; Heme; Molybdenum. CC -!- Formerly EC 1.6.6.1. PR PROSITE; PDOC00484; PR PROSITE; PDOC00170; DR P11832, NIA1_ARATH; P39867, NIA1_BRANA; P27967, NIA1_HORVU; DR P17571, NIA1_MAIZE; P16081, NIA1_ORYSA; P39865, NIA1_PHAVU; DR P54233, NIA1_SOYBN; P11605, NIA1_TOBAC; P11035, NIA2_ARATH; DR P39868, NIA2_BRANA; P27969, NIA2_HORVU; P39866, NIA2_PHAVU; DR P39870, NIA2_SOYBN; P08509, NIA2_TOBAC; P49102, NIA3_MAIZE; DR Q01170, NIA_CHLVU ; P43101, NIA_CICIN ; P17569, NIA_CUCMA ; DR P39869, NIA_LOTJA ; P39882, NIA_LOTTE ; P17570, NIA_LYCES ; DR P36859, NIA_PETHY ; P23312, NIA_SPIOL ; P36841, NIA_VOLCA ; // ID 1.7.1.2 DE Nitrate reductase (NAD(P)H). AN Assimilatory nitrate reductase. AN Assimilatory NAD(P)H-nitrate reductase. AN NAD(P)H bispecific nitrate reductase. AN Nitrate reductase (reduced nicotinamide adenine dinucleotide AN (phosphate)). AN Nitrate reductase NAD(P)H. AN NAD(P)H-nitrate reductase. AN Nitrate reductase [NAD(P)H]. AN NAD(P)H:nitrate oxidoreductase. CA Nitrite + NAD(P)(+) + H(2)O = nitrate + NAD(P)H. CF FAD or FMN; Heme; Molybdenum. CC -!- Formerly EC 1.6.6.2. PR PROSITE; PDOC00484; PR PROSITE; PDOC00170; DR P39871, NIA2_MAIZE; P27968, NIA7_HORVU; P27783, NIA_BETVE ; // ID 1.7.1.3 DE Nitrate reductase (NADPH). AN Assimilatory nitrate reductase. AN Assimilatory reduced nicotinamide adenine dinucleotide phosphate- AN nitrate reductase. AN NADPH-nitrate reductase. AN Assimilatory NADPH-nitrate reductase. AN Triphosphopyridine nucleotide-nitrate reductase. AN NADPH:nitrate reductase. AN Nitrate reductase (NADPH(2)). AN NADPH:nitrate oxidoreductase. CA Nitrite + NADP(+) + H(2)O = nitrate + NADPH. CF FAD; Heme; Molybdenum; Iron-sulfur. CC -!- Formerly EC 1.6.6.3. PR PROSITE; PDOC00484; PR PROSITE; PDOC00170; DR P36858, NIA_ASPNG ; P43100, NIA_BEABA ; P22945, NIA_EMENI ; DR P39863, NIA_FUSOX ; P36842, NIA_LEPMC ; P08619, NIA_NEUCR ; DR P39864, NIA_PHYIN ; P49050, NIA_PICAN ; Q05531, NIA_USTMA ; // ID 1.7.1.4 DE Nitrite reductase [NAD(P)H]. AN Nitrite reductase (reduced nicotinamide adenine dinucleotide AN (phosphate)). AN NADH-nitrite oxidoreductase. AN NADPH-nitrite reductase. AN Assimilatory nitrite reductase. AN Nitrite reductase [NAD(P)H(2)]. AN NAD(P)H:nitrite oxidoreductase. CA Ammonium hydroxide + 3 NAD(P)(+) + H(2)O = nitrite + 3 NAD(P)H. CF FAD; Iron; Siroheme; Iron-sulfur. CC -!- Formerly EC 1.6.6.4. DR P42435, NASD_BACSU; P42436, NASE_BACSU; P08201, NIRB_ECOLI; DR Q06458, NIRB_KLEPN; P23675, NIRD_ECOLI; P40789, NIRD_SALTY; DR P22944, NIR_EMENI ; P43504, NIR_LEPMC ; P38681, NIR_NEUCR ; // ID 1.7.1.5 DE Hyponitrite reductase. AN NADH:hyponitrite oxidoreductase. CA 2 hydroxylamine + 2 NAD(+) = hyponitrous acid + 2 NADH. CF Metal ions. CC -!- Formerly EC 1.6.6.6. // ID 1.7.1.6 DE Azobenzene reductase. AN New coccine (NC)-reductase. AN NC-reductase. AN Azo-dye reductase. AN Orange II azoreductase. AN NAD(P)H:1-(4'-sulfophenylazo)-2-naphthol oxidoreductase. AN Orange I azoreductase. AN Azo reductase. AN Azoreductase. AN Nicotinamide adenine dinucleotide (phosphate) azoreductase. AN NADPH-dependent azoreductase. AN Dimethylaminobenzene reductase. AN p-dimethylaminoazobenzene azoreductase. AN Dibromopropylaminophenylazobenzoic azoreductase. AN N,N-dimethyl-4-phenylazoaniline azoreductase. AN p-aminoazobenzene reductase. AN Methyl red azoreductase. AN NADPH:4-(dimethylamino)azobenzene oxidoreductase. CA N,N-dimethyl-1,4-phenylenediamine + aniline + NADP(+) = CA 4-(dimethylamino)azobenzene + NADPH. CC -!- Formerly EC 1.6.6.7. // ID 1.7.1.7 DE GMP reductase. AN Guanosine 5'-monophosphate oxidoreductase. AN Guanosine 5'-monophosphate reductase. AN NADPH:GMP oxidoreductase (deaminating). AN Guanosine monophosphate reductase. AN Guanylate reductase. AN NADPH:guanosine-5'-phosphate oxidoreductase (deaminating). AN Guanosine 5'-phosphate reductase. CA Inosine 5'-phosphate + NH(3) + NADP(+) = guanosine 5'-phosphate + CA NADPH. CC -!- Formerly EC 1.6.6.8. PR PROSITE; PDOC00391; DR P36959, GMP1_HUMAN; Q9DCZ1, GMP1_MOUSE; Q9Z244, GMP1_RAT ; DR Q9P2T1, GMP2_HUMAN; Q99L27, GMP2_MOUSE; P27442, GMPR_ASCSU; DR O16294, GMPR_CAEEL; Q9NJD8, GMPR_ONCVO; P59075, GMPR_PHYIN; DR P57300, GUAC_BUCAI; Q8K9U0, GUAC_BUCAP; P59443, GUAC_BUCBP; DR Q8X984, GUAC_ECO57; P15344, GUAC_ECOLI; Q8Z9F9, GUAC_SALTI; DR Q8ZRT5, GUAC_SALTY; Q9KMW9, GUAC_VIBCH; Q8D632, GUAC_VIBVU; DR Q8ZBI2, GUAC_YERPE; // ID 1.7.1.8 DE Deleted entry. // ID 1.7.1.9 DE Nitroquinoline-N-oxide reductase. AN 4-nitroquinoline 1-oxide reductase. AN 4NQO reductase. AN NAD(P)H:4-nitroquinoline-N-oxide oxidoreductase. CA 4-(hydroxyamino)quinoline N-oxide + 2 NAD(P)(+) + H(2)O = CA 4-nitroquinoline N-oxide + 2 NAD(P)H. CC -!- Formerly EC 1.6.6.10. // ID 1.7.1.10 DE Hydroxylamine reductase (NADH). AN Hydroxylamine reductase. AN Ammonium dehydrogenase. AN NADH-hydroxylamine reductase. AN N-hydroxy amine reductase. AN Hydroxylamine reductase (NADH). AN NADH:hydroxylamine oxidoreductase. CA NH(3) + NAD(+) + H(2)O = hydroxylamine + NADH. CC -!- Also acts on some hydroxamates. CC -!- Formerly EC 1.6.6.11. // ID 1.7.1.11 DE 4-(dimethylamino)phenylazoxybenzene reductase. AN N,N-dimethyl-p-aminoazobenzene oxide reductase. AN Dimethylaminoazobenzene N-oxide reductase. AN NADPH-dependent DMAB N-oxide reductase. AN NADPH:4-(dimethylamino)phenylazoxybenzene oxidoreductase. CA 4-(dimethylamino)phenylazobenzene + NADP(+) = CA 4-(dimethylamino)phenylazoxybenzene + NADPH. CC -!- Formerly EC 1.6.6.12. // ID 1.7.1.12 DE N-hydroxy-2-acetamidofluorene reductase. AN N-hydroxy-2-acetylaminofluorene reductase. AN NAD(P)H:N-hydroxy-2-acetamidofluorene N-oxidoreductase. CA 2-acetamidofluorene + NAD(P)(+) + H(2)O = N-hydroxy-2- CA acetamidofluorene + NAD(P)H. CC -!- Also acts, more slowly, on N-hydroxy-4-acetamidobiphenyl. CC -!- Formerly EC 1.6.6.13. // ID 1.7.2.1 DE Nitrite reductase (NO-forming). AN Nitrite reductase. AN Pseudomonas cytochrome oxidase. AN Cd-cytochrome nitrite reductase. AN [Nitrite reductase (cytochrome)] [misleading, see comments.]. AN Cytochrome c-551:O(2), NO(2)+ oxidoreductase. AN Cytochrome CD. AN Cytochrome cd1. AN Hydroxylamine (acceptor) reductase. AN Methyl viologen-nitrite reductase. AN Nitrite reductase (cytochrome; NO-forming). CA Nitric oxide + H(2)O + ferricytochrome c = nitrite + ferrocytochrome c. CF Copper or Iron; FAD. CC -!- The reaction is catalyzed by two types of enzymes, found in the CC perimplasm of denitrifying bacteria. CC -!- One type comprises proteins containing multiple copper centres, CC the other a heme protein, cytochrome cd(1). CC -!- Acceptors include c-type cytochromes such as cytochrome c-550 or CC cytochrome c-551 from Paracoccus denitrificans or Pseudomonas CC aeruginosa, and small blue copper proteins such as azurin and CC pseudoazurin. CC -!- Cytochrome cd(1) also has oxidase and hydroxylamine reductase CC activities. CC -!- May also catalyze the reaction of EC 1.7.99.1 since this is a CC well-known activity of cytochrome cd(1). CC -!- Formerly EC 1.6.6.5, EC 1.7.99.3 and EC 1.9.3.2. DR Q92Z29, NIRK_RHIME; Q51700, NIRS_PARDE; P72181, NIRS_PARPN; DR P24474, NIRS_PSEAE; P24040, NIRS_PSEST; P25006, NIR_ACHCY ; DR P38501, NIR_ALCFA ; P81445, NIR_ALCXX ; Q06006, NIR_PSECL ; DR Q01537, NIR_RHIGA ; Q60214, NIR_RHIHE ; Q53239, NIR_RHOSH ; // ID 1.7.2.2 DE Nitrite reductase (cytochrome; ammonia-forming). AN Cytochrome c nitrite reductase. AN Multiheme nitrite reductase. AN Cytochrome c552. CA Ammonia + 2 H(2)O + 6 ferricytochrome c = nitrite + CA 6 ferrocytochrome c + 7 H(+). CF Heme; Calcium. CC -!- The enzyme also reduces nitric oxide and hydroxylamine to CC ammonia, and sulfite to sulfide. DR P32050, NRFA_ECOLI; P45017, NRFA_HAEIN; Q9CPL4, NRFA_PASMU; DR Q8Z1Q9, NRFA_SALTI; Q8ZKF5, NRFA_SALTY; Q9Z4P4, NRFA_SULDE; DR Q9S1E5, NRFA_WOLSU; // ID 1.7.2.3 DE Trimethylamine-N-oxide reductase (cytochrome c). AN TMAO reductase. AN TOR. CA Trimethylamine + 2 (ferricytochrome c)-subunit + H(2)O = CA trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit. CF Bis(molybdopterin guanine dinucleotide)molybdenum cofactor. CC -!- The cytochrome c involved in photosynthetic bacteria is a CC pentahaem protein. CC -!- The reductant is a membrane-bound multiheme cytochrome c. CC -!- Also reduces dimethyl sulfoxide to dimethyl sulfide. DR Q52675, DMSA_RHOCA; P58360, TORA_ECO57; P33225, TORA_ECOLI; DR O87948, TORA_SHEMA; P58362, TORZ_ECO57; P46923, TORZ_ECOLI; DR P44798, TORZ_HAEIN; // ID 1.7.3.1 DE Nitroethane oxidase. AN Nitroethane reductase. CA Nitroethane + H(2)O + O(2) = acetaldehyde + nitrite + H(2)O(2). CC -!- Acts on some other aliphatic nitro-compounds. // ID 1.7.3.2 DE Acetylindoxyl oxidase. CA N-acetylindoxyl + O(2) = N-acetylisatin + H(2)O. // ID 1.7.3.3 DE Urate oxidase. AN Uric acid oxidase. AN Uricase. AN Uricase II. CA Urate + O(2) = 5-hydroxyisourate + H(2)O(2). CF Copper. CC -!- The initial products decompose to form allantoin. PR PROSITE; PDOC00315; DR O04420, URIC_ARATH; Q00511, URIC_ASPFL; Q45697, URIC_BACSB; DR O32141, URIC_BACSU; P34798, URIC_CANLI; P16163, URIC_DROME; DR P22673, URIC_DROPS; O44111, URIC_DROSU; P23194, URIC_DROVI; DR P33282, URIC_EMENI; P25688, URIC_MOUSE; P25689, URIC_PAPHA; DR P53763, URIC_PHAVU; P78609, URIC_PICJA; P16164, URIC_PIG ; DR P11645, URIC_RABIT; P09118, URIC_RAT ; O74409, URIC_SCHPO; DR P04670, URIC_SOYBN; P34799, URID_CANLI; O04104, URID_SOYBN; // ID 1.7.3.4 DE Hydroxylamine oxidase. CA Hydroxylamine + O(2) = nitrite + H(2)O. CF Heme. CC -!- Hemoprotein with 7 c-type hemes and one p-460 type heme per subunit. DR Q50925, HAO_NITEU ; // ID 1.7.3.5 DE 3-aci-nitropropanoate oxidase. CA 3-aci-nitropropanoate + O(2) = 3-oxopropanoate + nitrite + H(2)O(2). CF FMN. CC -!- The primary products of the enzymatic reaction are probably the CC nitropropanoate free radical and superoxide. CC -!- Also acts, more slowly, on 4-aci-nitrobutanoate. // ID 1.7.7.1 DE Ferredoxin--nitrite reductase. CA Ammonia + H(2)O + OH(-) + 3 oxidized ferredoxin = nitrite + 3 reduced CA ferredoxin. CF Heme; Iron. PR PROSITE; PDOC00314; DR P38500, NIR_BETVE ; P17847, NIR_MAIZE ; Q51879, NIR_PHOLA ; DR P05314, NIR_SPIOL ; P39661, NIR_SYNP7 ; // ID 1.7.7.2 DE Ferredoxin--nitrate reductase. AN Assimilatory nitrate reductase. CA Nitrite + H(2)O + 2 oxidized ferredoxin = nitrate + 2 reduced CA ferredoxin. CF Molybdenum; Iron-sulfur. // ID 1.7.99.1 DE Hydroxylamine reductase. AN Hydroxylamine (acceptor) reductase. CA Ammonia + H(2)O + acceptor = hydroxylamine + reduced acceptor. CF Flavoprotein. CC -!- Reduced pyocyanine, methylene blue and flavins act as donors for CC the reduction of hydroxylamine. CC -!- May be identical to EC 1.7.2.1. DR Q51700, NIRS_PARDE; P72181, NIRS_PARPN; P24474, NIRS_PSEAE; DR P24040, NIRS_PSEST; // ID 1.7.99.2 DE Deleted entry. // ID 1.7.99.3 DE Transferred entry: 1.7.2.1. // ID 1.7.99.4 DE Nitrate reductase. AN Respiratory nitrate reductase. CA Nitrite + acceptor = nitrate + reduced acceptor. CC -!- The Pseudomonas enzyme is a cytochrome, but the enzyme from CC Micrococcus halodenitrificans is an iron protein containing CC molybdenum. CC -!- Reduced benzyl viologen and other dyes bring about the reduction of CC nitrate. PR PROSITE; PDOC00392; DR P39185, NAPA_ALCEU; P81186, NAPA_DESDE; P33937, NAPA_ECOLI; DR Q56350, NAPA_PARPN; Q53176, NAPA_RHOSH; O33732, NARB_SHEFR; DR P39458, NARB_SYNP7; P73448, NARB_SYNY3; P42175, NARG_BACSU; DR P09152, NARG_ECOLI; P42176, NARH_BACSU; P11349, NARH_ECOLI; DR P42177, NARI_BACSU; P11350, NARI_ECOLI; P42178, NARJ_BACSU; DR P11351, NARJ_ECOLI; P19316, NARV_ECOLI; P19317, NARW_ECOLI; DR P19318, NARY_ECOLI; P19319, NARZ_ECOLI; Q06457, NASA_KLEPN; DR P42434, NASC_BACSU; // ID 1.7.99.5 DE 5,10-methylenetetrahydrofolate reductase (FADH). CA 5-methyltetrahydrofolate + acceptor = 5,10-methylenetetrahydrofolate + CA reduced acceptor. CF FAD. CC -!- Formerly EC 1.1.1.68 and EC 1.1.99.15. DR O67422, METF_AQUAE; P57154, METF_BUCAI; Q8KA62, METF_BUCAP; DR P00394, METF_ECOLI; P71319, METF_ERWCA; P45208, METF_HAEIN; DR P11003, METF_SALTY; O54235, METF_STRLI; // ID 1.7.99.6 DE Nitrous-oxide reductase. CA N(2) + H(2)O + acceptor = nitrous oxide + reduced acceptor. CF Copper. CC -!- Reduced viologens or methylene blue act as donors for the reduction CC of nitrous oxide. DR P94127, NOSZ_ACHCY; Q59105, NOSZ_ALCEU; Q51705, NOSZ_PARDE; DR P19573, NOSZ_PSEST; Q59746, NOSZ_RHIME; Q9HYL2, NSZ1_PSEAE; DR Q01710, NSZ2_PSEAE; // ID 1.7.99.7 DE Nitric-oxide reductase. CA Nitrous oxide + acceptor + H(2)O = 2 nitric oxide + reduced acceptor. CC -!- A heterodimer of cytochromes b and c. CC -!- Phenazine methosulfate can act as acceptor. DR Q59647, NORB_PSEAE; P98008, NORB_PSEST; Q51662, NORC_PARDE; DR O50651, NORC_PARHA; Q59646, NORC_PSEAE; Q52527, NORC_PSEST; DR O06844, NORC_RHOSH; // ID 1.8.1.1 DE Deleted entry. // ID 1.8.1.2 DE Sulfite reductase (NADPH). CA H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH. CF FAD; FMN; Heme. PR PROSITE; PDOC00314; DR P57502, CYSI_BUCAI; P17846, CYSI_ECOLI; P17845, CYSI_SALTY; DR P52673, CYSI_THIRO; P57503, CYSJ_BUCAI; Q8K9D3, CYSJ_BUCAP; DR P38038, CYSJ_ECOLI; P38039, CYSJ_SALTY; P52674, CYSJ_THIRO; DR Q09878, MT10_SCHPO; P39692, MT10_YEAST; // ID 1.8.1.3 DE Hypotaurine dehydrogenase. CA Hypotaurine + H(2)O + NAD(+) = taurine + NADH. CF Molybdenum; Heme. // ID 1.8.1.4 DE Dihydrolipoamide dehydrogenase. AN Lipoamide reductase (NADH). AN E3 component of alpha-ketoacid dehydrogenase complexes. AN Lipoyl dehydrogenase. AN Dihydrolipoyl dehydrogenase. AN Diaphorase. CA Dihydrolipoamide + NAD(+) = lipoamide + NADH. CF FAD. CC -!- Component of the multienzyme pyruvate dehydrogenase complex and CC 2-oxoglutarate dehydrogenase complex. CC -!- Formerly EC 1.6.4.3. DI Congenital infantile lactic acidosis; MIM:246900. PR PROSITE; PDOC00073; DR P11959, DLD1_BACST; P21880, DLD1_BACSU; P09063, DLD1_PSEPU; DR P54533, DLD2_BACSU; P31052, DLD2_PSEPU; O34324, DLD3_BACSU; DR P31046, DLD3_PSEPU; P35484, DLDH_ACHLA; P52992, DLDH_ALCEU; DR P18925, DLDH_AZOVI; P57303, DLDH_BUCAI; Q8K9T7, DLDH_BUCAP; DR P49819, DLDH_CANFA; Q9PJI3, DLDH_CHLMU; Q9Z773, DLDH_CHLPN; DR Q8KCW2, DLDH_CHLTE; O84561, DLDH_CHLTR; O50311, DLDH_CHLVI; DR P00391, DLDH_ECOLI; P43784, DLDH_HAEIN; Q04829, DLDH_HALVO; DR P09622, DLDH_HUMAN; O08749, DLDH_MOUSE; P47513, DLDH_MYCGE; DR Q50068, DLDH_MYCLE; P75393, DLDH_MYCPN; O53747, DLDH_MYCTU; DR P31023, DLDH_PEA ; P09623, DLDH_PIG ; P14218, DLDH_PSEFL; DR O05940, DLDH_RHIET; P95596, DLDH_RHOCA; O00087, DLDH_SCHPO; DR P80503, DLDH_SOLTU; Q59822, DLDH_STAAM; P72740, DLDH_SYNY3; DR Q04933, DLDH_TRYBB; P90597, DLDH_TRYCR; Q9KPF6, DLDH_VIBCH; DR O50286, DLDH_VIBPA; P09624, DLDH_YEAST; P50970, DLDH_ZYMMO; DR O18480, DLHD_MANSE; // ID 1.8.1.5 DE 2-oxopropyl-CoM reductase (carboxylating). AN NADPH:2-(2-ketopropylthio)ethanesulfonate oxidoreductase/carboxylase. AN NADPH:2-ketopropyl-coenzyme M oxidoreductase/carboxylase. AN 2-KPCC. CA 2-mercaptoethanesulfonate + acetoacetate + NADP(+) = CA 2-(2-oxopropylthio)ethanesulfonate + CO(2) + NADPH. CC -!- Also acts on thioethers longer in chain length on the oxo side, CC e.g. 2-oxobutyl-CoM, but this portion must be attached to CoM CC (2-mercaptoethanesulfonate); no CoM analogs will substitute. CC -!- This enzyme forms component II of a four-component enzyme system CC {comprising EC.4.2.99.19 (component I), EC 1.8.1.5 (component II), CC EC 1.1.1.268 (component III) and EC 1.1.1.269 (component IV)} that CC is involved in epoxyalkane carboxylation in Xanthobacter sp. CC strain Py2. // ID 1.8.1.6 DE Cystine reductase. AN Cystine reductase (NADH). AN NADH-dependent cystine reductase. AN Cystine reductase (NADH). AN NADH:L-cystine oxidoreductase. CA 2 L-cysteine + NAD(+) = L-cystine + NADH. CC -!- Formerly EC 1.6.4.1. // ID 1.8.1.7 DE Glutathione-disulfide reductase. AN Glutathione reductase. AN Glutathione reductase (NADPH). AN NADPH-glutathione reductase. AN GSH reductase. AN GSSG reductase. AN NADPH-GSSG reductase. AN Glutathione S-reductase. AN NADPH:oxidized-glutathione oxidoreductase. CA 2 glutathione + NADP(+) = glutathione disulfide + NADPH. CF FAD. CC -!- Activity is dependent on a redox-active disulfide in each of the CC active centres. CC -!- Formerly EC 1.6.4.2. DI Hemolytic anemia due to glutathione reductase deficiency; MIM:138300. PR PROSITE; PDOC00073; DR P42770, GSHC_ARATH; P27456, GSHC_PEA ; P48640, GSHC_SOYBN; DR Q43154, GSHC_SPIOL; P80461, GSHC_TOBAC; P48638, GSHR_ANASP; DR P48641, GSHR_ARATH; O04955, GSHR_BRARP; P48639, GSHR_BURCE; DR P30635, GSHR_CAEEL; P06715, GSHR_ECOLI; P43783, GSHR_HAEIN; DR P00390, GSHR_HUMAN; P47791, GSHR_MOUSE; P48642, GSHR_ORYSA; DR Q43621, GSHR_PEA ; O15770, GSHR_PLAF7; Q94655, GSHR_PLAFK; DR P23189, GSHR_PSEAE; P78965, GSHR_SCHPO; P11804, GSHR_SPISP; DR Q60151, GSHR_STRTR; P41921, GSHR_YEAST; // ID 1.8.1.8 DE Protein-disulfide reductase. AN Protein disulphide reductase. AN Insulin-glutathione transhydrogenase. AN Disulfide reductase. AN NAD(P)H:protein-disulfide oxidoreductase. CA Protein dithiol + NAD(P)+ = protein disulfide + NAD(P)H. CC -!- Formerly EC 1.6.4.4. DR Q9PHR3, DSBD_CAMJE; P58162, DSBD_ECO57; P36655, DSBD_ECOLI; DR P44919, DSBD_HAEIN; Q9JTL9, DSBD_NEIMA; Q9JYM0, DSBD_NEIMB; DR Q9XDB2, DSBD_PANCI; Q9CP40, DSBD_PASMU; Q9KJZ3, DSBD_PSESP; DR Q8XV41, DSBD_RALSO; Q8Z1A8, DSBD_SALTI; Q8ZKC3, DSBD_SALTY; DR Q9KNN1, DSBD_VIBCH; Q8ZIY9, DSBD_YERPE; Q9HUW5, DSD1_PSEAE; DR Q9I104, DSD2_PSEAE; P33636, THI2_ECOLI; // ID 1.8.1.9 DE Thioredoxin-disulfide reductase. AN NADP-thioredoxin reductase. AN NADPH-thioredoxin reductase. AN Thioredoxin reductase (NADPH). AN NADPH:oxidized thioredoxin oxidoreductase. CA Thioredoxin + NADP(+) = thioredoxin disulfide + NADPH. CC -!- May be identical to EC 1.8.1.10. CC -!- Formerly EC 1.6.4.5. PR PROSITE; PDOC00496; DR Q39243, TRB1_ARATH; P29509, TRB1_YEAST; Q39242, TRB2_ARATH; DR P38816, TRB2_YEAST; P91938, TRX1_DROME; Q9VNT5, TRX2_DROME; DR O66790, TRXB_AQUAE; P80880, TRXB_BACSU; P94284, TRXB_BORBU; DR O62768, TRXB_BOVIN; P57399, TRXB_BUCAI; P81433, TRXB_BUCAP; DR Q17745, TRXB_CAEEL; Q9PKT7, TRXB_CHLMU; Q9Z8M4, TRXB_CHLPN; DR O84101, TRXB_CHLTR; P52213, TRXB_CLOLI; P39916, TRXB_COXBU; DR P09625, TRXB_ECOLI; P50971, TRXB_EUBAC; P43788, TRXB_HAEIN; DR Q9ZL18, TRXB_HELPJ; P56431, TRXB_HELPY; Q16881, TRXB_HUMAN; DR Q928B5, TRXB_LISIN; O32823, TRXB_LISMO; Q9JMH6, TRXB_MOUSE; DR P47348, TRXB_MYCGE; P46843, TRXB_MYCLE; P75531, TRXB_MYCPN; DR Q98PK9, TRXB_MYCPU; O30973, TRXB_MYCSM; P52214, TRXB_MYCTU; DR P51978, TRXB_NEUCR; P43496, TRXB_PENCH; Q25861, TRXB_PLAF5; DR Q92I02, TRXB_RICCN; Q9ZD97, TRXB_RICPR; Q92375, TRXB_SCHPO; DR Q05741, TRXB_STRCL; P52215, TRXB_STRCO; O83790, TRXB_TREPA; DR Q9PR71, TRXB_UREPA; Q9KSS4, TRXB_VIBCH; P80892, TRXB_VIBFI; // ID 1.8.1.10 DE CoA-glutathione reductase. AN CoA-glutathione reductase (NADPH). AN Coenzyme A glutathione disulfide reductase. AN NADPH-dependent coenzyme A-SS-glutathione reductase. AN Coenzyme A disulfide-glutathione reductase. AN NADPH:CoA-glutathione oxidoreductase. CA CoA + glutathione + NADP(+) = CoA-glutathione + NADPH. CF Flavoprotein. CC -!- The substrate is a mixed disulfide. CC -!- May be identical to EC 1.8.1.9. CC -!- Formerly EC 1.6.4.6. // ID 1.8.1.11 DE Asparagusate reductase. AN Asparagusate reductase (NADH). AN Asparagusate dehydrogenase. AN Asparagusic dehydrogenase. AN NADH:asparagusate oxidoreductase. CA 3-mercapto-2-mercaptomethylpropanoate + NAD(+) = asparagusate + NADH. CC -!- Also acts on lipoate. CC -!- Formerly EC 1.6.4.7. // ID 1.8.1.12 DE Trypanothione-disulfide reductase. AN Trypanothione reductase. AN N(1),N(8)-bis(glutathionyl)spermidine reductase. AN NADPH:trypanothione oxidoreductase. CA Trypanothione + NADP(+) = trypanothione disulfide + NADPH. CF FAD. CC -!- Trypanothione is the oxidized form of N(1),N(6)-bis(glutathionyl) CC spermidine from the insect-parasitic trypanosomatid Crithidia CC fasciculata. CC -!- The activity is dependent on a redox-active cystine at the active CC centre (cf. EC 1.8.1.7). CC -!- Formerly EC 1.6.4.8. PR PROSITE; PDOC00073; DR P39040, TYTR_CRIFA; P39050, TYTR_LEIDO; P39051, TYTR_TRYBB; DR P13110, TYTR_TRYCO; P28593, TYTR_TRYCR; // ID 1.8.1.13 DE Bis-gamma-glutamylcystine reductase. AN Bis-gamma-glutamylcystine reductase (NADPH). AN NADPH:bis-gamma-glutamylcysteine oxidoreductase. CA 2 gamma-glutamylcysteine + NADP(+) = bis-gamma-glutamylcystine + CA NADPH. CC -!- Highly specific. CC -!- Not identical with EC 1.8.1.7 or EC 1.8.1.14. CC -!- Formerly EC 1.6.4.9. // ID 1.8.1.14 DE CoA-disulfide reductase. AN CoA-disulfide reductase (NADH). AN NADH:CoA-disulfide oxidoreductase. CA 2 CoA + NAD(+) = CoA-disulfide + NADH. CC -!- Not identical with EC 1.8.1.6, EC 1.8.1.7, or EC 1.8.1.13. CC -!- Formerly EC 1.6.4.10. // ID 1.8.1.15 DE Mycothione reductase. AN Mycothiol-disulfide reductase. CA 2 mycothiol + NAD(P)+ = mycothione + NAD(P)H. CF FAD. CC -!- No activity with glutathione, trypanothione or coenzyme A as CC substrate. // ID 1.8.2.1 DE Sulfite dehydrogenase. CA Sulfite + 2 ferricytochrome c + H(2)O = sulfate + 2 ferrocytochrome c. CC -!- Associated with cytochrome c-551. // ID 1.8.2.2 DE Thiosulfate dehydrogenase. AN Tetrathionate synthase. CA 2 thiosulfate + 2 ferricytochrome c = tetrathionate + 2 ferrocytochrome CA c. // ID 1.8.3.1 DE Sulfite oxidase. CA Sulfite + O(2) + H(2)O = sulfate + H(2)O(2). CF Heme; Molybdenum. DI Sulfite oxidase deficiency; MIM:272300. PR PROSITE; PDOC00484; PR PROSITE; PDOC00170; DR P07850, SUOX_CHICK; Q9VWP4, SUOX_DROME; P51687, SUOX_HUMAN; DR Q8R086, SUOX_MOUSE; Q07116, SUOX_RAT ; // ID 1.8.3.2 DE Thiol oxidase. CA 4 R'C(R)SH + O(2) = 2 R'C(R)S-S(R)CR' + 2 H(2)O. CC -!- R may be =S or =O, or a variety of other groups. The enzyme is not CC specific for R'. // ID 1.8.3.3 DE Glutathione oxidase. CA 2 glutathione + O(2) = oxidized glutathione + H(2)O(2). CF FAD. CC -!- Also acts, more slowly, on L-cysteine and several other thiols. // ID 1.8.3.4 DE Methanethiol oxidase. AN Methylmercaptan oxidase. CA Methanethiol + O(2) + H(2)O = formaldehyde + H(2)S + H(2)O(2). // ID 1.8.3.5 DE Prenylcysteine oxidase. AN Prenylcysteine lyase. CA An S-prenyl-L-cysteine + O(2) + H(2)O = a prenal + L-cysteine + CA H(2)O(2). CF FAD. CC -!- Cleaves the thioether bond of S-prenyl-L-cysteines, such as CC S-farnesylcysteine and S-geranylgeranylcysteine. CC -!- N-Acetyl-prenylcysteine and prenylcysteinyl peptides are not CC substrates. CC -!- May represent the final step in the degradation of prenylated CC proteins in mammalian tissues. CC -!- Originally thought to be a simple lyase, EC 4.4.1.18. DR P57681, PCL1_ARATH; Q9UHG3, PCL1_HUMAN; // ID 1.8.4.1 DE Glutathione--homocystine transhydrogenase. CA 2 glutathione + homocystine = oxidized glutathione + 2 homocysteine. CC -!- The reactions catalyzed by this enzyme and by others in this CC subclass may be similar to those catalyzed by EC 2.5.1.18. // ID 1.8.4.2 DE Protein-disulfide reductase (glutathione). AN Glutathione--insulin transhydrogenase. AN Insulin reductase. CA 2 glutathione + protein-disulfide = oxidized glutathione + CA protein-dithiol. CC -!- Reduces insulin and some other proteins. PR PROSITE; PDOC00172; // ID 1.8.4.3 DE Glutathione--CoA-glutathione transhydrogenase. CA CoA + oxidized glutathione = CoA-glutathione + glutathione. // ID 1.8.4.4 DE Glutathione--cystine transhydrogenase. CA 2 glutathione + cystine = oxidized glutathione + 2 cysteine. // ID 1.8.4.5 DE Methionine-S-oxide reductase. AN Methyl sulfoxide reductase I and II. CA L-methionine + oxidized thioredoxin = L-methionine S-oxide + reduced CA thioredoxin. CC -!- Dithiothreitol can replace reduced thioredoxin in the reverse CC reaction. CC -!- Other methyl sulfoxides can replace methionine sulfoxide in the CC reverse reaction. // ID 1.8.4.6 DE Protein-methionine-S-oxide reductase. AN Peptide methionine sulfoxide reductase. AN Peptide Met(O) reductase. CA Protein L-methionine + oxidized thioredoxin = protein L-methionine CA S-oxide + reduced thioredoxin. CC -!- Dithiothreitol, but not 2-mercaptoethanol, can replace reduced CC thioredoxin in the reverse reaction. CC -!- Does not act on free methionine (cf. EC 1.8.4.5). DR P35593, MAB1_STRPN; Q97RX3, MAB2_STRPN; Q8YXZ4, MSA1_ANASP; DR Q9A9I6, MSA1_CAUCR; Q9CFC8, MSA1_LACLA; Q98JV5, MSA1_RHILO; DR Q92SY7, MSA1_RHIME; Q99QD5, MSA1_STAAM; P72622, MSA1_SYNY3; DR Q8YWD8, MSA2_ANASP; Q9A9E9, MSA2_CAUCR; Q9CE42, MSA2_LACLA; DR Q98DV6, MSA2_RHILO; Q92LI5, MSA2_RHIME; Q99U63, MSA2_STAAM; DR Q93P63, MSA2_STAAW; P72800, MSA2_SYNY3; Q92Y45, MSA3_RHIME; DR Q9AL99, MSAB_ACTAC; Q93KF3, MSAB_CAMFE; P45213, MSAB_HAEIN; DR Q9ZMK8, MSAB_HELPJ; O25011, MSAB_HELPY; P14930, MSAB_NEIGO; DR Q9JWM8, MSAB_NEIMA; Q9K1N8, MSAB_NEIMB; Q9LAM9, MSAB_STRGC; DR Q938P0, MSAB_STRP3; Q8P046, MSAB_STRP8; Q99YT1, MSAB_STRPY; DR O83641, MSAB_TREPA; Q9KLX6, MSAB_VIBCH; Q92RA4, MSB1_RHIME; DR Q92Y46, MSB2_RHIME; P54150, MSRA_ARATH; Q9KAN8, MSRA_BACHD; DR P54154, MSRA_BACSU; P54149, MSRA_BOVIN; P54151, MSRA_BRANA; DR Q8YDE7, MSRA_BRUME; Q9PHN0, MSRA_CAMJE; Q97MV3, MSRA_CLOAB; DR Q8XH97, MSRA_CLOPE; Q9APY4, MSRA_CORML; Q9RTB6, MSRA_DEIRA; DR Q8XCG3, MSRA_ECO57; P27110, MSRA_ECOLI; Q9ZEQ8, MSRA_ERWCH; DR P54152, MSRA_FRAAN; Q9HQG0, MSRA_HALN1; Q9UJ68, MSRA_HUMAN; DR Q9SEC2, MSRA_LACSA; Q92AE8, MSRA_LISIN; Q8Y640, MSRA_LISMO; DR P54153, MSRA_LYCES; O26635, MSRA_METTH; P47648, MSRA_MYCGE; DR Q9CCZ3, MSRA_MYCLE; P75188, MSRA_MYCPN; Q98PE5, MSRA_MYCPU; DR P96814, MSRA_MYCTU; Q93S39, MSRA_OCHAN; Q9CN40, MSRA_PASMU; DR Q9HUF1, MSRA_PSEAE; O69761, MSRA_PSEFL; Q8Y1C6, MSRA_RALSO; DR Q8Z150, MSRA_SALTI; Q8ZK71, MSRA_SALTY; Q09859, MSRA_SCHPO; DR Q9EWF7, MSRA_STRCO; Q8K8E4, MSRA_STRP3; Q8P272, MSRA_STRP8; DR Q9A149, MSRA_STRPY; Q97Y45, MSRA_SULSO; Q9AJF7, MSRA_THEVU; DR Q9PQK2, MSRA_UREPA; Q9KP30, MSRA_VIBCH; Q8PNY8, MSRA_XANAC; DR Q8VS50, MSRA_XANCH; Q8PCA6, MSRA_XANCP; Q9PC45, MSRA_XYLFA; DR Q87D27, MSRA_XYLFT; P40029, MSRA_YEAST; Q8ZB94, MSRA_YERPE; DR Q8UGX7, MSRB_AGRT5; Q9KCX2, MSRB_BACHD; P54155, MSRB_BACSU; DR Q89EM9, MSRB_BRAJA; Q8YBR7, MSRB_BRUME; Q9A6B1, MSRB_CAUCR; DR Q97IU0, MSRB_CLOAB; Q9ZNJ9, MSRB_CLOHI; Q8XJZ6, MSRB_CLOPE; DR Q9RUK6, MSRB_DEIRA; P39903, MSRB_ECOLI; Q9XB39, MSRB_ENTFA; DR Q9CJ17, MSRB_LACLA; Q88W33, MSRB_LACPL; Q8F7W8, MSRB_LEPIN; DR Q92AE9, MSRB_LISIN; Q8Y641, MSRB_LISMO; O26807, MSRB_METTH; DR P47686, MSRB_MYCGE; P75129, MSRB_MYCPN; Q9CMB1, MSRB_PASMU; DR Q9I016, MSRB_PSEAE; Q88LQ6, MSRB_PSEPK; Q885Q1, MSRB_PSESM; DR Q8XYL1, MSRB_RALSO; Q8XGD3, MSRB_SALTY; Q99U64, MSRB_STAAM; DR Q93P62, MSRB_STAAW; Q8CSK6, MSRB_STAEP; Q8K7M6, MSRB_STRP3; DR Q8P172, MSRB_STRP8; Q99ZV6, MSRB_STRPY; Q8DJK9, MSRB_SYNEL; DR Q9KQK0, MSRB_VIBCH; Q87MS5, MSRB_VIBPA; Q8D849, MSRB_VIBVU; DR Q9PF29, MSRB_XYLFA; Q87AJ9, MSRB_XYLFT; Q8ZEK7, MSRB_YERPE; // ID 1.8.4.7 DE Enzyme-thiol transhydrogenase (glutathione-disulfide). AN [Xanthine-dehydrogenase]:oxidized-glutathione S-oxidoreductase. AN Enzyme-thiol transhydrogenase (oxidized-glutathione). AN Glutathione-dependent thiol:disulfide oxidoreductase. AN Thiol:disulphide oxidoreductase. CA [Xanthine dehydrogenase] + glutathione disulfide = [xanthine oxidase] CA + 2 glutathione. CC -!- Converts EC 1.1.1.204 into EC 1.1.3.22 in the presence of CC glutathione disulfide. CC -!- Also reduces the disulfide bond of ricin. CC -!- Not inhibited by Cu(2+) or thiol reagents. // ID 1.8.4.8 DE Phosphoadenylyl-sulfate reductase (thioredoxin). AN Phosphoadenosine-phosphosulfate reductase. AN PAPS reductase, thioredoxin-dependent. AN PAdoPS reductase. AN Thioredoxin:adenosine 3'-phosphate 5'-phosphosulfate reductase. AN 3'-phosphoadenylylsulfate reductase. AN Thioredoxin:3'-phospho-adenylylsulfate reductase. AN PAPS sulfotransferase. AN PAPS reductase. AN Phosphoadenosine-phosphosulfate reductase. CA Adenosine 3',5'-bisphosphate + sulfite + oxidized thioredoxin = CA 3'-phosphoadenylyl sulfate + reduced thioredoxin. CC -!- Specific for PAPS. CC -!- The enzyme from E.coli will use thioredoxins from other species. CC -!- Formerly EC 1.8.99.4. DR P94498, CYH1_BACSU; O06737, CYH2_BACSU; Q8UH67, CYSH_AGRT5; DR Q9KCT3, CYSH_BACHD; P57501, CYSH_BUCAI; P56860, CYSH_DEIRA; DR Q8X7U3, CYSH_ECO57; Q8FEI9, CYSH_ECOL6; P17854, CYSH_ECOLI; DR P71752, CYSH_MYCTU; O05927, CYSH_PSEAE; Q98GP9, CYSH_RHILO; DR P56891, CYSH_RHIME; O33579, CYSH_RHITR; Q8Z460, CYSH_SALTI; DR P17853, CYSH_SALTY; Q8EB01, CYSH_SHEON; Q55309, CYSH_SYNP7; DR P72794, CYSH_SYNY3; P52672, CYSH_THIRO; Q9KUX2, CYSH_VIBCH; DR Q87L92, CYSH_VIBPA; Q8CWK6, CYSH_VIBVU; Q8PHC7, CYSH_XANAC; DR Q8P607, CYSH_XANCP; Q9PD82, CYSH_XYLFA; Q87DH1, CYSH_XYLFT; DR P56859, MT16_EMENI; Q10270, MT16_SCHPO; P18408, MT16_YEAST; // ID 1.8.4.9 DE Adenylyl-sulfate reductase (glutathione). AN Plant-type 5'-adenylylsulfate reductase. AN 5'-adenylylsulfate reductase. AN AMP,sulfite:oxidized-glutathione oxidoreductase (adenosine-5'- AN phosphosulfate-forming). CA AMP + sulfite + glutathione disulfide = adenylyl sulfate + 2 CA glutathione. CC -!- This enzyme differs from EC 1.8.99.2, in using glutathione as the CC reductant. CC -!- Glutathione can be replaced by gamma-glutamylcysteine or CC dithiothreitol, but not by thioredoxin, glutaredoxin or CC mercaptoethanol. CC -!- The enzyme from Arabidopsis thaliana contains a glutaredoxin-like CC domain. CC -!- The enzyme is also found in other photosynthetic eukaryotes, e.g., CC the Madagascar periwinkle, Catharanthus roseus and the hollow green CC seaweed, Enteromorpha intestinalis. DR P92979, APR1_ARATH; P92981, APR2_ARATH; P92980, APR3_ARATH; // ID 1.8.5.1 DE Glutathione dehydrogenase (ascorbate). CA 2 glutathione + dehydroascorbate = oxidized glutathione + ascorbate. // ID 1.8.6.1 DE Transferred entry: 2.5.1.18. // ID 1.8.7.1 DE Sulfite reductase (ferredoxin). CA H(2)S + 3 oxidized ferredoxin + 3 H(2)O = sulfite + 3 reduced ferredoxin. CF Iron. PR PROSITE; PDOC00314; DR P30008, SIR_SYNP7 ; P72854, SIR_SYNY3 ; // ID 1.8.99.1 DE Sulfite reductase. CA H(2)S + acceptor + 3 H(2)O = sulfite + reduced acceptor. CF Iron. CC -!- A stoichiometry of six molecules of reduced methyl viologen per CC molecule of sulfide formed was found. // ID 1.8.99.2 DE Adenylylsulfate reductase. CA AMP + sulfite + acceptor = adenylylsulfate + reduced acceptor. CF FAD; Iron. CC -!- Methyl viologen can act as acceptor. // ID 1.8.99.3 DE Hydrogensulfite reductase. AN Bisulfite reductase. AN Dissimilatory sulfite reductase. AN Desulfoviridin. AN Desulforubidin. AN Desulfofuscidin. CA (O(3)S.S.SO(3))(2-) + acceptor + 2 H(2)O + OH(-) = 3 (HSO(3))(-) + CA reduced acceptor. CF Iron-sulfur; Siroheme. CC -!- Methyl viologen can act as acceptor. CC -!- A group of sirohemoproteins containing iron-sulfur centres (p-582). DR Q59109, DSRA_ARCFU; O33998, DSRA_CHRVI; Q59110, DSRB_ARCFU; DR P94693, DSVA_DESGI; P45574, DSVA_DESVH; P94694, DSVB_DESGI; DR P45575, DSVB_DESVH; P45573, DSVC_DESVH; // ID 1.8.99.4 DE Transferred entry: 1.8.4.8. // ID 1.9.3.1 DE Cytochrome-c oxidase. AN Cytochrome oxidase. AN Cytochrome a(3). AN Cytochrome aa(3). AN Warburg's respiratory enzyme. AN Complex IV (mitochondrial electron transport). CA 4 ferrocytochrome c + O(2) = 4 ferricytochrome c + 2 H(2)O. CF Copper. CC -!- The reduction of O(2) to water is accompanied by the extrusion of CC four protons from the intramitochondrial compartment. CC -!- Several bacteria appear to contain analogous oxidases. DI Cytochrome-c-oxidase deficiency; MIM:220110. PR PROSITE; PDOC00074; PR PROSITE; PDOC00075; PR PROSITE; PDOC00663; DR P98005, CO13_THETH; P98057, CO14_BRAJA; Q37370, COX1_ACACA; DR P48887, COX1_ALBCO; Q09333, COX1_ALBTU; P80440, COX1_ALLMA; DR P29643, COX1_AMICA; P50656, COX1_ANAPL; P34838, COX1_ANOGA; DR P33504, COX1_ANOQU; P20374, COX1_APILI; O03515, COX1_APTAU; DR Q07063, COX1_ARATH; Q37705, COX1_ARTSF; P24881, COX1_ASCSU; DR Q33820, COX1_ASTPE; Q04440, COX1_BACFI; P16262, COX1_BACP3; DR P24010, COX1_BACSU; P41293, COX1_BALMU; P24983, COX1_BALPH; DR P24794, COX1_BETVU; Q36724, COX1_BLAGE; P00396, COX1_BOVIN; DR P31833, COX1_BRAJA; Q9MIY8, COX1_BRARE; P24893, COX1_CAEEL; DR Q9ZZ64, COX1_CANFA; Q33375, COX1_CANSI; Q36347, COX1_CAPHI; DR O78681, COX1_CARAU; O03521, COX1_CASBE; O03198, COX1_CERSI; DR P18943, COX1_CHICK; P08681, COX1_CHLRE; P50668, COX1_CHOBI; DR P48866, COX1_CHOCR; P50669, COX1_CHOFU; P50670, COX1_CHOOC; DR P50671, COX1_CHORO; P24984, COX1_COTJA; P98003, COX1_CRION; DR P34188, COX1_CROLA; P48867, COX1_CYACA; P24985, COX1_CYPCA; DR O21327, COX1_DASNO; P41310, COX1_DIDMA; O79548, COX1_DINSE; DR Q34345, COX1_DROMA; P00399, COX1_DROME; O03524, COX1_DRONO; DR Q34391, COX1_DROSE; Q34388, COX1_DROSI; P00400, COX1_DROYA; DR Q8W9N4, COX1_DUGDU; P00402, COX1_EMENI; Q33439, COX1_EPHEQ; DR P92477, COX1_EQUAS; P48888, COX1_FELCA; Q36775, COX1_GADMO; DR P29645, COX1_GEOSD; P29646, COX1_GOMVA; P38595, COX1_HALGR; DR P33518, COX1_HALN1; P48868, COX1_HANWI; Q9ZZY9, COX1_HIPAM; DR P48659, COX1_HORSE; P00395, COX1_HUMAN; P20386, COX1_KLULA; DR O03167, COX1_LATCH; P14544, COX1_LEITA; P29647, COX1_LEPOC; DR P29644, COX1_LEPSP; Q36421, COX1_LOCMI; Q34941, COX1_LUMTE; DR P92661, COX1_MACRO; P08742, COX1_MAIZE; P26856, COX1_MARPO; DR P29648, COX1_MEGAT; Q35101, COX1_METSE; P00397, COX1_MOUSE; DR O53290, COX1_MYCTU; P41774, COX1_MYTED; O21079, COX1_MYXGL; DR P03945, COX1_NEUCR; O03539, COX1_NOTPE; P08743, COX1_OENBE; DR P48170, COX1_ONCMY; Q36452, COX1_ORNAN; P14578, COX1_ORYSA; DR P29649, COX1_PANBU; Q9ZXY2, COX1_PAPHA; P12700, COX1_PARLI; DR P05489, COX1_PARTE; Q00502, COX1_PARVE; P12786, COX1_PEA ; DR Q96000, COX1_PECMA; O79672, COX1_PELSU; Q35536, COX1_PETMA; DR Q00527, COX1_PHOVI; Q02211, COX1_PHYME; Q07434, COX1_PHYPO; DR O79876, COX1_PIG ; P25001, COX1_PISOC; O99252, COX1_PLABE; DR O99255, COX1_PLACH; Q02766, COX1_PLAFA; P20681, COX1_PODAN; DR Q95911, COX1_POLOR; P29650, COX1_POLSP; P29651, COX1_POLSX; DR P29652, COX1_POMNI; P92692, COX1_PONPA; Q05143, COX1_PROWI; DR O79429, COX1_RABIT; P05503, COX1_RAT ; O03546, COX1_RHEAM; DR Q08855, COX1_RHILE; O99818, COX1_RHISA; Q96062, COX1_RHIUN; DR P98059, COX1_RHOCA; P33517, COX1_RHOSH; O54069, COX1_RICPR; DR P98001, COX1_SACDO; Q9ZZM6, COX1_SALSA; P29653, COX1_SALTR; DR P29654, COX1_SCAPL; P07657, COX1_SCHPO; O79403, COX1_SCYCA; DR O78749, COX1_SHEEP; P05502, COX1_SORBI; P07506, COX1_SOYBN; DR Q9ZZ52, COX1_SQUAC; O21399, COX1_STRCA; P15544, COX1_STRPU; DR P50676, COX1_SYNVU; Q06473, COX1_SYNY3; P11947, COX1_TETPY; DR Q56408, COX1_THETH; O03554, COX1_TINMA; Q01555, COX1_TRIRU; DR P04371, COX1_TRYBB; P08741, COX1_WHEAT; P00398, COX1_XENLA; DR P00401, COX1_YEAST; P29870, COX2_ACHDO; P50672, COX2_ACOWI; DR P29871, COX2_ADABI; P50692, COX2_AEDAE; P48889, COX2_ALBCO; DR Q09334, COX2_ALBTU; O47870, COX2_ALLMI; P98024, COX2_ALOPA; DR P29655, COX2_AMICA; P98019, COX2_ANAPL; P34840, COX2_ANOGA; DR P33505, COX2_ANOQU; Q37369, COX2_ANTAM; P50267, COX2_APIFL; DR P50268, COX2_APIKO; P20375, COX2_APILI; P50673, COX2_APOSY; DR O03889, COX2_APTAU; Q37706, COX2_ARTSF; P24882, COX2_ASCSU; DR Q37411, COX2_ASTPE; Q04441, COX2_BACFI; Q03438, COX2_BACP3; DR P24011, COX2_BACSU; P41294, COX2_BALMU; P24986, COX2_BALPH; DR P98012, COX2_BETVU; Q37416, COX2_BISBI; P50674, COX2_BOSJA; DR Q37419, COX2_BOSTR; P00404, COX2_BOVIN; O47428, COX2_BRAFL; DR O79417, COX2_BRALA; Q9MIY7, COX2_BRARE; P43369, COX2_BREAN; DR P43370, COX2_BRECS; P43372, COX2_BRENA; P50678, COX2_BUBDE; DR P24894, COX2_CAEEL; P50666, COX2_CAIMO; P50661, COX2_CALGO; DR O47667, COX2_CANAD; O47669, COX2_CANAU; O63855, COX2_CANFA; DR P43373, COX2_CANGA; O47671, COX2_CANME; P98031, COX2_CANSI; DR Q37430, COX2_CAPHI; O78682, COX2_CARAU; O03890, COX2_CASBE; DR P50683, COX2_CAVAP; P26455, COX2_CERAE; P98020, COX2_CERGA; DR O03851, COX2_CERSI; Q37440, COX2_CERUN; P98027, COX2_CHEME; DR P18944, COX2_CHICK; P98025, COX2_CHOBI; P48869, COX2_CHOCR; DR P98026, COX2_CHOFU; P98030, COX2_CHORO; O47670, COX2_CHRBR; DR P50684, COX2_COTJA; P50685, COX2_CRABU; P50662, COX2_CRACA; DR P34189, COX2_CROLA; P29872, COX2_CTEFE; P50693, COX2_CULQU; DR O47668, COX2_CUOAL; P48870, COX2_CYACA; P50686, COX2_CYNVA; DR P24987, COX2_CYPCA; P50679, COX2_DAMPP; P50687, COX2_DASNO; DR P27168, COX2_DAUCA; P98032, COX2_DAUMA; P43374, COX2_DEKBR; DR P41311, COX2_DIDMA; O79549, COX2_DINSE; P29854, COX2_DROAI; DR P29856, COX2_DROAM; P29859, COX2_DROBF; P29860, COX2_DROLO; DR P00408, COX2_DROME; O03891, COX2_DRONO; P29862, COX2_DRONR; DR P29864, COX2_DROPS; P50253, COX2_DROSI; P29865, COX2_DROSU; DR P00409, COX2_DROYA; Q8W9N3, COX2_DUGDU; O47672, COX2_DUSTH; DR P43375, COX2_EENNA; P13588, COX2_EMENI; P92478, COX2_EQUAS; DR P98033, COX2_EULMA; P29873, COX2_EXERO; P48890, COX2_FELCA; DR Q37741, COX2_GADMO; P29874, COX2_GALME; P50688, COX2_GALSE; DR P50680, COX2_GAZSP; P50689, COX2_GEOCP; P29657, COX2_GEOSD; DR P29658, COX2_GOMVA; Q37472, COX2_GORBE; P26456, COX2_GORGO; DR P38596, COX2_HALGR; P48871, COX2_HANWI; P98034, COX2_HAPGR; DR Q9ZZY8, COX2_HIPAM; P48660, COX2_HORSE; P00403, COX2_HUMAN; DR Q96127, COX2_HYLLA; P25312, COX2_HYLSY; P20387, COX2_KLULA; DR P43376, COX2_KLUTH; P98036, COX2_LAGLA; P29875, COX2_LASSP; DR O03848, COX2_LATCH; P14545, COX2_LEITA; P98035, COX2_LEMCA; DR P98047, COX2_LEMVA; P29659, COX2_LEPOC; P29656, COX2_LEPSP; DR P14573, COX2_LOCMI; Q9TA26, COX2_LOXAF; Q37545, COX2_LUMTE; DR O47674, COX2_LYCPI; Q37548, COX2_MACCA; P11948, COX2_MACFA; DR P98038, COX2_MACMU; P92662, COX2_MACRO; P00412, COX2_MAIZE; DR P98037, COX2_MANLE; P26857, COX2_MARPO; P29660, COX2_MEGAT; DR O47496, COX2_METSE; P24988, COX2_MICPE; P00405, COX2_MOUSE; DR Q10375, COX2_MYCTU; Q00227, COX2_MYTED; Q9G2X2, COX2_MYXGL; DR P00411, COX2_NEUCR; O03892, COX2_NOTPE; P98039, COX2_NYCCO; DR O47675, COX2_NYCPR; P05490, COX2_OENBE; P29876, COX2_ONCFA; DR P48171, COX2_ONCMY; Q37718, COX2_ORNAN; P04373, COX2_ORYSA; DR P26457, COX2_PANPA; P50690, COX2_PANTR; P98040, COX2_PAPAN; DR P08306, COX2_PARDE; P12701, COX2_PARLI; P08748, COX2_PARPR; DR P08749, COX2_PARTE; P08744, COX2_PEA ; O79673, COX2_PELSU; DR P29877, COX2_PERAM; Q37595, COX2_PERFA; Q37604, COX2_PETMA; DR Q00528, COX2_PHOVI; Q37596, COX2_PHYHA; Q02212, COX2_PHYME; DR P50667, COX2_PIG ; P25002, COX2_PISOC; P29163, COX2_PNECA; DR P20682, COX2_PODAN; Q96183, COX2_POLOR; P29661, COX2_POLSX; DR P92693, COX2_PONPA; P92721, COX2_PONPP; Q37605, COX2_PONPY; DR P98042, COX2_PROTA; O47676, COX2_PSECP; O47677, COX2_PSEGY; DR O47678, COX2_PSESU; P98049, COX2_RABIT; P00406, COX2_RAT ; DR O03893, COX2_RHEAM; O99819, COX2_RHISA; Q96190, COX2_RHIUN; DR Q03736, COX2_RHOSH; Q9ZDC6, COX2_RICPR; Q37649, COX2_ROULE; DR P43377, COX2_SACEX; Q37677, COX2_SALSA; P29662, COX2_SCAPL; DR P29878, COX2_SCHGR; P21534, COX2_SCHPO; P50691, COX2_SCICA; DR O79404, COX2_SCYCA; O78750, COX2_SHEEP; P98021, COX2_SIMVI; DR P29879, COX2_SITGR; P80498, COX2_SOLTU; P05491, COX2_SOYBN; DR O47679, COX2_SPEVE; Q9ZZ51, COX2_SQUAC; O21400, COX2_STRCA; DR P15545, COX2_STRPU; P29880, COX2_SYMST; P50675, COX2_SYNCA; DR P98054, COX2_SYNVU; Q06474, COX2_SYNY3; P98043, COX2_TARBA; DR P98046, COX2_TARSY; P98044, COX2_THEGE; P98052, COX2_THETH; DR O03895, COX2_TINMA; Q37685, COX2_TRAIM; Q01556, COX2_TRIRU; DR P04372, COX2_TRYBB; P98023, COX2_TRYCR; Q37684, COX2_TUPGL; DR P32646, COX2_VIGUN; O47680, COX2_VULMA; O47681, COX2_VULVU; DR O47673, COX2_VULZE; P00413, COX2_WHEAT; P47918, COX2_WILMR; DR P06029, COX2_WILSA; P00407, COX2_XENLA; P00410, COX2_YEAST; DR P98048, COX2_YPOMA; P29881, COX2_ZOOAN; Q37374, COX3_ACACA; DR Q36952, COX3_AEGCO; O47691, COX3_AEPME; P48891, COX3_ALBCO; DR P80439, COX3_ALLMA; P50657, COX3_ANAPL; P34842, COX3_ANOGA; DR P33508, COX3_ANOQU; O47702, COX3_ANTCE; O47701, COX3_ANTMR; DR P34843, COX3_APILI; P92514, COX3_ARATH; Q33752, COX3_ARBLI; DR Q33845, COX3_ARTSA; Q36309, COX3_ARTSF; P24879, COX3_ASCSU; DR Q33824, COX3_ASTPE; Q04442, COX3_BACFI; Q03439, COX3_BACP3; DR P24012, COX3_BACSU; P41295, COX3_BALMU; P24989, COX3_BALPH; DR P00415, COX3_BOVIN; O47425, COX3_BRALA; Q9MIY4, COX3_BRARE; DR P24891, COX3_CAEEL; Q9ZZ61, COX3_CANFA; Q34214, COX3_CANPA; DR Q96133, COX3_CARAU; O47693, COX3_CEPNA; O03201, COX3_CERSI; DR P18945, COX3_CHICK; P48872, COX3_CHOCR; P34198, COX3_CROLA; DR P48873, COX3_CYACA; P15952, COX3_CYPCA; O47694, COX3_DAMLU; DR O21331, COX3_DASNO; P41312, COX3_DIDMA; O79552, COX3_DINSE; DR P00417, COX3_DROME; P50271, COX3_DROSI; P00418, COX3_DROYA; DR Q8W9N0, COX3_DUGDU; P00421, COX3_EMENI; P92481, COX3_EQUAS; DR P48892, COX3_FELCA; P55777, COX3_GADMO; O47708, COX3_GAZCU; DR O48374, COX3_GAZDA; O48308, COX3_GAZDO; O48346, COX3_GAZGA; DR O47703, COX3_GAZGR; O47709, COX3_GAZLE; O47705, COX3_GAZRU; DR O47710, COX3_GAZSA; O48316, COX3_GAZSU; O47706, COX3_GAZTH; DR P38597, COX3_HALGR; P48874, COX3_HANWI; P32808, COX3_HELAN; DR Q9ZZY5, COX3_HIPAM; P48661, COX3_HORSE; P00414, COX3_HUMAN; DR Q95707, COX3_HYLLA; O03170, COX3_LATCH; P14546, COX3_LEITA; DR O47700, COX3_LITWA; P14574, COX3_LOCMI; O47475, COX3_LOLBL; DR Q34943, COX3_LUMTE; P92665, COX3_MACRO; O47699, COX3_MADGU; DR Q95840, COX3_MAGGR; P09138, COX3_MAIZE; P26858, COX3_MARPO; DR O47491, COX3_METSE; P00416, COX3_MOUSE; Q10385, COX3_MYCTU; DR P41775, COX3_MYTED; O63915, COX3_MYXGL; O47698, COX3_NEOMO; DR P00422, COX3_NEUCR; Q35242, COX3_OCTDO; P08745, COX3_OENBE; DR P20684, COX3_ONCCL; P48172, COX3_ONCMY; P20683, COX3_ONCNE; DR Q36455, COX3_ORNAN; P14852, COX3_ORYSA; O47695, COX3_OUROU; DR Q9ZXX8, COX3_PAPHA; P06030, COX3_PARDE; P12702, COX3_PARLI; DR O47692, COX3_PELCP; O79676, COX3_PELSU; Q35539, COX3_PETMA; DR Q00529, COX3_PHOVI; Q35916, COX3_PIG ; P25003, COX3_PISOC; DR Q36675, COX3_PLAVI; Q02654, COX3_PODAN; Q95914, COX3_POLOR; DR P92696, COX3_PONPA; Q37620, COX3_PROWI; Q37600, COX3_PYLLI; DR O79433, COX3_RABIT; O47696, COX3_RAPCA; O47697, COX3_RAPME; DR P05505, COX3_RAT ; O99822, COX3_RHISA; P80441, COX3_RHIST; DR Q96065, COX3_RHIUN; Q9ZDX3, COX3_RICPR; Q36860, COX3_SALSA; DR P14058, COX3_SCHCO; P14575, COX3_SCHPO; O79407, COX3_SCYCA; DR O21619, COX3_SHEEP; P14853, COX3_SOYBN; Q35826, COX3_SPOFR; DR Q9ZZ48, COX3_SQUAC; O21403, COX3_STRCA; P15546, COX3_STRPU; DR O47690, COX3_SYNCA; P50677, COX3_SYNVU; Q06475, COX3_SYNY3; DR Q37679, COX3_THEAN; O47685, COX3_TRAIM; O47686, COX3_TRAOR; DR O47688, COX3_TRASP; O47687, COX3_TRASR; O47689, COX3_TRAST; DR Q36837, COX3_TRIRU; Q37355, COX3_TRYBO; Q03227, COX3_VICFA; DR P15953, COX3_WHEAT; P00419, COX3_XENLA; P00420, COX3_YEAST; DR Q04452, COX4_BACFI; Q03440, COX4_BACP3; P24013, COX4_BACSU; DR P30815, COX4_DICDI; P06809, COX4_NEUCR; P80327, COX4_ONCMY; DR P77921, COX4_PARDE; P79010, COX4_SCHPO; P04037, COX4_YEAST; DR O93980, COX5_ASPNG; P29505, COX5_DICDI; P06810, COX5_NEUCR; DR O74988, COX5_SCHPO; P26310, COX6_DICDI; Q01359, COX6_NEUCR; DR Q9UTF6, COX6_SCHPO; P00427, COX6_YEAST; P10174, COX7_YEAST; DR P04039, COX8_YEAST; P07255, COX9_YEAST; P00426, COXA_BOVIN; DR P99501, COXA_CANFA; Q94514, COXA_DROME; P20674, COXA_HUMAN; DR O61694, COXA_MANSE; P12787, COXA_MOUSE; P80328, COXA_ONCMY; DR P11240, COXA_RAT ; P82543, COXA_THETH; P80972, COXA_THUOB; DR P00428, COXB_BOVIN; P10606, COXB_HUMAN; P19536, COXB_MOUSE; DR P12075, COXB_RAT ; P80499, COXB_SOLTU; P80974, COXB_THUOB; DR Q42841, COXC_HORVU; P19173, COXC_IPOBA; P80500, COXC_SOLTU; DR P80973, COXC_THUOB; P07471, COXD_BOVIN; Q02221, COXD_HUMAN; DR P43023, COXD_MOUSE; P10817, COXD_RAT ; P13182, COXE_BOVIN; DR Q20779, COXE_CAEEL; O13082, COXE_CYPCA; P20609, COXE_DICDI; DR P12074, COXE_HUMAN; P43024, COXE_MOUSE; O13085, COXE_ONCMY; DR Q9TTT7, COXE_RABIT; P10818, COXE_RAT ; O74471, COXE_SCHPO; DR P80975, COXE_THUOB; P32799, COXE_YEAST; P80329, COXF_ONCMY; DR P00429, COXG_BOVIN; P14854, COXG_HUMAN; P56391, COXG_MOUSE; DR P80430, COXG_RAT ; O94581, COXG_SCHPO; P80976, COXG_THUOB; DR Q01519, COXG_YEAST; P04038, COXH_BOVIN; P09669, COXH_HUMAN; DR P80331, COXH_ONCMY; P11950, COXH_RAT ; P80977, COXH_THUOB; DR P11951, COXI_MOUSE; P80978, COXI_THUOB; P13184, COXJ_BOVIN; DR Q9TR29, COXJ_CANFA; Q9VHS2, COXJ_DROME; P14406, COXJ_HUMAN; DR P48771, COXJ_MOUSE; P80333, COXJ_ONCMY; P35171, COXJ_RAT ; DR Q9TR30, COXJ_SHEEP; P80979, COXJ_THUOB; P07470, COXK_BOVIN; DR Q9TRZ8, COXK_CANFA; P24310, COXK_HUMAN; P56392, COXK_MOUSE; DR P80332, COXK_ONCMY; Q8SPJ9, COXK_PIG ; Q9TR28, COXK_SHEEP; DR P80330, COXL_ONCMY; P13183, COXM_BOVIN; P98053, COXM_BRAJA; DR P24311, COXM_HUMAN; P56393, COXM_MOUSE; P80431, COXM_RAT ; DR P80981, COXM_THUOB; P98000, COXN_BRAJA; P80980, COXN_THUOB; DR P00430, COXO_BOVIN; P15954, COXO_HUMAN; P17665, COXO_MOUSE; DR P80334, COXO_ONCMY; P80432, COXO_RAT ; P80982, COXO_THUOB; DR P10175, COXQ_BOVIN; P48772, COXQ_MOUSE; P80335, COXQ_ONCMY; DR P80336, COXQ_RABIT; P16221, COXQ_RAT ; P80337, COXQ_SHEEP; DR P80983, COXQ_THUOB; P14622, COXR_BOVIN; P10176, COXR_HUMAN; DR Q64445, COXR_MOUSE; P80433, COXR_RAT ; P80984, COXR_THUOB; DR P20610, COXS_DICDI; Q02226, COXT_SOYBN; P08305, CX1A_PARDE; DR P98002, CX1B_PARDE; O46584, CX41_AOTAZ; P00423, CX41_BOVIN; DR O46589, CX41_CEBAP; O46578, CX41_GORGO; P13073, CX41_HUMAN; DR O46580, CX41_HYLAG; O46587, CX41_MANSP; P19783, CX41_MOUSE; DR O46577, CX41_PANTR; O46586, CX41_PERPO; Q95283, CX41_PIG ; DR O46585, CX41_PITPI; O46579, CX41_PONPY; O46588, CX41_PRECR; DR Q9TTT8, CX41_RABIT; P10888, CX41_RAT ; O46582, CX41_SAISC; DR O46590, CX41_SAIUS; O46581, CX41_THEGE; Q9I8U0, CX41_THUOB; DR Q96KJ9, CX42_HUMAN; Q91W29, CX42_MOUSE; Q91Y94, CX42_RAT ; DR P80971, CX42_THUOB; P00424, CX5A_YEAST; P00425, CX5B_YEAST; DR P98055, FIXN_AGRT7; P98056, FIXN_AZOCA; Q03073, FIXN_BRAJA; DR Q05572, FIXN_RHIME; // ID 1.9.3.2 DE Transferred entry: 1.7.2.1. // ID 1.9.6.1 DE Nitrate reductase (cytochrome). CA Ferrocytochrome + nitrate = ferricytochrome + nitrite. // ID 1.9.99.1 DE Iron--cytochrome-c reductase. CA Ferrocytochrome c + Fe(3+) = ferricytochrome c + Fe(2+). CF Iron. // ID 1.10.1.1 DE Trans-acenaphthene-1,2-diol dehydrogenase. CA (+-)-trans-acenaphthene-1,2-diol + NADP(+) = acenaphthenequinone + NADPH. CC -!- Some preparations also utilize NAD(+). // ID 1.10.2.1 DE L-ascorbate--cytochrome-b5 reductase. CA L-ascorbate + ferricytochrome b5 = monodehydroascorbate + CA ferrocytochrome b5. // ID 1.10.2.2 DE Ubiquinol--cytochrome c reductase. AN Ubiquinone-cytochrome c oxidoreductase. AN Cytochrome bc1 complex. AN Complex III (mitochondrial electron transport). CA QH(2) + 2 ferricytochrome c = Q + 2 ferrocytochrome c. CC -!- Contains cytochrome b-562, cytochrome b-566, cytochrome c1, and CC 2-iron ferredoxin. CC -!- Depending on the organism and physiological conditions, either two CC or four protons are extruded from the cytoplasmic to the non- CC cytoplasmic compartment (cf. EC 1.6.99.3). PR PROSITE; PDOC00171; DR P29677, MPPA_SOLTU; P11913, MPPB_NEUCR; P31800, UCR1_BOVIN; DR P43264, UCR1_EUGGR; P31930, UCR1_HUMAN; Q9CZ13, UCR1_MOUSE; DR P49729, UCR1_TOBAC; P07256, UCR1_YEAST; P23004, UCR2_BOVIN; DR P43265, UCR2_EUGGR; P22695, UCR2_HUMAN; Q9DB77, UCR2_MOUSE; DR O60044, UCR2_NEUCR; P32551, UCR2_RAT ; P78761, UCR2_SCHPO; DR P51132, UCR2_TOBAC; P07257, UCR2_YEAST; P51133, UCR3_TOBAC; DR P51134, UCR4_TOBAC; P51135, UCR5_TOBAC; P00129, UCR6_BOVIN; DR Q9GP40, UCR6_ECHMU; O01369, UCR6_FASHE; P14927, UCR6_HUMAN; DR Q9D855, UCR6_MOUSE; O01374, UCR6_SCHMA; P48502, UCR6_SOLTU; DR P49345, UCR7_KLULA; P46268, UCR7_PICJA; O74533, UCR7_SCHPO; DR P00128, UCR7_YEAST; P43266, UCR9_EUGGR; O74433, UCR9_SCHPO; DR P22289, UCR9_YEAST; P00126, UCRH_BOVIN; P07919, UCRH_HUMAN; DR P99028, UCRH_MOUSE; P48504, UCRH_SOLTU; P00127, UCRH_YEAST; DR P13272, UCRI_BOVIN; P51130, UCRI_BRAJA; O31214, UCRI_CHRVI; DR P47985, UCRI_HUMAN; P49727, UCRI_MAIZE; P07056, UCRI_NEUCR; DR P05417, UCRI_PARDE; P20788, UCRI_RAT ; P08500, UCRI_RHOCA; DR P23136, UCRI_RHORU; Q02762, UCRI_RHOSH; P81380, UCRI_RHOVI; DR Q9ZDQ5, UCRI_RICPR; Q09154, UCRI_SCHPO; P37841, UCRI_SOLTU; DR P08067, UCRI_YEAST; P13271, UCRQ_BOVIN; P81247, UCRQ_EQUAR; DR O14949, UCRQ_HUMAN; P49346, UCRQ_KLULA; Q9CQ69, UCRQ_MOUSE; DR P48503, UCRQ_NEUCR; P50523, UCRQ_SCHPO; P46269, UCRQ_SOLTU; DR P08525, UCRQ_YEAST; P00130, UCRX_BOVIN; Q9XY35, UCRX_DROME; DR Q9UDW1, UCRX_HUMAN; P46270, UCRX_SOLTU; P37299, UCRX_YEAST; DR P07552, UCRY_BOVIN; O14957, UCRY_HUMAN; P48505, UCRY_SOLTU; // ID 1.10.3.1 DE Catechol oxidase. AN Diphenol oxidase. AN O-diphenolase. AN Phenolase. AN Polyphenol oxidase. AN Tyrosinase. CA 2 catechol + O(2) = 2 1,2-benzoquinone + 2 H(2)O. CF Copper. CC -!- Also acts on a variety of substituted catechols. CC -!- Many of these enzymes also catalyze the reaction listed under CC EC 1.14.18.1; this is especially true for the classical tyrosinase. PR PROSITE; PDOC00398; DR Q00024, PPO1_AGABI; Q08303, PPOA_LYCES; Q08304, PPOB_LYCES; DR Q06355, PPOB_SOLTU; Q08305, PPOC_LYCES; Q08306, PPOD_LYCES; DR Q08307, PPOE_LYCES; Q08296, PPOF_LYCES; P43309, PPO_MALDO ; DR P43310, PPO_SPIOL ; Q06215, PPO_VICFA ; P43311, PPO_VITVI ; // ID 1.10.3.2 DE Laccase. AN Urishiol oxidase. CA 4 benzenediol + O(2) = 4 benzosemiquinone + 2 H(2)O. CF Copper. CC -!- A group of multi-copper proteins of low specificity. CC -!- Act on both O- and P-quinols, and often acting also on aminophenols CC and phenylenediamine. CC -!- The semiquinone may react further either enzymically or non- CC enzymically. PR PROSITE; PDOC00076; DR Q12541, LAC1_AGABI; Q12570, LAC1_BOTCI; Q03966, LAC1_CRYPA; DR P17489, LAC1_EMENI; P06811, LAC1_NEUCR; Q01679, LAC1_PHLRA; DR Q12729, LAC1_PLEOS; P56193, LAC1_THACU; Q02497, LAC1_TRAHI; DR Q99044, LAC1_TRAVI; Q12542, LAC2_AGABI; P10574, LAC2_NEUCR; DR Q12739, LAC2_PLEOS; P78722, LAC2_PODAN; Q02075, LAC2_THACU; DR Q12718, LAC2_TRAVE; Q99046, LAC2_TRAVI; Q02079, LAC3_THACU; DR Q99049, LAC3_TRAVI; Q02081, LAC4_THACU; Q12719, LAC4_TRAVE; DR Q99055, LAC4_TRAVI; Q12717, LAC5_TRAVE; Q99056, LAC5_TRAVI; // ID 1.10.3.3 DE L-ascorbate oxidase. AN Ascorbase. CA 2 L-ascorbate + O(2) = 2 dehydroascorbate + 2 H(2)O. CF Copper. PR PROSITE; PDOC00076; DR Q00624, ASO_BRANA ; P24792, ASO_CUCMA ; P37064, ASO_CUCPM ; DR P14133, ASO_CUCSA ; Q40588, ASO_TOBAC ; // ID 1.10.3.4 DE O-aminophenol oxidase. AN Isophenoxazine synthase. CA 2 2-aminophenol + 3 O(2) = 2 isophenoxazine + 6 H(2)O. CF Flavoprotein; Manganese. CC -!- Isophenoxazine may be formed by a secondary condensation from the CC initial oxidation product. // ID 1.10.3.5 DE 3-hydroxyanthranilate oxidase. AN 3-hydroxyanthranilic acid oxidase. CA 3-hydroxyanthranilate + O(2) = 6-imino-5-oxocyclohexa-1,3- CA dienecarboxylate + H(2)O(2). // ID 1.10.3.6 DE Rifamycin-B-oxidase. CA Rifamycin B + O(2) = rifamycin O + H(2)O(2). CC -!- Also acts on benzene-1,4-diol and, more slowly, on some other CC P-quinols. CC -!- Not identical with EC 1.10.3.1, EC 1.10.3.2, EC 1.10.3.4 or CC EC 1.10.3.5. // ID 1.10.3.7 DE Transferred entry: 1.21.3.4. // ID 1.10.3.8 DE Transferred entry: 1.21.3.5. // ID 1.10.99.1 DE Plastoquinol--plastocyanin reductase. AN Cytochrome b6f complex. CA Plastoquinol-1 + 2 oxidized plastocyanin = plastoquinone + 2 reduced CA plastocyanin. CC -!- A cytochrome f,b6 complex separated from chloroplasts. CC -!- Also acts, more slowly, on plastoquinol-9 and ubiquinols. CC -!- Cytochrome c-552 can act instead of plastocyanin, more slowly. DR P30361, UCRA_TOBAC; Q02585, UCRB_TOBAC; P70758, UCRI_ANASP; DR Q46136, UCRI_CHLLT; P49728, UCRI_CHLRE; Q9F722, UCRI_CHLTE; DR P14698, UCRI_NOSSP; P26291, UCRI_PEA ; P08980, UCRI_SPIOL; DR P26292, UCRI_SYNP2; P26290, UCRI_SYNY3; Q9SBN3, UCRI_VOLCA; // ID 1.11.1.1 DE NADH peroxidase. CA NADH + H(2)O(2) = NAD(+) + 2 H(2)O. CF FAD. CC -!- Ferricyanide, quinones, etc., can replace H(2)O(2). DR P37062, NAPE_ENTFA; // ID 1.11.1.2 DE NADPH peroxidase. CA NADPH + H(2)O(2) = NADP(+) + 2 H(2)O. // ID 1.11.1.3 DE Fatty acid peroxidase. CA Palmitate + 2 H(2)O(2) = pentadecanal + CO(2) + 3 H(2)O. CC -!- Acts on long-chain fatty acids from dodecanoic to octadecanoic acid. // ID 1.11.1.4 DE Transferred entry: 1.13.11.11. // ID 1.11.1.5 DE Cytochrome-c peroxidase. CA 2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O. CF Heme. PR PROSITE; PDOC00394; DR P55929, CCPR_NITEU; P14532, CCPR_PSEAE; P00431, CCPR_YEAST; DR P37197, YHJA_ECOLI; // ID 1.11.1.6 DE Catalase. CA 2 H(2)O(2) = O(2) + 2 H(2)O. CF Heme; Manganese. CC -!- This enzyme can also act as an EC 1.11.1.7 for which several organic CC substances, especially ethanol, can act as a hydrogen donor. CC -!- A manganese protein containing Mn(3+) in the resting state, which CC also belongs here, is often called pseudocatalase. CC -!- Enzymes from some microorganisms, such as Penicillium simplicissimum, CC which exhibit both catalase and peroxidase activity, have sometimes CC been referred to as catalase-peroxidase. DI Acatalasia; MIM:115500. PR PROSITE; PDOC00395; DR Q96528, CAT1_ARATH; Q27487, CAT1_CAEEL; P48350, CAT1_CUCPE; DR P17598, CAT1_GOSHI; P55307, CAT1_HORVU; P30264, CAT1_LYCES; DR P18122, CAT1_MAIZE; O08404, CAT1_MYCFO; Q9C168, CAT1_NEUCR; DR P49315, CAT1_NICPL; P81138, CAT1_PENJA; Q01297, CAT1_RICCO; DR P49284, CAT1_SOLTU; P29756, CAT1_SOYBN; P49319, CAT1_TOBAC; DR Q43206, CAT1_WHEAT; P25819, CAT2_ARATH; O61235, CAT2_CAEEL; DR P48351, CAT2_CUCPE; P30567, CAT2_GOSHI; P55308, CAT2_HORVU; DR Q9XHH3, CAT2_LYCES; P12365, CAT2_MAIZE; Q8X182, CAT2_NEUCR; DR P49316, CAT2_NICPL; P49318, CAT2_RICCO; P55312, CAT2_SOLTU; DR P55313, CAT2_WHEAT; Q42547, CAT3_ARATH; P48352, CAT3_CUCPE; DR P18123, CAT3_MAIZE; Q9C169, CAT3_NEUCR; P49317, CAT3_NICPL; DR O48560, CAT3_SOYBN; O48561, CAT4_SOYBN; O28050, CATA_ARCFU; DR P90682, CATA_ASCSU; P78574, CATA_ASPFU; Q9AXH0, CATA_AVIMR; DR P45737, CATA_BACFR; P14412, CATA_BACST; P26901, CATA_BACSU; DR P48062, CATA_BORPE; P55304, CATA_BOTCI; P00432, CATA_BOVIN; DR Q9PT92, CATA_BRARE; Q59170, CATA_BRUME; Q59296, CATA_CAMJE; DR O13289, CATA_CANAL; Q96VB8, CATA_CANBO; O97492, CATA_CANFA; DR P07820, CATA_CANTR; Q9M5L6, CATA_CAPAN; O31066, CATA_CAUCR; DR Q64405, CATA_CAVPO; Q59337, CATA_DEIRA; Q9ZN99, CATA_DESVM; DR O77229, CATA_DICDI; P17336, CATA_DROME; P13029, CATA_ECOLI; DR P55305, CATA_EMENI; Q8X1P0, CATA_ERYGR; P44390, CATA_HAEIN; DR O59651, CATA_HALMA; O73955, CATA_HALN1; P45739, CATA_HELAN; DR Q9ZKX5, CATA_HELPJ; P77872, CATA_HELPY; P04040, CATA_HUMAN; DR P07145, CATA_IPOBA; P30265, CATA_LACSK; Q9WXB9, CATA_LEGPN; DR Q926X0, CATA_LISIN; Q8Y3P9, CATA_LISMO; P24168, CATA_LISSE; DR O93662, CATA_METBA; P29422, CATA_MICLU; P24270, CATA_MOUSE; DR P46817, CATA_MYCBO; Q04657, CATA_MYCIT; Q59557, CATA_MYCSM; DR Q08129, CATA_MYCTU; Q59602, CATA_NEIGO; Q27710, CATA_ONCVE; DR P29611, CATA_ORYSA; P25890, CATA_PEA ; P11934, CATA_PENJA; DR P32290, CATA_PHAAU; P30263, CATA_PICAN; O62839, CATA_PIG ; DR P42321, CATA_PROMI; O52762, CATA_PSEAE; Q59714, CATA_PSEPU; DR Q9PWF7, CATA_RANRU; P04762, CATA_RAT ; P95631, CATA_RHIME; DR P37743, CATA_RHOCA; Q8Z303, CATA_SALTI; P17750, CATA_SALTY; DR P55306, CATA_SCHPO; P55310, CATA_SECCE; O24339, CATA_SOLAP; DR P55311, CATA_SOLME; Q9Z598, CATA_STRCO; Q9XZD5, CATA_TOXGO; DR O68146, CATA_VIBFI; P15202, CATA_YEAST; Q9X6B0, CATA_YERPE; DR Q9Y7C2, CATB_AJECA; Q92405, CATB_ASPFU; P78619, CATB_EMENI; DR P55309, CATB_ORYSA; Q59635, CATB_PSEAE; P46206, CATB_PSESY; DR Q9RJH9, CATB_STRCO; O87864, CATB_STRRE; P30266, CATE_BACFI; DR P42234, CATE_BACSU; P21179, CATE_ECOLI; P50979, CATE_MYCAV; DR P95539, CATE_PSEPU; Q9X576, CATE_RHIME; P55303, CATR_ASPNG; DR P06115, CATT_YEAST; P94377, CATX_BACSU; // ID 1.11.1.7 DE Peroxidase. AN Myeloperoxidase. AN Lactoperoxidase. CA Donor + H(2)O(2) = oxidized donor + 2 H(2)O. CF Heme. DI Myeloperoxidase deficiency with disseminated candidiasis; MIM:254600. PR PROSITE; PDOC00394; DR O17433, 1CPX_DIRIM; O77834, PDX6_BOVIN; P30041, PDX6_HUMAN; DR O08709, PDX6_MOUSE; O35244, PDX6_RAT ; Q9FX85, PE10_ARATH; DR Q96519, PE11_ARATH; Q96520, PE12_ARATH; O49293, PE13_ARATH; DR Q9SI17, PE14_ARATH; Q9SI16, PE15_ARATH; Q96518, PE16_ARATH; DR Q9SJZ2, PE17_ARATH; Q9SK52, PE18_ARATH; O22959, PE19_ARATH; DR Q9SLH7, PE20_ARATH; Q42580, PE21_ARATH; P24102, PE22_ARATH; DR O80912, PE23_ARATH; Q9ZV04, PE24_ARATH; O80822, PE25_ARATH; DR O22862, PE26_ARATH; Q43735, PE27_ARATH; Q9SS67, PE28_ARATH; DR Q9LSP0, PE29_ARATH; Q9LSY7, PE30_ARATH; Q9LHA7, PE31_ARATH; DR Q9LHB9, PE32_ARATH; P24101, PE33_ARATH; Q9SMU8, PE34_ARATH; DR Q96510, PE35_ARATH; Q9SD46, PE36_ARATH; Q9LDN9, PE37_ARATH; DR Q9LDA4, PE38_ARATH; Q9SUT2, PE39_ARATH; O23474, PE40_ARATH; DR O23609, PE41_ARATH; Q9SB81, PE42_ARATH; Q9SZH2, PE43_ARATH; DR Q93V93, PE44_ARATH; Q96522, PE45_ARATH; O81772, PE46_ARATH; DR Q9SZB9, PE47_ARATH; O81755, PE48_ARATH; O23237, PE49_ARATH; DR Q43731, PE50_ARATH; Q9SZE7, PE51_ARATH; Q9FLC0, PE52_ARATH; DR Q42578, PE53_ARATH; Q9FG34, PE54_ARATH; Q96509, PE55_ARATH; DR Q9LXG3, PE56_ARATH; Q43729, PE57_ARATH; P59120, PE58_ARATH; DR Q39034, PE59_ARATH; Q9FMR0, PE60_ARATH; Q9FLV5, PE61_ARATH; DR Q9FKA4, PE62_ARATH; Q9FL16, PE63_ARATH; Q43872, PE64_ARATH; DR Q9FJR1, PE65_ARATH; Q9LT91, PE66_ARATH; Q9LVL2, PE67_ARATH; DR Q9LVL1, PE68_ARATH; Q96511, PE69_ARATH; Q9FMI7, PE70_ARATH; DR Q43387, PE71_ARATH; Q9FJZ9, PE72_ARATH; Q43873, PE73_ARATH; DR Q02567, PEM1_PHACH; P22195, PER1_ARAHY; Q96506, PER1_ARATH; DR P27337, PER1_HORVU; P15003, PER1_LYCES; P37834, PER1_ORYSA; DR Q05855, PER1_WHEAT; P22196, PER2_ARAHY; P17179, PER2_ARMRU; DR P19135, PER2_CUCSA; Q01548, PER2_HORVU; P15004, PER2_LYCES; DR P37835, PER2_ORYSA; O23044, PER3_ARATH; P17180, PER3_ARMRU; DR Q9LE15, PER4_ARATH; Q9M9Q9, PER5_ARATH; O48677, PER6_ARATH; DR Q9SY33, PER7_ARATH; Q9LNL0, PER8_ARATH; Q96512, PER9_ARATH; DR P00433, PERA_ARMRU; P15232, PERB_ARMRU; P15233, PERC_ARMRU; DR P59121, PERE_ARMRU; P11678, PERE_HUMAN; P49290, PERE_MOUSE; DR P80550, PERE_PIG ; P80025, PERL_BOVIN; P22079, PERL_HUMAN; DR P05164, PERM_HUMAN; P11247, PERM_MOUSE; Q42517, PERN_ARMRU; DR Q01603, PERO_DROME; P80679, PERX_ARMRU; P00434, PERX_BRARA; DR P16147, PERX_LUPPO; Q02200, PERX_NICSY; P12437, PERX_SOLTU; DR P11965, PERX_TOBAC; P15984, PERX_WHEAT; P28313, PER_ARTRA ; DR P28314, PER_COPCI ; // ID 1.11.1.8 DE Iodide peroxidase. AN Iodotyrosine deiodase. AN Iodotyrosine deiodinase. AN Iodinase. AN Thyroid peroxidase. AN Thyroperoxidase. CA Iodide + H(2)O(2) = iodine + 2 H(2)O. CF Heme. DI Defect in thyroid hormonogenesis II; MIM:274500. PR PROSITE; PDOC00394; DR Q8HYB7, PERT_CANFA; P07202, PERT_HUMAN; P35419, PERT_MOUSE; DR P09933, PERT_PIG ; P14650, PERT_RAT ; // ID 1.11.1.9 DE Glutathione peroxidase. CA 2 glutathione + H(2)O(2) = oxidized glutathione + 2 H(2)O. CF Selenium. CC -!- Steroid and lipid hydroperoxides, but not the product of reaction CC of EC 1.13.11.12 on phospholipids, can act as acceptor, but more CC slowly than H(2)O(2) (cf. EC 1.11.1.12). DI Hemolytic anemia due to glutathione peroxidase deficiency; MIM:138320. PR PROSITE; PDOC00396; DR O70325, GHH1_MOUSE; P36970, GHH1_RAT ; Q9CFV1, GPO_LACLA ; DR O32770, GPO_LACLC ; P74250, GPO_SYNY3 ; O08368, GPWA_PSEWI; DR P00435, GSHC_BOVIN; O02621, GSHC_CAEEL; P07203, GSHC_HUMAN; DR P11352, GSHC_MOUSE; P11909, GSHC_RABIT; P04041, GSHC_RAT ; DR Q00277, GSHC_SCHMA; O62327, GSHD_CAEEL; O46607, GSHE_CANFA; DR O75715, GSHE_HUMAN; P28714, GSHE_MACFA; P21765, GSHE_MOUSE; DR O18994, GSHE_PIG ; P30710, GSHE_RAT ; P18283, GSHG_HUMAN; DR Q9JHC0, GSHG_MOUSE; O48646, GSHH_ARATH; Q06652, GSHH_CITSI; DR O49069, GSHH_GOSHI; O23968, GSHH_HELAN; P36969, GSHH_HUMAN; DR O24031, GSHH_LYCES; Q9LEF0, GSHH_MESCR; P30708, GSHH_NICSY; DR P36968, GSHH_PIG ; O23814, GSHH_SPIOL; Q9FXS3, GSHH_TOBAC; DR P36014, GSHH_YEAST; P38143, GSHI_YEAST; O59858, GSHJ_SCHPO; DR P40581, GSHJ_YEAST; P37141, GSHP_BOVIN; P22352, GSHP_HUMAN; DR P46412, GSHP_MOUSE; P23764, GSHP_RAT ; P35665, GSHU_BRUMA; DR Q95003, GSHU_CAEEL; P52033, GSHU_DIRIM; P35666, GSHU_WUCBA; DR O04922, GSHX_ARATH; P12079, GSHX_HUMAN; P81087, GSHX_PINPS; DR P52032, GSHY_ARATH; O24296, GSHY_PEA ; Q64625, GSHY_RAT ; DR Q9LYB4, GSHZ_ARATH; O23970, GSHZ_HELAN; // ID 1.11.1.10 DE Chloride peroxidase. AN Chloroperoxidase. CA 2 RH + 2 chloride + H(2)O(2) = 2 RCl + 2 H(2)O. CF Heme. CC -!- Brings about the chlorination of a range of organic molecules, CC forming stable C-Cl bonds. CC -!- Also acts on bromide and iodide. DR P04963, PRXC_CALFU; P49053, PRXC_CURIN; O31158, PRXC_PSEFL; DR P25026, PRXC_PSEPY; O31168, PRXC_STRAU; P49323, PRXC_STRLI; DR Q55921, PRXC_SYNY3; // ID 1.11.1.11 DE L-ascorbate peroxidase. AN Ascorbic acid peroxidase. CA L-ascorbate + H(2)O(2) = dehydroascorbate + 2 H(2)O. PR PROSITE; PDOC00394; DR Q05431, APX1_ARATH; P48534, APX1_PEA ; P82281, TL29_ARATH; DR Q9THX6, TL29_LYCES; P81833, TL29_SPIOL; // ID 1.11.1.12 DE Phospholipid-hydroperoxide glutathione peroxidase. AN Peroxidation-inhibiting protein. CA 2 glutathione + a lipid hydroperoxide = oxidized glutathione + lipid + CA 2 H(2)O. CF Selenium. CC -!- The products of action of EC 1.13.11.12 on phospholipids can act as CC acceptor. CC -!- Also acts on H(2)O(2), but much more slowly (cf. EC 1.11.1.9). DR Q91XR9, GHH2_MOUSE; Q91XR8, GHH2_RAT ; // ID 1.11.1.13 DE Manganese peroxidase. AN Mn-dependent peroxidase. CA 2 Mn(2+) + 2 H(+) + H(2)O(2) = 2 Mn(3+) + 2 H(2)O. CF Heme. CC -!- Involved in the oxidative degradation of lignin in white rot CC Basidiomycetes. DR P19136, PEM4_PHACH; // ID 1.11.1.14 DE Diarylpropane peroxidase. AN Diarylpropane oxygenase. AN Ligninase I. CA 1,2-bis(3,4-dimethoxyphenyl)propane-1,3-diol + H(2)O(2) = CA veratraldehyde + 1-(3,4-dimethylphenyl)ethane-1,2-diol + 4 H(2)O. CF Heme. CC -!- Brings about the oxidative cleavage of C-C bonds in a number of CC model compounds, and oxidizes benzyl alcohols to aldehydes or CC ketones. CC -!- Involved in the oxidative breakdown of lignin in white rot CC Basidiomycetes. DR P49012, LIG2_PHACH; P21764, LIG3_PHACH; P11542, LIG4_PHACH; DR P11543, LIG5_PHACH; P50622, LIG6_PHACH; P06181, LIG8_PHACH; DR P31837, LIGA_PHACH; P20011, LIGA_TRAVE; P31838, LIGB_PHACH; DR P20012, LIGB_TRAVE; P20013, LIGC_TRAVE; P20010, LIG_PHLRA ; // ID 1.12.1.1 DE Transferred entry: 1.12.7.2. // ID 1.12.1.2 DE Hydrogen dehydrogenase. AN Hydrogenase. AN H(2):NAD(+) oxidoreductase. AN NAD-linked hydrogenase. AN Bidirectional hydrogenase. CA H(2) + NAD(+) = H(+) + NADH. CF Iron-sulfur; Nickel; FMN or FAD. DR P22317, HOXF_ALCEU; P22658, HOXF_RHOOP; P22320, HOXH_ALCEU; DR P22661, HOXH_RHOOP; P22318, HOXU_ALCEU; P22659, HOXU_RHOOP; DR P22319, HOXY_ALCEU; P22660, HOXY_RHOOP; // ID 1.12.1.3 DE Hydrogen dehydrogenase (NADP). AN NADP-linked hydrogenase. AN NADP-reducing hydrogenase. CA H(2) + NADP(+) = H(+) + NADPH. CF Iron-sulfur; Flavoprotein. // ID 1.12.2.1 DE Cytochrome-c3 hydrogenase. AN H(2):ferricytochrome c3 oxidoreductase. AN Cytochrome c3 reductase. AN Cytochrome hydrogenase. CA 2 H(2) + ferricytochrome c3 = 4 H(+) + ferrocytochrome c3. CF Iron-sulfur; Nickel. CC -!- Some of the enzyme contain nickel ([NiFe]-hydrogenases) and, of CC these, some contain selenocysteine ([NiFeSe]-hydrogenases). CC -!- Methylene blue and other acceptors can also be reduced. DR P80509, HC3L_THIFE; P80510, HC3S_THIFE; P18188, PHNL_DESFR; DR P12944, PHNL_DESGI; P21852, PHNL_DESVM; P13061, PHNS_DESDE; DR P18187, PHNS_DESFR; P12943, PHNS_DESGI; P13062, PHNS_DESMU; DR Q06173, PHNS_DESVH; P21853, PHNS_DESVM; // ID 1.12.5.1 DE Hydrogen:quinone oxidoreductase. AN Hydrogen-ubiquinone oxidoreductase. AN Hydrogen:menaquinone oxidoreductase. AN Membrane-bound hydrogenase. AN Quinone-reactive Ni/Fe-hydrogenase. CA H(2) + menaquinone = menaquinol. CF Nickel; Iron-sulfur. CC -!- Also catalyzes the reduction of water-soluble quinones (e.g. 2,3- CC dimethylnaphthoquinone) or viologen dyes (benzyl viologen or CC methyl viologen) by H(2). CC -!- Formerly EC 1.12.99.3. PR PROSITE; PDOC00400; DR P31883, MBHL_WOLSU; P31884, MBHS_WOLSU; // ID 1.12.7.1 DE Transferred entry: 1.12.7.2. // ID 1.12.7.2 DE Ferredoxin hydrogenase. AN H(2) oxidizing hydrogenase. AN H(2) producing hydrogenase [ambiguous]. AN Bidirectional hydrogenase. AN Hydrogen-lyase [ambiguous]. AN Hydrogenlyase. AN Hydrogenase. AN Hydrogenase (ferredoxin). AN Hydrogenase I. AN Hydrogenase II. AN Hydrogenlyase [ambiguous]. AN Uptake hydrogenase [ambiguous]. CA H(2) + oxidized ferredoxin = reduced ferredoxin + 2 H(+). CF Iron-sulfur; Nickel. CC -!- Can use molecular hydrogen for the reduction of a variety of CC substances. CC -!- Formerly EC 1.12.1.1, EC 1.12.7.1, EC 1.18.3.1 and EC 1.18.99.1. PR PROSITE; PDOC00400; DR P29166, PHF1_CLOPA; P07598, PHFL_DESVH; P13629, PHFL_DESVO; DR P07603, PHFS_DESVH; P13628, PHFS_DESVO; // ID 1.12.98.1 DE Coenzyme F420 hydrogenase. AN 8-hydroxy-5-deazaflavin-reducing hydrogenase. AN F420-reducing hydrogenase. AN Coenzyme F420-dependent hydrogenase. CA H(2) + coenzyme F420 = reduced coenzyme F420. CF Iron; FAD; Nickel. CC -!- The enzyme from some sources contains selenocysteine. CC -!- The enzyme also reduces the riboflavin analogue of F420, flavins CC and methylviologen, but to a lesser extent. CC -!- The hydrogen acceptor coenzyme F420 is a deazaflavin derivative. CC -!- Formerly EC 1.12.99.1. DR P80489, FRHA_METBA; Q60338, FRHA_METJA; P19496, FRHA_METTH; DR Q00390, FRHA_METVO; P80490, FRHB_METBA; Q60341, FRHB_METJA; DR P19499, FRHB_METTH; Q00391, FRHB_METVO; P80491, FRHG_METBA; DR Q60340, FRHG_METJA; P19498, FRHG_METTH; Q00393, FRHG_METVO; // ID 1.12.98.2 DE N(5),N(10)-methenyltetrahydromethanopterin hydrogenase. AN H(2)-forming N(5),N(10)-methylenetetrahydromethanopterin AN dehydrogenase. AN Nonmetal hydrogenase. CA H(2) + N(5),N(10)-methenyltetrahydromethanopterin = H(+) + N(5),N(10)- CA methylenetetrahydromethanopterin. CC -!- Does not catalyze the reduction of artificial dyes by H(2). CC -!- Does not by itself catalyze a H(2)/H(+) exchange reaction. CC -!- Does not contain nickel or iron-sulfur clusters. CC -!- Formerly EC 1.12.99.4. // ID 1.12.98.3 DE Methanosarcina-phenazine hydrogenase. AN Methanophenazine hydrogenase. AN Methylviologen-reducing hydrogenase. CA H(2) + 2-(2,3-dihydropentaprenyloxy)phenazine = 2- CA dihydropentaprenyloxyphenazine. CF Nickel; Iron-sulfur. CC -!- The enzyme from some sources contains selenocysteine. // ID 1.12.99.1 DE Transferred entry: 1.12.98.1. // ID 1.12.99.2 DE Deleted entry. // ID 1.12.99.3 DE Transferred entry: 1.12.5.1. // ID 1.12.99.4 DE Transferred entry: 1.12.98.2. // ID 1.12.99.5 DE Deleted entry. // ID 1.12.99.6 DE Hydrogenase (acceptor). AN H(2) producing hydrogenase [ambiguous]. AN Hydrogen-lyase [ambiguous]. AN Hydrogenlyase [ambiguous]. AN Uptake hydrogenase [ambiguous]. CA H(2) + acceptor = 2 H(+) + reduced acceptor. CF Iron-sulfur; Nickel. CC -!- Uses molecular hydrogen for the reduction of a variety of CC substances. DR P31891, MBHL_ALCEU; P33374, MBHL_ALCHY; P18191, MBHL_AZOCH; DR P21949, MBHL_AZOVI; P12636, MBHL_BRAJA; Q46046, MBHL_CITFR; DR P19927, MBHL_ECOLI; O33406, MBHL_OLICA; P18636, MBHL_RHILV; DR P15284, MBHL_RHOCA; P17632, MBHL_RHOGE; P37181, MBHM_ECOLI; DR P31892, MBHS_ALCEU; P33375, MBHS_ALCHY; P18190, MBHS_AZOCH; DR P21950, MBHS_AZOVI; P12635, MBHS_BRAJA; Q46045, MBHS_CITFR; DR P19928, MBHS_ECOLI; O33405, MBHS_OLICA; P18637, MBHS_RHILV; DR P15283, MBHS_RHOCA; P17633, MBHS_RHOGE; Q46847, MBHT_ECOLI; DR P13065, PHSL_DESBA; P13066, PHSL_DESBN; P13063, PHSS_DESBA; DR P13064, PHSS_DESBN; // ID 1.13.11.1 DE Catechol 1,2-dioxygenase. AN Catechase. AN Pyrocatechase. CA Catechol + O(2) = cis,cis-muconate. CF Iron. CC -!- Involved in the metabolism of nitro-aromatic compounds by a strain CC of Pseudomonas putida. PR PROSITE; PDOC00079; DR P07773, CATA_ACICA; P81422, CATA_ACIRA; P95607, CATA_RHOOP; DR P11451, CLCA_PSEPU; O67987, CLCA_RHOOP; O33948, CTA1_ACILW; DR O33950, CTA2_ACILW; P31019, PHEB_PSESP; P27098, TCBC_PSESQ; DR P05403, TFDC_ALCEU; // ID 1.13.11.2 DE Catechol 2,3-dioxygenase. AN Metapyrocatechase. AN Cato2ase. AN 2,3-pyrocatechase. CA Catechol + O(2) = 2-hydroxymuconate semialdehyde. CF Iron. CC -!- The enzyme from Alcaligines sp. strain O-1 has also been shown to CC catalyze the reaction: 3-Sulfocatechol + O(2) + H(2)O = 2- CC hydroxymuconate + bisulfite. It has been referred to as 3- CC sulfocatechol 2,3-dioxygenase. Further work will be necessary to CC show whether or not this is a distinct enzyme. PR PROSITE; PDOC00078; DR Q53034, CATA_RHORH; P17262, DMPB_PSESP; P17295, MPC1_ALCEU; DR P17296, MPC2_ALCEU; P08127, NAHH_PSEPU; P31003, PHEB_BACST; DR P06622, XYE1_PSEPU; Q04285, XYE2_PSEPU; P27887, XYLE_PSEAE; // ID 1.13.11.3 DE Protocatechuate 3,4-dioxygenase. AN Protocatechuate oxygenase. CA 3,4-dihydroxybenzoate + O(2) = 3-carboxy-cis,cis-muconate. CF Iron. PR PROSITE; PDOC00079; DR P20371, PCXA_ACICA; P15109, PCXA_BURCE; P00436, PCXA_PSEPU; DR P20372, PCXB_ACICA; P15110, PCXB_BURCE; P00437, PCXB_PSEPU; // ID 1.13.11.4 DE Gentisate 1,2-dioxygenase. AN Gentisate oxygenase. AN Gentisic acid oxidase. CA 2,5-dihydroxybenzoate + O(2) = maleylpyruvate. CF Iron. // ID 1.13.11.5 DE Homogentisate 1,2-dioxygenase. AN Homogentisicase. AN Homogentisate oxygenase. AN Homogentisic acid oxidase. CA Homogentisate + O(2) = 4-maleylacetoacetate. CF Iron. DI Alkaptonuria; MIM:203500. DR Q9ZRA2, HGD_ARATH ; Q89XH1, HGD_BRAJA ; Q9Y041, HGD_CAEEL ; DR Q9A5B8, HGD_CAUCR ; Q9VKJ0, HGD_DROME ; Q00667, HGD_EMENI ; DR Q93099, HGD_HUMAN ; Q9S4T0, HGD_LEGPN ; O09173, HGD_MOUSE ; DR Q9X4G0, HGD_PSEAE ; Q88E47, HGD_PSEPK ; Q87Z79, HGD_PSESM ; DR Q8XRZ0, HGD_RALSO ; Q983J4, HGD_RHILO ; Q9X4F5, HGD_RHIME ; DR Q9S2B5, HGD_STRCO ; Q8PQ74, HGD_XANAC ; Q8PDA2, HGD_XANCP ; // ID 1.13.11.6 DE 3-hydroxyanthranilate 3,4-dioxygenase. AN 3-hydroxyanthranilate oxygenase. AN 3-hydroxyanthranilic acid dioxygenase. AN 3-hydroxyanthranilic acid oxidase. CA 3-hydroxyanthranilate + O(2) = 2-amino-3-carboxymuconate semialdehyde. CF Iron. CC -!- The product of the reaction spontaneously rearrange to quinolinic CC acid (quin). DR P46952, 3HAO_HUMAN; P46953, 3HAO_RAT ; P47096, 3HAO_YEAST; // ID 1.13.11.7 DE Deleted entry. // ID 1.13.11.8 DE Protocatechuate 4,5-dioxygenase. AN Protocatechuate 4,5-oxygenase. CA Protocatechuate + O(2) = 4-carboxy-2-hydroxymuconate semialdehyde. CF Iron. DR P22635, PCYA_PSEPA; P22636, PCYB_PSEPA; // ID 1.13.11.9 DE 2,5-dihydroxypyridine 5,6-dioxygenase. AN 2,5-dihydroxypyridine oxygenase. AN Pyridine-2,5-diol dioxygenase. CA 2,5-dihydroxypyridine + O(2) = maleamate + formate. CF Iron. // ID 1.13.11.10 DE 7,8-dihydroxykynurenate 8,8A-dioxygenase. AN 7,8-dihydroxykynurenate oxygenase. CA 7,8-dihydroxykynurenate + O(2) = 5-(3-carboxy-3-oxopropenyl)-4,6- CA dihydroxypyridine-2-carboxylate. CF Iron. // ID 1.13.11.11 DE Tryptophan 2,3-dioxygenase. AN Tryptophan pyrrolase. AN Tryptophanase. AN Tryptophan oxygenase. AN Tryptamin 2,3-dioxygenase. AN Tryptophan peroxidase. CA L-tryptophan + O(2) = L-formylkynurenine. CF Heme. CC -!- Broad specificity towards tryptamine and derivatives including D- CC and L-tryptophan, 5-hydroxytryptophan and serotonin. CC -!- Formerly EC 1.11.1.4. DR Q09474, T23O_CAEEL; P48775, T23O_HUMAN; P48776, T23O_MOUSE; DR P21643, T23O_RAT ; P20351, VERM_DROME; // ID 1.13.11.12 DE Lipoxygenase. AN Lipoxidase. AN Carotene oxidase. AN Lipoperoxidase. CA Linoleate + O(2) = (9Z,11E)-(13S)-13-hydroperoxyoctadeca-9,11-dienoate. CF Iron. CC -!- Also oxidizes other methylene-interrupted polyunsaturated fatty CC acids. PR PROSITE; PDOC00077; DR Q06327, LOX1_ARATH; P29114, LOX1_HORVU; P38414, LOX1_LENCU; DR P37831, LOX1_SOLTU; P08170, LOX1_SOYBN; P29250, LOX2_ORYSA; DR P14856, LOX2_PEA ; P09439, LOX2_SOYBN; P09918, LOX3_PEA ; DR P09186, LOX3_SOYBN; P38417, LOX4_SOYBN; P38415, LOXA_LYCES; DR P27480, LOXA_PHAVU; P38416, LOXB_LYCES; P27481, LOXB_PHAVU; DR P38418, LOXC_ARATH; P38419, LOXC_ORYSA; P24095, LOXX_SOYBN; // ID 1.13.11.13 DE Ascorbate 2,3-dioxygenase. CA Ascorbate + O(2) = oxalate + threonate. CF Iron. // ID 1.13.11.14 DE 2,3-dihydroxybenzoate 3,4-dioxygenase. AN O-pyrocatechuate oxygenase. AN 2,3-dihydroxybenzoic oxygenase. CA 2,3-dihydroxybenzoate + O(2) = 3-carboxy-2-hydroxymuconate semialdehyde. // ID 1.13.11.15 DE 3,4-dihydroxyphenylacetate 2,3-dioxygenase. AN Homoprotocatechuate 2,3-dioxygenase. AN HPC dioxygenase. CA 3,4-dihydroxyphenylacetate + O(2) = 2-hydroxy-5-carboxymethylmuconate CA semialdehyde. CF Iron. DR Q05353, HPCB_ECOLI; // ID 1.13.11.16 DE 3-carboxyethylcatechol 2,3-dioxygenase. CA 3-(2-dihydroxyphenyl)propanoate + O(2) = 2-hydroxy-6-oxonona-2,4- CA diene-1,9-dioate. CF Iron. // ID 1.13.11.17 DE Indole 2,3-dioxygenase. AN Indole oxidase. CA Indole + O(2) = 2-formylaminobenzaldehyde. CF Flavoprotein; Copper. CC -!- The enzyme from jasminum is a flavoprotein containing copper, and CC forms anthranilate as the final product. CC -!- One enzyme from Tecoma stans is also a flavoprotein containing CC copper and uses three atoms of oxygen per molecule of indole, CC to form anthranil (3,4-benzisoxazole). CC -!- A second enzyme from Tecoma stans, which is not a flavoprotein, CC uses four atoms of oxygen and forms anthranilate as the final CC product. // ID 1.13.11.18 DE Sulfur dioxygenase. CA Sulfur + O(2) + H(2)O = sulfite. CF Iron. // ID 1.13.11.19 DE Cysteamine dioxygenase. AN Persulfurase. CA Cysteamine + O(2) = hypotaurine. CF Iron. // ID 1.13.11.20 DE Cysteine dioxygenase. CA L-cysteine + O(2) = 3-sulfinoalanine. CF Iron; NAD(P)H. DR Q16878, CYDX_HUMAN; P21816, CYDX_RAT ; // ID 1.13.11.21 DE Transferred entry: 1.14.99.36. // ID 1.13.11.22 DE Caffeate 3,4-dioxygenase. CA 3,4-dihydroxy-trans-cinnamate + O(2) = 3-(2-carboxyethenyl)-cis,cis- CA muconate. // ID 1.13.11.23 DE 2,3-dihydroxyindole 2,3-dioxygenase. CA 2,3-dihydroxyindole + O(2) = anthranilate + CO(2). // ID 1.13.11.24 DE Quercetin 2,3-dioxygenase. CA Quercetin + O(2) = 2-protocatechuoylphloroglucinolcarboxylate + CO. CF Copper. CC -!- Quercetin is a flavonol. // ID 1.13.11.25 DE 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione DE 4,5-dioxygenase. AN Steroid 4,5-dioxygenase. AN 3-alkylcatechol 2,3-dioxygenase. CA 3,4-dihydroxy-9,10-secoandrosta-1,3,5(10)-triene-9,17-dione + O(2) = CA 3-hydroxy-5,9,17-trioxo-4,5:9,10-disecoandrosta-1(10),2-dien-4-oate. CF Iron. CC -!- Also acts on 3-isopropylcatechol and 3-tert-butyl-5-methylcatechol. // ID 1.13.11.26 DE Peptide-tryptophan 2,3-dioxygenase. AN Pyrrolooxygenase. AN Tryptophan pyrrolooxygenase. CA Peptide tryptophan + O(2) = peptide formylkynurenine. CC -!- Also acts on tryptophan. // ID 1.13.11.27 DE 4-hydroxyphenylpyruvate dioxygenase. AN p-Hydroxyphenylpyruvate dioxygenase. AN 4-hydroxyphenylpyruvate hydroxylase. AN p-hydroxyphenylpyruvate oxidase. CA 4-hydroxyphenylpyruvate + O(2) = homogentisate + CO(2). CF Iron. DI Tyrosinemia, type III; MIM:276710. DR P93836, HPPD_ARATH; Q22633, HPPD_CAEEL; Q00415, HPPD_COCPO; DR O23920, HPPD_DAUCA; O48604, HPPD_HORVU; P32754, HPPD_HUMAN; DR P49429, HPPD_MOUSE; O42764, HPPD_MYCGR; Q02110, HPPD_PIG ; DR P80064, HPPD_PSESP; P32755, HPPD_RAT ; Q9ARF9, HPPD_SOLSC; DR Q53586, HPPD_STRAW; Q27203, HPPD_TETTH; Q53407, LLY_LEGPN ; // ID 1.13.11.28 DE 2,3-dihydroxybenzoate 2,3-dioxygenase. CA 2,3-dihydroxybenzoate + O(2) = 2-carboxy-cis,cis-muconate. CC -!- Also acts, more slowly, with 2,3-dihydroxy-4-toluate and 2,3- CC dihydroxy-4-cumate. // ID 1.13.11.29 DE Stizolobate synthase. CA 3,4-dihydroxy-L-phenylalanine + O(2) = 4-(L-alanin-3-yl)-2-hydroxy- CA cis,cis-muconate 6-semialdehyde. CF Zinc. CC -!- The intermediate product undergoes ring closure and oxidation, with CC NAD(P)(+) as acceptor, to stizolobic acid. // ID 1.13.11.30 DE Stizolobinate synthase. CA 3,4-dihydroxy-L-phenylalanine + O(2) = 5-(L-alanin-3-yl)-2-hydroxy- CA cis,cis-muconate 6-semialdehyde. CF Zinc. CC -!- The intermediate product undergoes ring closure and oxidation, with CC NAD(P)(+) as acceptor, to stizolobinic acid. // ID 1.13.11.31 DE Arachidonate 12-lipoxygenase. AN 12-lipoxygenase. CA Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa- CA 5,8,10,14-tetraenoate. CF Iron. CC -!- The product is rapidly converted to the corresponding 12S-hydroxy CC compound. PR PROSITE; PDOC00077; DR Q02759, LOX2_RAT ; P55249, LOXE_MOUSE; P39654, LOXL_MOUSE; DR P27479, LOXP_BOVIN; P18054, LOXP_HUMAN; P39655, LOXP_MOUSE; DR P16469, LOXP_PIG ; O19043, LOXP_RABIT; // ID 1.13.11.32 DE 2-nitropropane dioxygenase. AN Nitroalkane oxidase. AN 2-NPD. CA 2 2-nitropropane + O(2) = 2 acetone + 2 nitrite. CF Iron; FMN. CC -!- Some other nitroalkanes, including nitroethane, 1-nitropropane and CC 3-nitro-2-pentanol, can act as donors, more slowly. DR Q01284, 2NPD_NEUCR; Q12723, 2NPD_WILMR; // ID 1.13.11.33 DE Arachidonate 15-lipoxygenase. AN 15-lipoxygenase. AN Arachidonate omega-6 lipoxygenase. CA Arachidonate + O(2) = (5Z,8Z,11,Z,13E)-(15S)-15-hydroperoxyicosa- CA 5,8,11,13-tetraenoate. CF Iron. CC -!- The product is rapidly converted to the corresponding 15S-hydroxy CC compound. PR PROSITE; PDOC00077; DR P16050, LOX1_HUMAN; P12530, LOX1_RABIT; O15296, LX1B_HUMAN; DR O35936, LX1B_MOUSE; // ID 1.13.11.34 DE Arachidonate 5-lipoxygenase. AN 5-lipoxygenase. AN Leukotriene-A4 synthase. CA Arachidonate + O(2) = (6E,8Z,11Z,14Z)-(5S)-5-hydroperoxycosa- CA 6,8,11,14-tetraenoate. CF Iron. CC -!- The product is rapidly converted to leukotriene A4. PR PROSITE; PDOC00077; DR P09917, LOX5_HUMAN; P51399, LOX5_MESAU; P48999, LOX5_MOUSE; DR P12527, LOX5_RAT ; // ID 1.13.11.35 DE Pyrogallol 1,2-oxygenase. CA 1,2,3-trihydroxybenzene + O(2) = (Z)-5-oxohex-2-enedioate. // ID 1.13.11.36 DE Chloridazon-catechol dioxygenase. CA 5-amino-4-chloro-2-(2,3-dihydroxyphenyl)-3(2H)-pyridazinone + O(2) = CA 5-amino-4-chloro-2-(2-hydroxymuconoyl)-3(2H)-pyridazinone. CF Iron. CC -!- Involved in the breakdown of the herbicide chloridazon. CC -!- Not identical with EC 1.13.11.1, EC 1.13.11.2 or EC 1.13.11.5. // ID 1.13.11.37 DE Hydroxyquinol 1,2-dioxygenase. CA Benzene-1,2,4-triol + O(2) = 3-hydroxy-cis,cis-muconate. CF Iron. CC -!- The product isomerizes to 2-maleylacetate (cis-hex-2-enedioate). CC -!- Highly specific; catechol and pyrogallol are acted on at less than CC 1% of the rate at which benzene-1,2,4-triol is oxidized. // ID 1.13.11.38 DE 1-hydroxy-2-naphthoate 1,2-dioxygenase. AN 1-hydroxy-2-naphthoate-degrading enzyme. AN 1-hydroxy-2-naphthoic acid dioxygenase. CA 1-hydroxy-2-naphthoate + O(2) = (3E)-4-(2-carboxyphenyl)-2-oxobut-3- CA enoate. CF Iron. CC -!- Involved, with EC 4.1.2.34, in the metabolism of phenanthrene in CC bacteria. // ID 1.13.11.39 DE Biphenyl-2,3-diol 1,2-dioxygenase. AN 2,3-dihydroxybiphenyl dioxygenase. CA Biphenyl-2,3-diol + O(2) = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + CA H(2)O. CC -!- Also acts on 3-isopropylcatechol, forming 7-methyl-2-hydroxy-6-oxo- CC octa-2,4-dienoate. CC -!- Not identical with EC 1.13.11.2. PR PROSITE; PDOC00078; DR P47231, BHC1_RHOGO; P47232, BHC2_RHOGO; P47233, BHC3_RHOGO; DR P47228, BPHC_BURCE; P11122, BPHC_PSEPA; P08695, BPHC_PSEPS; DR P17297, BPHC_PSES1; // ID 1.13.11.40 DE Arachidonate 8-lipoxygenase. AN 8-lipoxygenase. CA Arachidonate + O(2) = (5Z,9E,11Z,14Z)-(8R)-8-hydroperoxyicosa-5,9,11,14- CA tetraenoate. CF Iron. CC -!- An enzyme from the coral Pseudolexaura porosa. PR PROSITE; PDOC00077; DR O16025, AOSL_PLEHO; // ID 1.13.11.41 DE 2,4'-dihydroxyacetophenone dioxygenase. CA 2,4'-dihydroxyacetophenone + O(2) = 4-hydroxybenzoate + formate. // ID 1.13.11.42 DE Indoleamine-pyrrole 2,3-dioxygenase. AN Indoleamine 2,3-dioxygenase. CA L-tryptophan + O(2) = N-formylkynurenine. CF Heme. CC -!- Acts on many substituted and unsubstituted indoleamines, including CC melatonin. CC -!- Involved in the degradation of melatonin. PR PROSITE; PDOC00684; DR P14902, I23O_HUMAN; P28776, I23O_MOUSE; // ID 1.13.11.43 DE Lignostilbene alpha beta-dioxygenase. CA 1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene + O(2) = 2 vanillin. CF Iron. CC -!- The enzyme catalyzes oxidative cleavage of the interphenyl double CC bond in the synthetic substrate and lignin-derived stilbenes. CC -!- It is responsible for the degradation of a diarylpropane-type CC structure in lignin. // ID 1.13.11.44 DE Linoleate diol synthase. AN Linoleate (8R)-dioxygenase. AN Linoleate 8-dioxygenase. CA Linoleate + O(2) = (9Z,12Z)-(7S,8S)-dihydroxyoctadeca-9,12-dienoate. CF Heme. CC -!- Oleate and linolenate are also substrates, whereas stearate, elaidate, CC gamma-linolenate, arachidonate and eicosapentaenate are not. CC -!- This enzyme differs from EC 1.13.11.12 because it catalyzes the CC formation of a hydroperoxide without affecting the double bonds of CC the substrate. DR Q9UUS2, LIDS_GAEGR; // ID 1.13.11.45 DE Linoleate 11-lipoxygenase. AN Linoleate dioxygenase. AN Manganese lipoxygenase. CA Linoleate + O(2) = (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate. CC -!- The product (9Z,12Z)-(11S)-11-hydroperoxyoctadeca-9,12-dienoate, CC is converted, more slowly, into (9Z,11E)-(13R)-13- CC hydroperoxyoctadeca-9,11-dienoate. CC -!- The enzyme from the fungus Gaeumannomyces graminis requires Mn(2+). CC -!- It also acts on alpha-linolenate, whereas gamma-linolenate is a CC poor substrate. CC -!- Oleate and arachidonate are not substrates. // ID 1.13.11.46 DE 4-hydroxymandelate synthase. AN 4-hydroxyphenylpyruvate dioxygenase II. CA 4-hydroxyphenylpyruvate + O(2) = 4-hydroxymandelate + CO(2). CF Iron(2+). CC -!- Involved in the biosynthesis of the vancomycin group of CC glycopeptide antibiotics. // ID 1.13.11.47 DE 3-hydroxy-4-oxoquinoline 2,4-dioxygenase. AN (1H)-3-hydroxy-4-oxoquinoline 2,4-dioxygenase. AN 3-hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase. AN 3-hydroxy-4(1H)-one, 2,4-dioxygenase. AN Quinoline-3,4-diol 2,4-dioxygenase. CA 3-hydroxy-1H-quinolin-4-one + O(2) = N-formylanthranilate + CO. CC -!- Does not contain a metal centre or organic cofactor. CC -!- Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with CC concomitant release of carbon monoxide. CC -!- The enzyme from Pseudomonas putida is highly specific for this CC substrate. CC -!- Formerly EC 1.13.99.5. // ID 1.13.11.48 DE 3-hydroxy-2-methyl-quinolin-4-one 2,4-dioxygenase. AN (1H)-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase. CA 3-hydroxy-2-methyl-1H-quinolin-4-one + O(2) = N-acetylanthranilate + CA CO. CC -!- Does not contain a metal centre or organic cofactor. CC -!- Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with CC concomitant release of carbon monoxide. CC -!- The enzyme from Arthrobacter sp. can also act on 3-hydroxy-4- CC oxoquinoline, forming N-formylanthranilate and CO (cf. CC EC 1.13.11.47), but more slowly. // ID 1.13.11.49 DE Chlorite O(2)-lyase. AN [Chlorite dismutase]. CA Chloride + O(2) = chlorite. CF Iron; Protoheme IX. CC -!- Reaction occurs in the reverse direction in chlorate- and CC perchlorate-reducing bacteria. CC -!- There is no activity when chlorite is replaced by hydrogen CC peroxide, perchlorate, chlorate or nitrite. CC -!- The term 'chlorite dismutase' is misleading as the reaction CC does not involve dismutation/disproportionation. // ID 1.13.12.1 DE Arginine 2-monooxygenase. AN Arginine decarboxylase. AN Arginine oxygenase (decarboxylating). AN Arginine decarboxy-oxidase. CA L-arginine + O(2) = 4-guanidobutanamide + CO(2) + H(2)O. CF Flavoprotein. CC -!- Also acts on canavanine and homoarginine. // ID 1.13.12.2 DE Lysine 2-monooxygenase. AN Lysine oxygenase. CA L-lysine + O(2) = 5-aminopentanamide + CO(2) + H(2)O. CF FAD. CC -!- Also acts on other diamino acids. // ID 1.13.12.3 DE Tryptophan 2-monooxygenase. CA L-tryptophan + O(2) = indole-3-acetamide + CO(2) + H(2)O. DR Q09109, TR2M_AGRRH; P04029, TR2M_AGRT4; Q04564, TR2M_AGRVI; DR Q47861, TR2M_PANAY; P06617, TR2M_PSESS; P25017, TR2N_AGRVI; // ID 1.13.12.4 DE Lactate 2-monooxygenase. AN Lactate oxidative decarboxylase. AN Lactate oxidase. AN Lactate oxygenase. CA (S)-lactate + O(2) = acetate + CO(2) + H(2)O. CF FMN. CC -!- Formerly EC 1.1.3.2. PR PROSITE; PDOC00482; DR P21795, LA2M_MYCSM; // ID 1.13.12.5 DE Renilla-luciferin 2-monooxygenase. AN Renilla-type luciferase. AN Luciferase. AN Aequorin. CA Renilla luciferin + O(2) = oxidized Renilla luciferin + CO(2) + light. CC -!- 8-benzyl-2-(4-hydroxybenzyl)-6-(4-hydroxyphenyl)imidazo-[1,2- CC A]pyrazin-3(7H)-one is similar to, and as active as, luciferin CC from the coelenterate Renilla. CC -!- The native luciferin has the benzyl group replaced by an CC unidentified group of approximately 200 Da. CC -!- The enzyme may be assayed by measurement of light emission. DR P27652, LUCI_RENRE; // ID 1.13.12.6 DE Cypridina-luciferin 2-monooxygenase. AN Cypridina-type luciferase. AN Luciferase. CA Cypridina luciferin + O(2) = oxidized Cypridina luciferin + CO(2) + CA light. CC -!- Cypridina luciferin is [3-[3,7-dihydro-6-(1H-indol-3-yl)-2-[(S)-1- CC methyl-6-propyl]-3-oxoimidazo-[1,2-a]pyrazin-8-yl]propyl]guanidine. CC -!- The enzyme may be assayed by measurement of light emission. DR P17554, LUCI_VARHI; // ID 1.13.12.7 DE Photinus-luciferin 4-monooxygenase (ATP-hydrolyzing). AN Firefly luciferase. AN Luciferase. AN Photinus pyralis luciferase. CA Photinus luciferin + O(2) + ATP = oxidized Photinus luciferin + CO(2) + CA H(2)O + AMP + diphosphate + light. CC -!- Photinus luciferin is (S)-4,5-dihydro-2-(6-hydroxy-2- CC benzothiazoloyl)-4-thiazolecarboxylic acid. CC -!- The first step in the reaction is the formation of an acid anhydride CC between the carboxylic group and AMP, with the release of CC diphosphate. CC -!- The enzyme may be assayed by measurement of light emission. PR PROSITE; PDOC00427; DR P13129, LUCI_LUCCR; Q01158, LUCI_LUCLA; P08659, LUCI_PHOPY; // ID 1.13.12.8 DE Watasemia-luciferin 2-monooxygenase. AN Watasemia-type luciferase. AN Luciferase. CA Watasemia luciferin + O(2) = oxidized Watasemia luciferin + CO(2) + CA light. CC -!- Watasemia luciferin is 8-(phenylmethyl)-6-(4-sulfooxyphenyl)-2- CC [(4-sulfooxyphenyl)methyl]imidazo[1,2A]pyrazin-3(7H)-one. CC -!- The enzyme may be assayed by measurement of light emission. // ID 1.13.12.9 DE Phenylalanine 2-monooxygenase. AN L-phenylalanine oxidase (deaminating and decarboxylating). CA L-phenylalanine + O(2) = 2-phenylacetamide + CO(2) + H(2)O. CC -!- Also catalyzes a reaction similar to that of EC 1.4.3.2, forming CC 3-phenylpyruvate, NH(3) and H(2)O(2), but more slowly. // ID 1.13.12.10 DE Deleted entry. // ID 1.13.12.11 DE Methylphenyltetrahydropyridine N-monooxygenase. CA 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine + O(2) = 1-methyl-4-phenyl- CA 1,2,3,6-tetrahydropyridine N-oxide + methanol. CF FAD. // ID 1.13.12.12 DE Apo-beta-carotenoid-14',13'-dioxygenase. CA 8'-apo-beta-carotenol + O(2) = 14'-apo-beta-carotenal + H(2)O. CC -!- A thiol-dependent enzyme. CC -!- Unlike EC 1.14.99.36, it is not active towards beta-carotene. CC -!- Presumably 2-methyl-6-oxohepta-2,4-dienal is also formed in this CC reaction. // ID 1.13.99.1 DE Inositol oxygenase. AN Meso-inositol oxygenase. AN Myo-inositol oxygenase. AN MOO. CA Myo-inositol + O(2) = D-glucuronate + H(2)O. CF Iron. DR Q9UGB7, MIOX_HUMAN; Q9QXN5, MIOX_MOUSE; Q8WN98, MIOX_PIG ; DR Q9QXN4, MIOX_RAT ; // ID 1.13.99.2 DE Transferred entry: 1.14.12.10. // ID 1.13.99.3 DE Tryptophan 2'-dioxygenase. AN Indole-3-alkane alpha-hydroxylase. AN Tryptophan side-chain alpha,beta-oxidase. AN Tryptophan side-chain oxidase. AN TSO. CA L-tryptophan + O(2) = 3-indolylglycolaldehyde + CO(2) + NH(3). CF Heme. CC -!- Acts on a number of indolyl-3-alkane derivatives, oxidizing the CC 3-side-chain in the 2'-position. Best substrates are L-tryptophan CC and 5-hydroxy-L-tryptophan. // ID 1.13.99.4 DE Transferred entry: 1.14.12.9. // ID 1.13.99.5 DE Transferred entry: 1.13.11.47. // ID 1.14.11.1 DE Gamma-butyrobetaine,2-oxoglutarate dioxygenase. AN Gamma-butyrobetaine hydroxylase. AN Gamma-BBH. CA 4-trimethylammoniobutanoate + 2-oxoglutarate + O(2) = CA 3-hydroxy-4-trimethylammoniobutanoate + succinate + CO(2). CF Iron; Ascorbate. DR Q19000, BODG_CAEEL; O75936, BODG_HUMAN; Q924Y0, BODG_MOUSE; DR P80193, BODG_PSESK; Q9QZU7, BODG_RAT ; Q98KK0, BODG_RHILO; // ID 1.14.11.2 DE Procollagen-proline,2-oxoglutarate-4-dioxygenase. AN Protocollagen hydroxylase. AN Proline hydroxylase. AN Proline,2-oxoglutarate 4-dioxygenase. AN Prolyl 4-hydroxylase. AN Prolyl hydroxylase. CA Procollagen L-proline + 2-oxoglutarate + O(2) = procollagen trans-4- CA hydroxy-L-proline + succinate + CO(2). CF Iron; Ascorbate. PR PROSITE; PDOC00172; DR Q10576, P4H1_CAEEL; P13674, P4H1_HUMAN; Q60715, P4H1_MOUSE; DR P54001, P4H1_RAT ; Q20065, P4H2_CAEEL; O15460, P4H2_HUMAN; DR Q60716, P4H2_MOUSE; P16924, P4HA_CHICK; // ID 1.14.11.3 DE Pyrimidine-deoxynucleoside 2'-dioxygenase. AN Pyrimidine-deoxynucleoside,2-oxoglutarate 2'-dioxygenase. AN Thymidine 2'-hydroxylase. AN Thymidine 2-oxoglutarate dioxygenase. AN Pyrimidine deoxyribonucleoside 2'-hydroxylase. AN Deoxyuridine 2'-hydroxylase. AN Deoxyuridine 2'-dioxygenase. AN Thymidine 2'-dioxygenase. AN Thymidine dioxygenase. CA 2'-deoxyuridine + 2-oxoglutarate + O(2) = uridine + succinate + CO(2). CF Iron(2+); Ascorbate. CC -!- Also acts on thymidine (cf. EC 1.14.11.10). // ID 1.14.11.4 DE Procollagen-lysine 5-dioxygenase. AN Procollagen-lysine,2-oxoglutarate 5-dioxygenase. AN Lysine hydroxylase. AN Lysyl hydroxylase. AN Lysine,2-oxoglutarate 5-dioxygenase. CA Procollagen L-lysine + 2-oxoglutarate + O(2) = procollagen CA 5-hydroxy-L-lysine + succinate + CO(2). CF Iron; Ascorbate. DI Ehlers-Danlos syndrome, type VI; MIM:225400. PR PROSITE; PDOC01028; DR O77588, PLO1_BOVIN; P24802, PLO1_CHICK; Q02809, PLO1_HUMAN; DR Q9R0E2, PLO1_MOUSE; Q63321, PLO1_RAT ; O00469, PLO2_HUMAN; DR Q9R0B9, PLO2_MOUSE; O60568, PLO3_HUMAN; Q9R0E1, PLO3_MOUSE; DR Q20679, PLOD_CAEEL; // ID 1.14.11.5 DE Deleted entry. // ID 1.14.11.6 DE Thymine dioxygenase. AN Thymine,2-oxoglutarate dioxygenase. AN Thymine 7-hydroxylase. CA Thymine + 2-oxoglutarate + O(2) = 5-hydroxymethyluracil + succinate + CA CO(2). CF Iron; Ascorbate. CC -!- Also acts on 5-hydroxymethyluracil to oxidize its -CH(2)-OH group CC first to -CHO and then to -COOH. // ID 1.14.11.7 DE Procollagen-proline 3-dioxygenase. AN Procollagen-proline,2-oxoglutarate 3-dioxygenase. AN Proline,2-oxoglutarate 3-dioxygenase. AN Prolyl 3-hydroxylase. CA Procollagen L-proline + 2-oxoglutarate + O(2) = procollagen CA trans-3-hydroxy-L-proline + succinate + CO(2). CF Iron; Ascorbate. // ID 1.14.11.8 DE Trimethyllysine dioxygenase. AN Trimethyllysine,2-oxoglutarate dioxygenase. AN Epsilon-trimethyllysine 2-oxoglutarate dioxygenase. AN TML-alpha-ketoglutarate dioxygenase. AN TML hydroxylase. AN TML dioxygenase. AN TMLD. CA N(6),N(6),N(6)-trimethyl-L-lysine + 2-oxoglutarate + O(2) = 3-hydroxy- CA N(6),N(6),N(6)-trimethyl-L-lysine + succinate + CO(2). CF Iron; Ascorbate. DR Q9NVH6, TMLH_HUMAN; Q91ZE0, TMLH_MOUSE; Q96UB1, TMLH_NEUCR; DR Q91ZW6, TMLH_RAT ; // ID 1.14.11.9 DE Naringenin 3-dioxygenase. AN Naringenin,2-oxoglutarate 3-dioxygenase. AN Flavonone 3-hydroxylase. AN Flavanone synthase I. CA Naringenin + 2-oxoglutarate + O(2) = dihydrokaempferol + succinate + CA CO(2). CF Iron; Ascorbate. DR Q9S818, FL3H_ARATH; Q05963, FL3H_CALCH; Q05964, FL3H_DIACA; DR P28038, FL3H_HORVU; Q06942, FL3H_MALDO; Q05965, FL3H_MATIN; DR Q07353, FL3H_PETHY; P41090, FL3H_VITVI; // ID 1.14.11.10 DE Pyrimidine-deoxynucleoside 1'-dioxygenase. AN Pyrimidine-deoxynucleoside,2-oxoglutarate 1'-dioxygenase. AN Deoxyuridine-uridine 1'-dioxygenase. CA 2'-deoxyuridine + 2-oxoglutarate + O(2) = uracil + 2-deoxyribonolactone CA + succinate + CO(2). CF Iron(2+); Ascorbate. CC -!- Cf. EC 1.14.11.3. // ID 1.14.11.11 DE Hyoscyamine (6S)-dioxygenase. AN Hyoscyamine (6S)-hydroxylase. AN Hyoscyamine 6-beta-hydroxylase. CA L-hyoscyamine + 2-oxoglutarate + O(2) = (6S)-hydroxyhyoscyamine + CA succinate + CO(2). CF Iron; Ascorbate. DR P24397, HY6H_HYONI; // ID 1.14.11.12 DE Gibberellin-44 dioxygenase. AN Gibberellin A44 oxidase. CA Gibberellin 44 + 2-oxoglutarate + O(2) = gibberellin 19 + succinate + CA CO(2). CF Iron. // ID 1.14.11.13 DE Gibberellin 2-beta-dioxygenase. AN Gibberellin 2-beta-hydroxylase. CA Gibberellin 1 + 2-oxoglutarate + O(2) = 2-beta-hydroxygibberellin 1 + CA succinate + CO(2). CC -!- Also acts on a number of other gibberellins. // ID 1.14.11.14 DE 6-beta-hydroxyhyoscyamine epoxidase. AN Hydroxyhyoscyamine dioxygenase. CA (6S)-hydroxyhyoscyamine + 2-oxoglutarate + O(2) = scopolamine + CA succinate + CO(2). CF Iron; Ascorbate. // ID 1.14.11.15 DE Gibberellin 3-beta-dioxygenase. AN Gibberellin 3-beta-hydroxylase. CA Gibberellin 20 + 2-oxoglutarate + O(2) = gibberellin 1 + succinate + CA CO(2). CF Iron; Ascorbate. // ID 1.14.11.16 DE Peptide-aspartate beta-dioxygenase. AN Aspartate beta-hydroxylase. AN Aspartyl/asparaginyl beta-hydroxylase. CA Peptide L-aspartate + 2-oxoglutarate + O(2) = peptide 3-hydroxy-L- CA aspartate + succinate + CO(2). CF Iron. CC -!- Some vitamin K-dependent coagulation factors, as well as synthetic CC peptides based on the structure of the first epidermal growth factor CC domain of human coagulation factor IX or X, can act as acceptors. DR Q28056, ASPH_BOVIN; Q12797, ASPH_HUMAN; P59723, HIFN_BRARE; DR Q9NWT6, HIFN_HUMAN; Q8BLR9, HIFN_MOUSE; // ID 1.14.11.17 DE Taurine dioxygenase. AN 2-aminoethanesulfonate dioxygenase. AN Alpha-ketoglutarate-dependent taurine dioxygenase. CA Taurine + 2-oxoglutarate + O(2) = sulfite + aminoacetaldehyde + CA succinate + CO(2). CF Iron; Ascorbate. CC -!- The enzyme from E.coli also acts on pentanesulfonate, CC 3-(N-morpholino)propanesulfonate and 2-(1,3-dioxoisoindolin-2-yl) CC ethanesulfonate, but at lower rates. DR P37610, TAUD_ECOLI; // ID 1.14.11.18 DE Phytanoyl-CoA dioxygenase. AN Phytanoyl-CoA hydroxylase. AN Phytanoyl-CoA 2 oxoglutarate dioxygenase. AN Phytanoyl-CoA alpha-hydroxylase. AN Phytanoyl-CoA 2-hydroxylase. CA Phytanoyl-CoA + 2-oxoglutarate + O(2) = 2-hydroxyphytanoyl-CoA + CA succinate + CO(2). CF Iron(2+); Ascorbate. CC -!- Part of the peroxisomal phytanic acid alpha-oxidation pathway. DI Refsum disease; MIM:266500. DR O18778, PAHX_BOVIN; O62515, PAHX_CAEEL; O14832, PAHX_HUMAN; DR O35386, PAHX_MOUSE; P57093, PAHX_RAT ; // ID 1.14.11.19 DE Leucocyanidin oxygenase. AN Anthocyanidin synthase. AN Leucoanthocyanidin dioxygenase. CA Leucocyanidin + 2-oxoglutarate + O(2) = cis- and trans- CA dihydroquercetins + succinate + CO(2). CF Iron(2+); Ascorbate. CC -!- The enzyme is involved in the pathway by which many flowering CC plants make anthocyanin (glycosylated anthocyandin) flower CC pigments. CC -!- The intermediates are transformed into cis- and trans- CC dihydroquercetin, which the enzyme can also oxidize to quercetin. CC -!- Acidification of the products gives anthocyanidin, which, CC however, may not be a natural precursor of the anthocyanins. DR Q96323, LDOX_ARATH; P41213, LDOX_MAIZE; P51091, LDOX_MALDO; DR P51092, LDOX_PETHY; P51093, LDOX_VITVI; // ID 1.14.11.20 DE Desacetoxyvindoline 4-hydroxylase. AN Desacetoxyvindoline-4-hydroxylase. CA Desacetoxyvindoline + 2-oxoglutarate + O(2) = desacetylvindoline + CA succinate + CO(2). CF Iron(2+); Ascorbate. CC -!- Also acts on 16-methoxy-2,3-dihydro-3-hydroxytabersonine and to a CC lesser extent on 16-methoxy-2,3-dihydrotabersonine. DR O04847, DV4H_CATRO; // ID 1.14.12.1 DE Anthranilate 1,2-dioxygenase (deaminating, decarboxylating). AN Anthranilate hydroxylase. AN Anthranilic hydroxylase. AN Anthranilic acid hydroxylase. CA Anthranilate + NAD(P)H + O(2) + 2 H(2)O = catechol + CO(2) + NAD(P)(+) + CA NH(3). CF Iron. // ID 1.14.12.2 DE Transferred entry: 1.14.13.35. // ID 1.14.12.3 DE Benzene 1,2-dioxygenase. AN Benzene hydroxylase. CA Benzene + NADH + O(2) = cis-1,2-dihydrobenzene-1,2-diol + NAD(+). CF FAD; Iron-sulfur. CC -!- A system, containing a reductase which is an iron-sulfur CC flavoprotein, an iron-sulfur oxygenase and ferredoxin. PR PROSITE; PDOC00493; DR Q07944, BED1_PSEPU; Q07945, BED2_PSEPU; P08084, BNZA_PSEPU; DR P08085, BNZB_PSEPU; // ID 1.14.12.4 DE 3-hydroxy-2-methylpyridinecarboxylate dioxygenase. AN Methylhydroxypyridinecarboxylate oxidase. AN Methylhydroxypyridine carboxylate dioxygenase. CA 3-hydroxy-2-methylpyridine-5-carboxylate + NAD(P)H + O(2) = CA 2-(acetamidomethylene)succinate + NAD(P)(+). CF FAD. // ID 1.14.12.5 DE 5-pyridoxate dioxygenase. AN 5-pyridoxate oxidase. CA 3-hydroxy-4-hydroxymethyl-2-methylpyridine-5-carboxylate + NADPH + O(2) = CA 2-(acetamidomethylene)-3-(hydroxymethyl)succinate + NADP(+). CF Flavoprotein. // ID 1.14.12.6 DE Transferred entry: 1.14.13.66. // ID 1.14.12.7 DE Phthalate 4,5-dioxygenase. AN Phthalate dioxygenase. AN PDO. CA Phthalate + NADH + O(2) = cis-4,5-dihydroxycyclohexa-1(6),2-diene- CA 1,2-dicarboxylate + NAD(+) + H(2)O. CF Iron. CC -!- A system, containing a reductase which is an iron-sulfur CC flavoprotein, an iron-sulfur oxygenase, and no independent CC ferredoxin. DR Q05182, PHT2_PSEPU; Q05183, PHT3_PSEPU; // ID 1.14.12.8 DE 4-sulfobenzoate 3,4-dioxygenase. CA 4-sulfobenzoate + NADH + O(2) = 3,4-dihydroxybenzoate + sulfite + CA NAD(+). CF Iron. CC -!- A system, containing a reductase which is an iron-sulfur CC flavoprotein (FMN), an iron-sulfur oxygenase, and no independent CC Ferredoxin. // ID 1.14.12.9 DE 4-chlorophenylacetate 3,4-dioxygenase. CA 4-chlorophenyl acetate + NADH + O(2) + H(2)O = 3,4-dihydroxyphenyl CA acetate + chloride + NAD(+). CF Iron. CC -!- A system, containing a reductase and an iron-sulfur oxygenase, CC and no independent ferredoxin. CC -!- Also acts on 4-bromophenyl acetate. CC -!- Formerly EC 1.13.99.4. // ID 1.14.12.10 DE Benzoate 1,2-dioxygenase. AN Benzoate hydroxylase. AN Benzoic hydroxylase. CA Benzoate + NADH + O(2) = catechol + CO(2) + NAD(+). CF Iron. CC -!- A system, containing a reductase which is an iron-sulfur CC flavoprotein (FAD), and an iron-sulfur oxygenase. CC -!- Formerly EC 1.13.99.2. PR PROSITE; PDOC00493; DR P07769, BENA_ACICA; P07770, BENB_ACICA; // ID 1.14.12.11 DE Toluene dioxygenase. AN Toluene 1,2-dioxygenase. CA Toluene + NADH + O(2) = (1S,2R)-3-methylcyclohexa-3,5-diene-1,2-diol + CA NAD(+). CC -!- A system, containing a reductase which is an iron-sulfur CC flavoprotein (FAD), an iron-sulfur oxygenase, and a ferredoxin. CC -!- Some other aromatic compounds, including ethylbenzene, 4-xylene CC and some halogenated toluenes, are converted into the corresponding CC cis-dihydrodiols. // ID 1.14.12.12 DE Naphthalene 1,2-dioxygenase. CA Naphthalene + NADH + O(2) = (1R,2S)-1,2-dihydronaphthalene-1,2-diol + CA NAD(+). CF Iron. CC -!- A system, containing a reductase which is an iron-sulfur CC flavoprotein (FAD), an iron-sulfur oxygenase, and ferredoxin. PR PROSITE; PDOC00493; DR Q51494, NDOB_PSEAE; O07824, NDOB_PSEFL; P23094, NDOB_PSEPU; DR Q51495, NDOC_PSEAE; O07825, NDOC_PSEFL; P23095, NDOC_PSEPU; // ID 1.14.12.13 DE 2-chlorobenzoate 1,2-dioxygenase. CA 2-chlorobenzoate + NADH + O(2) = catechol + chloride + NAD(+) + CO(2). CF Iron. DR Q51601, CBDA_BURCE; Q51602, CBDB_BURCE; // ID 1.14.12.14 DE 2-aminobenzenesulfonate 2,3-dioxygenase. AN 2-aminosulfobenzene 2,3-dioxygenase. CA 2-aminobenzenesulfonate + NADH + H(+) + O(2) = 3-sulfocatechol + NH(3) + CA NAD(+). // ID 1.14.12.15 DE Terephthalate 1,2-dioxygenase. AN Benzene-1,4-dicarboxylate 1,2-dioxygenase. AN 1,4-dicarboxybenzoate 1,2-dioxygenase. CA Terephthalate + NADH + H(+) + O(2) = (1R,6S)-dihydroxycyclohexa-2,4- CA diene-1,4-dicarboxylate + NAD(+). CC -!- In C.testoteroni, contains a Rieske [2Fe-2S] centre. // ID 1.14.12.16 DE 2-hydroxyquinoline 5,6-dioxygenase. AN 2-oxo-1,2-dihydroquinoline 5,6-dioxygenase. AN Quinolin-2-ol 5,6-dioxygenase. AN Quinolin-2(1H)-one 5,6-dioxygenase. CA Quinolin-2-ol + NADH + O(2) = 2,5,6-trihydroxy-5,6-dihydroquinoline + CA NAD(+). CC -!- 3-methylquinolin-2-ol, quinolin-8-ol and quinolin-2,8-diol are also CC substrates. CC -!- Quinolin-2-ols exist largely as their quinolin-2(1H)-one tautomers. // ID 1.14.12.17 DE Nitric oxide dioxygenase. AN NOD. CA 2 NO + 2 O(2) + NAD(P)H = 2 NO(3-)+ NAD(P)(+). CF FAD; Heme. CC -!- It has been proposed that FAD functions as the electron carrier CC from NADPH to the ferric heme prosthetic group. DR P24232, HMPA_ECOLI; P26353, HMPA_SALTY; // ID 1.14.12.18 DE Biphenyl 2,3-dioxygenase. AN Biphenyl dioxygenase. CA Biphenyl + NADH + O(2) = (2R,3S)-3-phenylcyclohexa-3,5-diene-1,2-diol + CA NAD(+). CF Iron. CC -!- The enzyme from Pseudomonas sp. strain LB400 is part of a CC multicomponent system composed of an NADH:ferredoxin CC oxidoreductase (FAD cofactor), a [2Fe-2S] Rieske-type ferredoxin, CC and a terminal oxygenase that contains a [2Fe-2S] Rieske-type CC iron-sulfur cluster and a catalytic mononuclear nonheme iron CC center. CC -!- Chlorine-substituted biphenyls can also act as substrates. CC -!- Similar to the three-component enzyme systems EC 1.14.12.3 and CC EC 1.14.12.11. DR Q52438, BPA1_PSES1; Q52439, BPA2_PSES1; P37333, BPHA_BURCE; DR Q46372, BPHA_COMTE; Q52028, BPHA_PSEPS; P37334, BPHE_BURCE; DR Q46373, BPHE_COMTE; // ID 1.14.13.1 DE Salicylate 1-monooxygenase. AN Salicylate hydroxylase. AN Salicylic hydroxylase. CA Salicylate + NADH + O(2) = catechol + NAD(+) + H(2)O + CO(2). CF FAD. DR P23262, NHG1_PSEPU; Q53552, NHG2_PSEPU; // ID 1.14.13.2 DE 4-hydroxybenzoate 3-monooxygenase. AN p-hydroxybenzoate hydroxylase. AN Para-hydroxybenzoate hydroxylase. AN p-hydroxybenzoic acid hydroxylase. CA 4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O. CF FAD. CC -!- Most enzymes from Pseudomonas are highly specific for NAD(P)H (cf. CC EC 1.14.13.33). DR Q03298, PHHY_ACICA; P20586, PHHY_PSEAE; P00438, PHHY_PSEFL; // ID 1.14.13.3 DE 4-hydroxyphenylacetate 3-monooxygenase. AN p-hydroxyphenylacetate 3-hydroxylase. AN 4-Hydroxyphenylacetic acid-3-hydroxylase. AN 4 HPA 3-hydroxylase. CA 4-hydroxyphenylacetate + NADH + O(2) = 3,4-dihydroxyphenylacetate + CA NAD(+) + H(2)O. CF FAD. // ID 1.14.13.4 DE Melilotate 3-monooxygenase. AN 2-hydroxyphenylpropionate hydroxylase. AN Melilotate hydroxylase. AN Melilotic hydroxylase. CA 3-(2-hydroxyphenyl)propanoate + NADH + O(2) = CA 3-(2,3-dihydroxyphenyl)propanoate + NAD(+) + H(2)O. CF FAD. // ID 1.14.13.5 DE Imidazoleacetate 4-monooxygenase. AN Imidazoleacetate hydroxylase. AN Imidazoleacetic monooxygenase. CA 4-imidazoleacetate + NADH + O(2) = 5-hydroxy-4-imidazoleacetate + NAD(+) CA + H(2)O. CF FAD. // ID 1.14.13.6 DE Orcinol 2-monooxygenase. AN Orcinol hydroxylase. CA Orcinol + NADH + O(2) = 2,3,5-trihydroxytoluene + NAD(+) + H(2)O. CF FAD. // ID 1.14.13.7 DE Phenol 2-monooxygenase. AN Phenol hydroxylase. AN Phenol o-hydroxylase. CA Phenol + NADPH + O(2) = catechol + NADP(+) + H(2)O. CF FAD. CC -!- Also active with resorcinol and O-cresol. DR P19729, DMPK_PSESP; P19730, DMPL_PSESP; P19731, DMPM_PSESP; DR P19732, DMPN_PSESP; P19733, DMPO_PSESP; P19734, DMPP_PSESP; DR P15245, PH2M_TRICU; P31020, PHEA_PSESP; Q01551, TBUD_BURPI; // ID 1.14.13.8 DE Dimethylaniline monooxygenase (N-oxide forming). AN Dimethylaniline oxidase. AN Dimethylaniline N-oxidase. AN DMA oxidase. AN FAD-containing monooxygenase. AN FMO. CA N,N-dimethylaniline + NADPH + O(2) = N,N-dimethylaniline N-oxide + CA NADP(+) + H(2)O. CF FAD. CC -!- Acts on various dialkylarylamines. DI Trimethylaminuria; MIM:602079. DR Q95LA2, FMO1_CANFA; P49328, FMO1_CAVPO; Q01740, FMO1_HUMAN; DR P50285, FMO1_MOUSE; P16549, FMO1_PIG ; P17636, FMO1_RABIT; DR P36365, FMO1_RAT ; P36366, FMO2_CAVPO; Q99518, FMO2_HUMAN; DR Q28505, FMO2_MACMU; P17635, FMO2_RABIT; Q95LA1, FMO3_CANFA; DR P31513, FMO3_HUMAN; Q8SPQ7, FMO3_MACMU; P97501, FMO3_MOUSE; DR P32417, FMO3_RABIT; P31512, FMO4_HUMAN; P36367, FMO4_RABIT; DR P49109, FMO5_CAVPO; P49326, FMO5_HUMAN; P97872, FMO5_MOUSE; DR Q04799, FMO5_RABIT; O60774, FMO6_HUMAN; // ID 1.14.13.9 DE Kynurenine 3-monooxygenase. AN Kynurenine 3-hydroxylase. CA L-kynurenine + NADPH + O(2) = 3-hydroxy-L-kynurenine + NADP(+) + H(2)O. CF FAD. // ID 1.14.13.10 DE 2,6-dihydroxypyridine 3-monooxygenase. CA 2,6-dihydroxypyridine + NADH + O(2) = 2,3,6-trihydroxypyridine + NAD(+) + CA H(2)O. CF Flavoprotein. // ID 1.14.13.11 DE Trans-cinnamate 4-monooxygenase. AN Cinnamic acid 4-hydroxylase. AN Cinnamic acid 4-monooxygenase. AN Cinnamate 4-hydroxylase. AN Cinnamate 4-monooxygenase. AN CA4H. CA Trans-cinnamate + NADPH + O(2) = 4-hydroxycinnamate + NADP(+) + H(2)O. CF Heme-thiolate. CC -!- Also acts on NADH, more slowly. PR PROSITE; PDOC00081; DR P92994, TCMO_ARATH; P48522, TCMO_CATRO; O81928, TCMO_CICAR; DR Q96423, TCMO_GLYEC; Q04468, TCMO_HELTU; P37114, TCMO_MEDSA; DR Q43067, TCMO_PEA ; Q43033, TCMO_PETCR; P37115, TCMO_PHAAU; DR Q43054, TCMO_POPKI; O24312, TCMO_POPTM; Q9AR74, TCMO_RUTGR; DR Q42797, TCMO_SOYBN; Q43240, TCMO_ZINEL; // ID 1.14.13.12 DE Benzoate 4-monooxygenase. AN Benzoate 4-hydroxylase. AN Benzoate-para-hydroxylase. AN Benzoic acid 4-hydroxylase. AN p-hydroxybenzoate hydroxylase. CA Benzoate + NADPH + O(2) = 4-hydroxybenzoate + NADP(+) + H(2)O. CF Iron; Tetrahydropteridine. PR PROSITE; PDOC00081; DR P17549, CP53_ASPNG; // ID 1.14.13.13 DE Calcidiol 1-monooxygenase. AN 25-hydroxycholecalciferol-1-hydroxylase. AN 25-hydroxycholecalciferol 1-monooxygenase. CA Calcidiol + NADPH + O(2) = calcitriol + NADP(+) + H(2)O. DI Vitamin-D-dependent rickets type I; MIM:264700. // ID 1.14.13.14 DE Trans-cinnamate 2-monooxygenase. AN Cinnamic acid 2-hydroxylase. AN Cinnamic 2-hydroxylase. CA Trans-cinnamate + NADPH + O(2) = 2-hydroxycinnamate + NADP(+) + H(2)O. // ID 1.14.13.15 DE Cholestanetriol 26-monooxygenase. AN Cholestanetriol 26-hydroxylase. AN 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 26-hydroxylase. CA 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol + NADPH + O(2) = CA 5-beta-cholestane-3-alpha,7-alpha,12-alpha,26-tetraol + NADP(+) + H(2)O. // ID 1.14.13.16 DE Cyclopentanone monooxygenase. CA Cyclopentanone + NADPH + O(2) = 5-valerolactone + NADP(+) + H(2)O. // ID 1.14.13.17 DE Cholesterol 7-alpha-monooxygenase. AN Cholesterol 7-alpha-hydroxylase. CA Cholesterol + NADPH + O(2) = 7-alpha-hydroxycholesterol + NADP(+) + CA H(2)O. CF Heme-thiolate. PR PROSITE; PDOC00081; DR P46634, CP7A_CRIGR; P22680, CP7A_HUMAN; Q64505, CP7A_MOUSE; DR O46491, CP7A_PIG ; P51542, CP7A_RABIT; P18125, CP7A_RAT ; // ID 1.14.13.18 DE 4-hydroxyphenylacetate 1-monooxygenase. AN 4-hydroxyphenylacetate 1-hydroxylase. AN 4-hydroxyphenylacetic 1-hydroxylase. AN 4-HPA 1-hydroxylase. CA 4-hydroxyphenylacetate + NAD(P)H + O(2) = homogentisate + NAD(P)(+) + CA H(2)O. CF FAD. CC -!- Also acts on 4-hydroxyhydratropate forming 2-methylhomogentisate and CC on 4-hydroxyphenoxyacetate forming hydroquinone and glycolate. // ID 1.14.13.19 DE Taxifolin 8-monooxygenase. CA Taxifolin + NAD(P)H + O(2) = 2,3-dihydrogossypetin + NAD(P)(+) + H(2)O. CF Flavoprotein. CC -!- Converts a flavonol into a flavonone. CC -!- Also acts on fustin, but not on catechin, quercetin or CC mollisacacidin. // ID 1.14.13.20 DE 2,4-dichlorophenol 6-monooxygenase. AN 2,4-dichlorophenol hydroxylase. CA 2,4-dichlorophenol + NADPH + O(2) = 3,5-dichlorocatechol + NADP(+) + CA H(2)O. CF FAD. CC -!- Also acts, more slowly, on 4-chlorophenol and 4-chloro-2- CC methylphenol. CC -!- NADH can act instead of NADPH, but more slowly. DR P27138, TFDB_ALCEU; // ID 1.14.13.21 DE Flavonoid 3'-monooxygenase. AN Flavonoid 3'-hydroxylase. CA A flavonoid + NADPH + O(2) = 3'-hydroxyflavonoid + NADP(+) + H(2)O. CC -!- Acts on a number of flavonoids, including naringenin and CC dihydrokaempferol. CC -!- Does not act on 4-coumarate or 4-coumaroyl-CoA. DR Q9SD85, F3PH_ARATH; Q9SBQ9, F3PH_PETHY; // ID 1.14.13.22 DE Cyclohexanone monooxygenase. AN Cyclohexanone oxygenase. CA Cyclohexanone + NADPH + O(2) = 6-hexanolide + NADP(+) + H(2)O. CF FAD. CC -!- Acts on a number of other cyclic ketones. DR P12015, CYMO_ACISP; // ID 1.14.13.23 DE 3-hydroxybenzoate 4-monooxygenase. AN 3-hydroxybenzoate 4-hydroxylase. CA 3-hydroxybenzoate + NADPH + O(2) = 3,4-dihydroxybenzoate + NADP(+) + CA H(2)O. CF FAD. CC -!- Also acts on a number of analogs of 3-hydroxybenzoate substituted in CC the 2, 4, 5 and 6 positions. CC -!- Formerly EC 1.14.99.13. // ID 1.14.13.24 DE 3-hydroxybenzoate 6-monooxygenase. AN 3-hydroxybenzoate 6-hydroxylase. AN 3-hydroxybenzoic acid-6-hydroxylase. CA 3-hydroxybenzoate + NADH + O(2) = 2,5-dihydroxybenzoate + NAD(+) + H(2)O. CF FAD. CC -!- Also acts on a number of analogs of 3-hydroxybenzoate substituted in CC the 2, 4, 5 and 6 positions. CC -!- NADPH can act instead of NADH, more slowly. // ID 1.14.13.25 DE Methane monooxygenase. AN Methane hydroxylase. CA Methane + NAD(P)H + O(2) = methanol + NAD(P)(+) + H(2)O. CC -!- Broad specificity; many alkanes can be hydroxylated, and alkenes are CC converted into the corresponding epoxides; CO is oxidized to CO(2), CC ammonia is oxidized to hydroxylamine, and some aromatic compounds CC and cyclic alkanes can also be hydroxylated, more slowly. DR P22869, MEMA_METCA; P27353, MEMA_METTR; P18798, MEMB_METCA; DR P27354, MEMB_METTR; P11987, MEMG_METCA; P27355, MEMG_METTR; DR P22868, MMOC_METCA; Q53563, MMOC_METTR; // ID 1.14.13.26 DE Phosphatidylcholine 12-monooxygenase. AN Ricinoleic acid synthase. AN Oleate delta(12)-hydroxylase. CA 1-acyl-2-oleoyl-sn-glycero-3-phosphocholine + NADH + O(2) = CA 1-acyl-2-[(S)-12-hydroxyoleoyl]-sn-glycero-3-phosphocholine + NAD(+) + CA H(2)O. // ID 1.14.13.27 DE 4-aminobenzoate 1-monooxygenase. AN 4-aminobenzoate hydroxylase. AN 4-aminobenzoate dehydrogenase. CA 4-aminobenzoate + NAD(P)H + O(2) = 4-hydroxyaniline + NAD(P)(+) + CA H(2)O + CO(2). CF FAD. CC -!- Acts on anthranilate and 4-aminosalicylate but not on salicylate CC (cf. EC 1.14.13.1). // ID 1.14.13.28 DE 3,9-dihydroxypterocarpan 6A-monooxygenase. AN 3,9-dihydroxypterocarpan 6A-hydroxylase. CA (6AR,11AR)-3,9-dihydroxypterocarpan + NADPH + O(2) = (6AS,11AS)- CA 3,6A,9-trihydroxypterocarpan + NADP(+) + H(2)O. CF Heme-thiolate. CC -!- The product of the reaction is the biosynthetic precursor of the CC phytoalexin glyceollin in soybean. PR PROSITE; PDOC00081; // ID 1.14.13.29 DE 4-nitrophenol 2-monooxygenase. AN 4-nitrophenol-2-hydroxylase. AN 4-nitrophenol hydroxylase. CA 4-nitrophenol + NADH + O(2) = 4-nitrocatechol + NAD(+) + H(2)O. CF FAD. // ID 1.14.13.30 DE Leukotriene-B4 20-monooxygenase. AN Leukotriene-B4 omega-hydroxylase. AN Leukotriene-B4 20-hydroxylase. AN LTB4 omega-hydroxylase. AN LTB4 20-hydroxylase. CA (6Z,8E,10E,14Z)-(5S,12R)-5,12-dihydroxyicosa-6,8,10,14-tetraenoate + CA NADPH + O(2) = (6Z,8E,10E,14Z)-(5S,12R)-5,12,20-trihydroxyicosa- CA 6,8,10,14-tetraenoate + NADP(+) + H(2)O. CF Heme-thiolate. CC -!- Not identical with EC 1.14.13.34. PR PROSITE; PDOC00081; DR P78329, CPF2_HUMAN; Q08477, CPF3_HUMAN; // ID 1.14.13.31 DE 2-nitrophenol 2-monooxygenase. AN Nitrophenol oxygenase. CA 2-nitrophenol + NADPH + O(2) = catechol + nitrite + NADP(+) + H(2)O. CC -!- Involved in the metabolism of nitro-aromatic compounds by a strain CC of Pseudomonas putida. // ID 1.14.13.32 DE Albendazole monooxygenase. AN Albendazole sulfoxidase. CA Albendazole + NADPH + O(2) = albendazole S-oxide + NADP(+) + H(2)O. CF FAD. // ID 1.14.13.33 DE 4-hydroxybenzoate 3-monooxygenase (NAD(P)H). AN 4-hydroxybenzoate 3-hydroxylase. CA 4-hydroxybenzoate + NAD(P)H + O(2) = 3,4-dihydroxybenzoate + NAD(P)(+) + CA H(2)O. CF FAD. CC -!- The enzyme from Corynebacterium cyclohexanicum is highly specific CC for 4-hydroxybenzoate, but uses NADH and NADPH at approximately CC equal rates (cf. EC 1.14.13.2). It is less specific for NADPH than CC EC 1.14.13.2. // ID 1.14.13.34 DE Leukotriene-E4 20-monooxygenase. AN Leukotriene-E4 omega-hydroxylase. CA (7E,9E,11Z,14Z)-(5S,6R)-6-(cystein-S-yl)-5-hydroxyicosa-7,9,11,14- CA tetraenoate + NADPH + O(2) = 20-hydroxy-leukotriene E4 + NADP(+) + CA H(2)O. CC -!- Also acts on N-acetyl-leukotriene E4, more slowly. CC -!- Not identical with EC 1.14.13.30. // ID 1.14.13.35 DE Anthranilate 3-monooxygenase (deaminating). AN Anthranilate hydroxylase. AN Anthranilate 2,3-hydroxylase (deaminating). CA Anthranilate + NADPH + O(2) = 2,3-dihydroxybenzoate + NADP(+) + NH(3). CC -!- The enzyme from Aspergillus niger is an iron protein; that from the CC yeast Trichosporon cutaneum is a flavoprotein (FAD). CC -!- Formerly EC 1.14.12.2. // ID 1.14.13.36 DE 5-O-(4-coumaroyl)-D-quinate 3'-monooxygenase. AN 5-O-(4-coumaroyl)-D-quinate/shikimate 3'-hydroxylase. CA Trans-5-O-(4-coumaroyl)-D-quinate + NADPH + O(2) = trans-5-O-caffeoyl-D- CA quinate + NADP(+) + H(2)O. CC -!- Also acts on trans-5-O-(4-coumaroyl)shikimate. // ID 1.14.13.37 DE Methyltetrahydroprotoberberine 14-monooxygenase. AN Methyltetrahydroprotoberberine 14-hydroxylase. AN (S)-cis-N-methyltetrahydroprotoberberine-14-hydroxylase. CA (S)-N-methylcanadine + NADPH + O(2) = allocryptopine + NADP(+) + H(2)O. CF Heme-thiolate. PR PROSITE; PDOC00081; // ID 1.14.13.38 DE Anhydrotetracycline monooxygenase. AN Anhydrotetracycline oxygenase. AN ATC oxygenase. CA Anhydrotetracycline + NADPH + O(2) = 12-dehydrotetracycline + NADP(+) + CA H(2)O. CC -!- Involved in the biosynthesis of tetracyclines in Streptomyces sp. // ID 1.14.13.39 DE Nitric-oxide synthase. AN Nitric-oxide synthetase. AN NO synthase. AN Endothelium-derived relaxation factor-forming enzyme. AN Endothelium-derived relaxing factor synthase. AN NADPH-diaphorase. CA L-arginine + N NADPH + M O(2) = citrulline + nitric oxide + N NADP(+). CC -!- The enzyme in brain, but not that induced in lung or liver by CC endotoxin, requires calcium. The stoichiometry is not clear, but CC may involve a two-electron and a one-electron oxidation step. DR P29475, NOS1_HUMAN; Q9Z0J4, NOS1_MOUSE; O19132, NOS1_RABIT; DR P29476, NOS1_RAT ; Q29498, NOS1_SHEEP; Q27995, NOS2_BOVIN; DR O62699, NOS2_CANFA; Q28314, NOS2_CAPHI; Q92037, NOS2_CARAU; DR O54705, NOS2_CAVPO; Q90703, NOS2_CHICK; O46660, NOS2_MACMU; DR P29477, NOS2_MOUSE; Q92091, NOS2_ONCMY; P79290, NOS2_PIG ; DR O19114, NOS2_RABIT; Q06518, NOS2_RAT ; P29473, NOS3_BOVIN; DR P97270, NOS3_CAVPO; P29474, NOS3_HUMAN; P70313, NOS3_MOUSE; DR Q28969, NOS3_PIG ; Q62600, NOS3_RAT ; P79209, NOS3_SHEEP; DR O61608, NOS_ANOST ; Q27571, NOS_DROME ; O61309, NOS_LYMST ; DR Q26240, NOS_RHOPR ; Q9I9M2, NOS_SQUAC ; P35228, NS2A_HUMAN; DR P81272, NS2B_HUMAN; Q14961, NS2C_HUMAN; O60591, NS2D_HUMAN; // ID 1.14.13.40 DE Anthraniloyl-CoA monooxygenase. AN 2-aminobenzoyl-CoA monooxygenase/reductase. CA 2-aminobenzoyl-CoA + 2 NAD(P)H + O(2) = 2-amino-5-oxocyclohex-1- CA enecarboxyl-CoA + H(2)O + 2 NAD(P)(+). CF FAD. CC -!- The non-aromatic product is unstable and releases CO(2) and NH(3), CC forming 1,4-cyclohexanedione. // ID 1.14.13.41 DE Tyrosine N-monooxygenase. AN Tyrosine N-hydroxylase. CA Tyrosine + O(2) + NADPH = N-hydroxytyrosine + NADP(+) + H(2)O. CA N-hydroxytyrosine + O(2) + NADPH = N,N-dihydroxytyrosine + NADP(+) + CA H(2)O. CA N,N-dihydroxytyrosine = (Z)-[p-hydroxyphenylacetaldehyde oxime] + CA CO(2) + H(2)O. CF Heme-thiolate. CC -!- The third reaction is spontaneous. CC -!- The enzyme is involved in the biosynthesis of the cyanogenic CC glucoside dhurrin in sorghum. CC -!- In the reaction some 2-(4-hydroxyphenyl)-1-nitroethane is formed CC as a side product. PR PROSITE; PDOC00081; DR Q43135, C791_SORBI; // ID 1.14.13.42 DE Hydroxyphenylacetonitrile 2-monooxygenase. AN 4-hydroxyphenylacetonitrile hydroxylase. CA 4-hydroxyphenylacetonitrile + NADPH + O(2) = 4-hydroxymandelonitrile + CA NADP(+) + H(2)O. CF Heme-thiolate. PR PROSITE; PDOC00081; // ID 1.14.13.43 DE Questin monooxygenase. AN Questin oxygenase. CA Questin + NADPH + O(2) = sulochrin + NADP(+) + H(2)O. CC -!- The enzyme cleaves the anthraquinone ring of questin to form a CC benzophenone. CC -!- Involved in the biosynthesis of the seco-anthraquinone (+)-geodin. // ID 1.14.13.44 DE 2-hydroxybiphenyl 3-monooxygenase. CA 2-hydroxybiphenyl + NADH + O(2) = 2,3-dihydroxybiphenyl + NAD(+) + H(2)O. CC -!- Also converts 2,2'-dihydroxybiphenyl into 2,2',3-trihydroxy-biphenyl. // ID 1.14.13.45 DE CMP-N-acetylneuraminate monooxygenase. AN CMP-N-acetylneuraminate hydroxylase. AN CMP-Neu5Ac hydroxylase. CA CMP-N-acetylneuraminate + NAD(P)H + O(2) = CMP-N-glycoloylneuraminate + CA NAD(P)(+) + H(2)O. // ID 1.14.13.46 DE (-)-menthol monooxygenase. CA (-)-menthol + NADPH + O(2) = para-menthane-3,8-diol + NADP(+) + H(2)O. // ID 1.14.13.47 DE (-)-limonene 3-monooxygenase. AN (-)-limonene 3-hydroxylase. CA (-)-limonene + NADPH + O(2) = (-)-trans-isopiperitenol + NADP(+) + H(2)O. CF Heme-thiolate. CC -!- High specificity , but NADH can act instead of NADPH, more slowly. PR PROSITE; PDOC00081; // ID 1.14.13.48 DE (-)-limonene 6-monooxygenase. AN (-)-limonene 6-hydroxylase. CA (-)-limonene + NADPH + O(2) = (-)-trans-carveol + NADP(+) + H(2)O. CF Heme-thiolate. CC -!- High specificity , but NADH can act instead of NADPH, more slowly. PR PROSITE; PDOC00081; // ID 1.14.13.49 DE (-)-limonene 7-monooxygenase. AN (-)-limonene 7-hydroxylase. CA (-)-limonene + NADPH + O(2) = (-)-perillyl alcohol + NADP(+) + H(2)O. CF Heme-thiolate. CC -!- High specificity , but NADH can act instead of NADPH, more slowly. PR PROSITE; PDOC00081; // ID 1.14.13.50 DE Pentachlorophenol monooxygenase. AN Pentachlorophenol hydroxylase. AN Pentachlorophenol dehalogenase. AN PCP hydroxylase. CA Pentachlorophenol + NADPH + O(2) = tetrachlorohydroquinone + NADP(+) + CA chloride. CC -!- Some tetrachlorophenols and trichlorophenols can act as substrates. DR P42535, PCPB_SPHCR; // ID 1.14.13.51 DE 6-oxocineole dehydrogenase. CA 6-oxocineole + NADPH + O(2) = 1,6,6-trimethyl-2,7-dioxabicyclo- CA [3.2.2]nonan-3-one + NADP(+) + H(2)O. CC -!- The product undergoes non-enzymic cleavage and subsequent ring CC closure to form the lactone 4,5-dihydro-5,5-dimethyl-4-(3- CC oxobutyl)furan-2(3h)-one. // ID 1.14.13.52 DE Isoflavone 3'-hydroxylase. CA Formononetin + NADPH + O(2) = calycosin + NADP(+) + H(2)O. CF Heme-thiolate. CC -!- Also acts on biochanin A and other isoflavones with a 4'-methoxy CC group. CC -!- Involved in the biosynthesis of the pterocarpin phytoalexins CC medicarpin and maackiain. PR PROSITE; PDOC00081; // ID 1.14.13.53 DE Isoflavone 2'-hydroxylase. CA Formononetin + NADPH + O(2) = 2'-hydroxyformononetin + NADP(+) + CA H(2)O. CF Heme-thiolate. CC -!- Acts on isoflavones with a 4'-methoxy group. CC -!- Involved in the biosynthesis of the pterocarpin phytoalexins CC medicarpin and maackiain. PR PROSITE; PDOC00081; // ID 1.14.13.54 DE Ketosteroid monooxygenase. AN Steroid-ketone monooxygenase. CA Ketosteroid + NADPH + O(2) = steroid ester/lactone + NADP(+) + H(2)O. CF FAD. CC -!- Catalyzes three types of monooxygenase (Baeyer-Villiger oxidation) CC reaction. CC -!- (1) The oxidative esterification of a number of derivatives of CC pregn-4-ene-3,20-dione (progesterone) to produce the corresponding CC 17-alpha-hydroxysteroid 17-acetate ester, such as testosterone CC acetate: progesterone + NADPH + O(2) = testosterone acetate + NADP(+) CC + H(2)O. CC -!- (2) The oxidative lactonization of a number of derivatives of CC androst-4-ene-3,17-dione (androstenedione) to produce the 13,17- CC secoandrosteno-17,13-alpha-lactone, such as 3-oxo-13,17-secoandrost- CC 4-eno-17,13-alpha-lactone (testololactone): androstenedione + NADPH + CC O(2) = testololactone + NADP(+) + H(2)O. CC -!- (3) The oxidative cleavage of the 17beta-side-chain of 17-alpha- CC hydroxypregn-4-ene-3,20-dione (17-alpha-hydroxyprogesterone) to CC produce androst-4-ene-3,17-dione (androstenedione) and acetate: CC 17-alpha-hydroxyprogesterone + NADPH + O(2) = androstenedione + CC acetate + NADP(+) + H(2)O. CC -!- Reaction 1 is also catalyzed by EC 1.14.99.4 and reactions 2 and 3 CC correspond to that catalyzed by EC 1.14.99.12. The possibility that CC a single enzyme is responsible for the reactions ascribed to CC EC 1.14.99.4 and EC 1.14.99.12 in other tissues cannot be excluded. // ID 1.14.13.55 DE Protopine 6-monooxygenase. AN Protopine 6-hydroxylase. CA Protopine + NADPH + O(2) = 6-hydroxyprotopine + NADP(+) + H(2)O. CF Heme-thiolate. CC -!- Involved in benzophenanthridine alkaloid synthesis in higher plants. PR PROSITE; PDOC00081; // ID 1.14.13.56 DE Dihydrosanguinarine 10-monooxygenase. AN Dihydrosanguinarine 10-hydroxylase. CA Dihydrosanguinarine + NADPH + O(2) = 10-hydroxydihydrosanguinarine + CA NADP(+) + H(2)O. CF Heme-thiolate. CC -!- Involved in benzophenanthridine alkaloid synthesis in higher plants. PR PROSITE; PDOC00081; // ID 1.14.13.57 DE Dihydrochelirubine 12-monooxygenase. AN Dihydrochelirubine 12-hydroxylase. CA Dihydrochelirubine + NADPH + O(2) = 12-hydroxydihydrochelirubine + CA NADP(+) + H(2)O. CF Heme-thiolate. PR PROSITE; PDOC00081; // ID 1.14.13.58 DE Benzoyl-CoA 3-monooxygenase. AN Benzoyl-CoA 3-hydroxylase. CA Benzoyl-CoA + NADPH + O(2) = 3-hydroxybenzoyl-CoA + NADP(+) + H(2)O. CF FAD or FMN. CC -!- Benzoate is not a substrate. // ID 1.14.13.59 DE L-lysine 6-monooxygenase (NADPH). AN Lysine N(6)-hydroxylase. CA L-lysine + NADPH + O(2) = N(6)-hydroxy-L-lysine + NADP(+) + H(2)O. CF FAD. CC -!- The enzyme from strain EN 222 of E.coli is highly specific for L- CC lysine. L-ornithine and L-homolysine are, for example not substrates. DR P11295, IUCD_ECOLI; // ID 1.14.13.60 DE 27-hydroxycholesterol 7-alpha-monooxygenase. AN 27-hydroxycholesterol 7-alpha-hydroxylase. CA 27-hydroxycholesterol + NADPH + O(2) = 7-alpha,27-dihydroxycholesterol + CA NADP(+) + H(2)O. CF Heme-thiolate. CC -!- The enzyme from mammalian liver differs from EC 1.14.13.17 in CC having no activity towards cholesterol. PR PROSITE; PDOC00081; // ID 1.14.13.61 DE 2-hydroxyquinoline 8-monooxygenase. AN 2-oxo-1,2-dihydroquinoline 8-monooxygenase. CA Quinolin-2-ol + NADH + O(2) = quinolin-2,8-diol + NAD(+) + H(2)O. CF Iron. CC -!- Quinolin-2-ol exists largely as the quinolin-2(1H)-one tautomer. // ID 1.14.13.62 DE 4-hydroxyquinoline 3-monooxygenase. AN Quinolin-4(1H)-one 3-monooxygenase. AN 1-H-4-oxoquinoline 3-monooxygenase. CA Quinolin-4-ol + NADH + O(2) = quinolin-3,4-diol + NAD(+) + H(2)O. CC -!- Quinolin-4-ol exists largely as the quinolin-4(1H)-one tautomer. // ID 1.14.13.63 DE 3-hydroxyphenylacetate 6-hydroxylase. AN 3-hydroxyphenylacetate 6-monooxygenase. CA 3-hydroxyphenylacetate + NAD(P)H + O(2) = Homogentisate + NAD(P)(+) + CA H(2)O. CF FAD. CC -!- 3-hydroxyphenylacetate 6-hydroxylase from Flavobacterium sp. is CC highly specific for 3-hydroxyphenylacetate and uses NADH and NADPH as CC electron donors with similar efficiency. // ID 1.14.13.64 DE 4-hydroxybenzoate 1-hydroxylase. AN 4-hydroxybenzoate 1-monooxygenase. CA 4-hydroxybenzoate + NAD(P)H + O(2) = hydroquinone + NAD(P)(+) + H(2)O + CA CO(2). CF FAD. CC -!- The enzyme from Candida parapsilosis is specific for 4-hydroxybenzoate CC derivatives and prefers NADH to NADPH as electron donor. // ID 1.14.13.65 DE 2-hydroxyquinoline 8-monooxygenase. AN 2-oxo-1,2-Dihydroquinoline 5,6-dioxygenase. CA Quinolin-2-ol + NADH + O(2) = quinolin-2,8-diol + NAD(+). CC -!- 3-methyl-quinolin-2-ol is also a substrate. CC -!- Quinolin-2-ol exists largely as the quinolin-2(1H)-one tautomer. // ID 1.14.13.66 DE 2-hydroxycyclohexanone 2-monooxygenase. CA 2-hydroxycyclohexan-1-one + NADPH + O(2) = 6-hydroxyhexan-6-olide + CA NADP(+) + H(2)O. CC -!- The product decomposes spontaneously to 6-oxohexanoic acid (adipic CC semialdehyde). CC -!- Formerly EC 1.14.12.6. // ID 1.14.13.67 DE Quinine 3-monooxygenase. AN Quinine 3-hydroxylase. AN Nifedipine oxidase. CA Quinine + NADPH + O(2) = 3-hydroxyquinine + NADP(+) + H(2)O. CF Heme-thiolate. PR PROSITE; PDOC00081; DR P08684, CP34_HUMAN; // ID 1.14.13.68 DE 4-hydroxyphenylacetaldehyde oxime monooxygenase. AN 4-hydroxybenzeneacetaldehyde oxime monooxygenase. CA 4-hydroxyphenylacetaldehyde oxime + NADPH + O(2) = CA 4-hydroxymandelonitrile + NADP(+) + 2 H(2)O. CF Heme-thiolate. CC -!- Part of the biosynthetic pathway for dhurrin in Sorghum bicolor. PR PROSITE; PDOC00081; DR O48958, C7E1_SORBI; // ID 1.14.13.69 DE Alkene monooxygenase. AN Alkene epoxygenase. CA Propene + NADH + O(2) = 1,2-epoxypropane + NAD(+) + H(2)O. CF Iron(2+). CC -!- The enzyme from Xanthobacter sp. strain Py2 is a multicomponent CC enzyme comprising (1) an NADH reductase, which provides the CC reductant for O(2) activation; (2) a Rieske-type ferredoxin, CC which is an electron-transfer protein; (3) an oxygenase, which CC contains the catalytic centre for alkene epoxidation and (4) a CC small protein of unknown function that is essential for activity. CC -!- The enzyme oxygenates C2 to C6 aliphatic alkenes. CC -!- With 1,2-epoxypropane as substrate, the stereospecifity of the CC epoxypropane formed is 95% (R) and 5% (S). // ID 1.14.13.70 DE Sterol 14-demethylase. AN Obtusufoliol 14-demethylase. AN Lanosterol 14-demethylase. AN Lanosterol 14-alpha-demethylase. AN Sterol 14-alpha-demethylase. AN Cytochrome P450 51. CA Obtusifoliol + 3 O(2) + 3 NADPH = 4-alpha-methyl-5-alpha-ergosta- CA 8,14,24(28)-trien-3-beta-ol + formate + 3 NADP(+) + 3 H(2)O. CF Heme-thiolate. CC -!- The enzyme (P-450) catalyzes successive hydroxylations of the CC 14-alpha-methyl group and C-15, followed by elimination as formate CC leaving the 14(15) double bond. CC -!- This enzyme acts on a range of steroids with a 14-alpha-methyl CC group. PR PROSITE; PDOC00081; DR P10613, CP51_CANAL; P50859, CP51_CANGA; P14263, CP51_CANTR; DR Q9UVC3, CP51_CUNEL; Q16850, CP51_HUMAN; Q02315, CP51_ISSOR; DR P77901, CP51_MYCTU; Q12664, CP51_PENIT; O46420, CP51_PIG ; DR Q64654, CP51_RAT ; Q09736, CP51_SCHPO; P93846, CP51_SORBI; DR O14442, CP51_UNCNE; P49602, CP51_USTMA; P93596, CP51_WHEAT; DR P10614, CP51_YEAST; // ID 1.14.13.71 DE N-methylcoclaurine 3'-monooxygenase. AN N-methylcoclaurine 3'-hydroxylase. AN (S)-N-methylcoclaurine 3'-hydroxylase. AN Cytochrome P450 80B1. CA (S)-N-methylcoclaurine + NADPH + O(2) = (S)-3'-hydroxy-N- CA methylcoclaurine + NADP(+) + H(2)O. CF Heme-thiolate. CC -!- A P-450 protein involved in benzylisoquinoline alkaloid synthesis CC in higher plants. PR PROSITE; PDOC00081; DR O64899, C8B1_ESCCA; O64900, C8B2_ESCCA; // ID 1.14.13.72 DE Methylsterol monooxygenase. AN Methylsterol hydroxylase. AN 4-methylsterol oxidase. CA 4,4-dimethyl-5-alpha-cholest-7-en-3-beta-ol + NAD(P)H + O(2) = 4-beta- CA hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + CA NAD(P)(+) + H(2)O. CA 4-beta-hydroxymethyl-4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol + CA NAD(P)H + O(2) = 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4- CA alpha-carbaldehyde + NAD(P)(+) + 2 H(2)O. CA 3-beta-hydroxy-4-beta-methyl-5-alpha-cholest-7-ene-4-alpha- CA carbaldehyde + NAD(P)H + O(2) = 3-beta-hydroxy-4-beta-methyl-5-alpha- CA cholest-7-ene-4-alpha-carboxylate + NAD(P)(+) + H(2)O. CC -!- Requires cytochrome b5. CC -!- Also acts on 4-alpha-methyl-5-alpha-cholest-7-en-3-beta-ol. CC -!- The sterol can be based on cycloartenol as well as lanosterol. CC -!- Formerly EC 1.14.99.16. // ID 1.14.13.73 DE Tabersonine 16-hydroxylase. CA Tabersonine + NADPH + O(2) = 16-hydroxytabersonine + NADP(+) + H(2)O. CF Heme-thiolate. PR PROSITE; PDOC00081; // ID 1.14.13.74 DE 7-deoxyloganin 7-hydroxylase. CA 7-deoxyloganin + NADPH + O(2) = loganin + NADP(+) + H(2)O. CF Heme-thiolate. PR PROSITE; PDOC00081; // ID 1.14.13.75 DE Vinorine hydroxylase. CA Vinorine + NADPH + O(2) = vomilenine + NADP(+) + H(2)O. CF Heme-thiolate. CC -!- Forms a stage in the biosynthesis of the indole alkaloid ajmaline. PR PROSITE; PDOC00081; // ID 1.14.13.76 DE Taxane 10-beta-hydroxylase. AN 5-alpha-taxadienol-10-beta-hydroxylase. CA Taxa-4(20),11-dien-5-alpha-yl acetate + NADPH + O(2) = 10-beta- CA hydroxytaxa-4(20),11-dien-5-alpha-yl acetate + NADP + H(2)O. CF Heme-thiolate. PR PROSITE; PDOC00081; DR Q9AXM6, T10H_TAXCU; // ID 1.14.13.77 DE Taxane 13-alpha-hydroxylase. CA Taxa-4(20),11-dien-5a-ol + NADPH + O(2) = taxa-4(20),11-dien-5a,13a-diol CA + NADP + H(2)O. CF Heme-thiolate. PR PROSITE; PDOC00081; DR Q8W4T9, T13H_TAXCU; // ID 1.14.13.78 DE Ent-kaurene oxidase. CA (1) Ent-kaur-16-ene + NADPH + O(2) = ent-kaur-16-en-19-ol + NADP(+) + CA H(2)O. CA (2) Ent-kaur-16-en-19-ol + NADPH + O(2) = ent-kaur-16-en-19-al + NADP(+) CA + 2 H(2)O. CA (3) Ent-kaur-16-en-19-al + NADPH + O(2) = ent-kaur-16-en-19-oate + CA NADP(+) + H(2)O. CC -!- Requires cytochrome P450. CC -!- Catalyzes three sucessive oxidations of the 4-methyl group of CC ent-kaurene giving kaurenoic acid. // ID 1.14.13.79 DE Ent-kaurenoic acid oxidase. CA (1) Ent-kaur-16-en-19-oate + NADPH + O(2) = ent-7-alpha-hydroxykaur- CA 16-en-19-oate + NADP(+) + H(2)O. CA (2) Ent-7-alpha-hydroxykaur-16-en-19-oate + NADPH + O(2) = gibberellin CA A(12) aldehyde + NADP(+) + 2 H(2)O. CA (3) Gibberellin A(12) aldehyde + NADPH + O(2) = gibberellin A(12) + CA NADP(+) + H(2)O. CC -!- Requires cytochrome P450. CC -!- Catalyzes three sucessive oxidations of ent-kaurenoic acid. CC -!- The second step includes a ring-B contraction giving the gibbane CC skeleton. CC -!- In pumpkin (Cucurbita maxima) ent-6-alpha,7-alpha-dihydroxykaur-16- CC en-19-oate is also formed. // ID 1.14.14.1 DE Unspecific monooxygenase. AN Microsomal monooxygenase. AN Xenobiotic monooxygenase. AN Aryl-4-monooxygenase. AN Aryl hydrocarbon hydroxylase. AN Microsomal p450. AN Flavoprotein-linked monooxygenase. AN Cytochrome p450. CA RH + reduced flavoprotein + O(2) = ROH + oxidized flavoprotein + H(2)O. CF Heme-thiolate. CC -!- Acts on a wide range of substrates including many xenobiotics, CC steroids, fatty acids, vitamins and prostaglandins. CC -!- Reactions catalyzed include hydroxylation, epoxidation, N-oxidation, CC sulfooxidation, N-, S- and O-dealkylations, desulfation, deamination, CC and reduction of azo, nitro, and N-oxide groups. CC -!- Formerly EC 1.14.14.2 and EC 1.14.99.8. PR PROSITE; PDOC00081; DR P24903, C2F1_HUMAN; O18809, C2F3_CAPHI; O35293, C2F4_RAT ; DR Q98T91, C340_ORYLA; Q9JMA7, C341_MOUSE; Q9HB55, C343_HUMAN; DR Q9Y8G7, C505_FUSOX; P13527, C6A1_MUSDO; Q04552, C6B1_PAPPO; DR Q27664, C6B2_HELAM; Q27756, C6B3_PAPPO; Q27902, C6B4_PAPGL; DR Q95036, C6B5_PAPGL; Q95031, C6B6_HELAM; O61387, C6B7_HELAM; DR P56590, CP11_CANFA; Q06367, CP11_CAVPO; Q92039, CP11_CHACA; DR P79716, CP11_DICLA; P04798, CP11_HUMAN; O42430, CP11_LIMLI; DR O42231, CP11_LIZAU; Q9W683, CP11_LIZSA; P33616, CP11_MACFA; DR Q00557, CP11_MESAU; Q92148, CP11_MICTO; P00184, CP11_MOUSE; DR Q92110, CP11_ONCMY; Q92095, CP11_OPSTA; P98181, CP11_PAGMA; DR Q9YH64, CP11_PLAFE; Q92100, CP11_PLEPL; P05176, CP11_RABIT; DR P00185, CP11_RAT ; P56591, CP11_SHEEP; O42457, CP11_SPAAU; DR Q92116, CP11_STECH; P56592, CP12_CANFA; Q64391, CP12_CAVPO; DR Q01741, CP12_CHICK; P05177, CP12_HUMAN; P24453, CP12_MESAU; DR P00186, CP12_MOUSE; P00187, CP12_RABIT; P04799, CP12_RAT ; DR Q92109, CP13_ONCMY; P79760, CP14_CHICK; P79761, CP15_CHICK; DR Q16678, CP1B_HUMAN; Q64429, CP1B_MOUSE; Q64678, CP1B_RAT ; DR P04800, CP31_RAT ; P05183, CP32_RAT ; P05184, CP33_HUMAN; DR P20815, CP35_HUMAN; P80056, CP35_PAPSP; P11707, CP36_RABIT; DR P24462, CP37_HUMAN; P33268, CP38_MACFA; P51538, CP39_RAT ; DR Q64148, CP3A_MESAU; Q64459, CP3B_MOUSE; P24463, CP3C_CANFA; DR Q64464, CP3D_MOUSE; Q64417, CP3E_CAVPO; Q64406, CP3F_CAVPO; DR Q64481, CP3G_MOUSE; Q64409, CP3H_CAVPO; Q64581, CP3I_RAT ; DR P79152, CP3J_CAPAE; O18993, CP3L_CALJA; Q29496, CP3O_SHEEP; DR O09158, CP3P_MOUSE; O42563, CP3R_ONCMY; P79102, CP3S_BOVIN; DR P79401, CP3T_PIG ; Q9PVE8, CP3U_FUNHE; O70537, CP3V_MESAU; DR P10611, CP44_RABIT; P24464, CP48_RAT ; P13584, CP4B_HUMAN; DR Q64462, CP4B_MOUSE; P15128, CP4B_RABIT; P15129, CP4B_RAT ; DR P29981, CP4C_BLADI; P11711, CPA1_RAT ; P15149, CPA2_RAT ; DR P20812, CPA3_RAT ; P15392, CPA4_MOUSE; P20852, CPA5_MOUSE; DR P11509, CPA6_HUMAN; P20853, CPA7_HUMAN; P80055, CPA7_PAPSP; DR P24454, CPA8_MESAU; P24455, CPA9_MESAU; Q05555, CPAA_RABIT; DR Q05556, CPAB_RABIT; P56593, CPAC_MOUSE; Q16696, CPAD_HUMAN; DR P22779, CPAX_BOVIN; P00176, CPB1_RAT ; P04167, CPB2_RAT ; DR P13107, CPB3_RAT ; P00178, CPB4_RABIT; P12789, CPB5_RABIT; DR P20813, CPB6_HUMAN; P12790, CPB9_MOUSE; P12791, CPBA_MOUSE; DR P24460, CPBB_CANFA; P33272, CPBC_RAT ; O55071, CPBJ_MOUSE; DR Q62397, CPBK_MOUSE; P34033, CPBX_CAVPO; P00180, CPC1_RABIT; DR P00181, CPC2_RABIT; P00182, CPC3_RABIT; P11371, CPC4_RABIT; DR P00179, CPC5_RABIT; P05178, CPC6_RAT ; P05179, CPC7_RAT ; DR P10632, CPC8_HUMAN; P11712, CPC9_HUMAN; P11713, CPCA_HUMAN; DR P08683, CPCB_RAT ; P11510, CPCC_RAT ; P20814, CPCD_RAT ; DR P17666, CPCE_RABIT; P11372, CPCF_RABIT; P15123, CPCG_RABIT; DR P33260, CPCI_HUMAN; P33261, CPCJ_HUMAN; P33262, CPCK_MACFA; DR P56594, CPCL_CANFA; P19225, CPCM_RAT ; P24470, CPCN_RAT ; DR P33273, CPCO_RAT ; Q08078, CPCP_MESAU; P33263, CPCQ_MESAU; DR P33264, CPCR_MESAU; P33265, CPCS_MESAU; Q64458, CPCT_MOUSE; DR Q29510, CPCU_RABIT; Q29478, CPCV_CAPAE; P10633, CPD1_RAT ; DR P10634, CPD2_RAT ; P12938, CPD3_RAT ; P13108, CPD4_RAT ; DR P12939, CPD5_RAT ; P10635, CPD6_HUMAN; P11714, CPD9_MOUSE; DR P24456, CPDA_MOUSE; P24457, CPDB_MOUSE; Q01361, CPDE_BOVIN; DR Q29473, CPDF_CANFA; Q64403, CPDG_CAVPO; Q29488, CPDH_MACFA; DR Q64680, CPDI_RAT ; O18992, CPDJ_CALJA; O18963, CPE1_BOVIN; DR P05181, CPE1_HUMAN; P33266, CPE1_MACFA; P51581, CPE1_MESAU; DR Q05421, CPE1_MOUSE; P79383, CPE1_PIG ; P08682, CPE1_RABIT; DR P05182, CPE1_RAT ; P33274, CPF1_RAT ; P51869, CPF4_RAT ; DR P51870, CPF5_RAT ; P51871, CPF6_RAT ; P98187, CPF8_HUMAN; DR Q9HBI6, CPFB_HUMAN; Q9HCS2, CPFC_HUMAN; P24461, CPG1_RABIT; DR P10610, CPG1_RAT ; P05180, CPH1_CHICK; P20678, CPH2_CHICK; DR P52786, CPJ1_RABIT; P51589, CPJ2_HUMAN; P51590, CPJ3_RAT ; DR O54749, CPJ5_MOUSE; O54750, CPJ6_MOUSE; Q92090, CPK1_ONCMY; DR O93299, CPK3_ONCMY; O93297, CPK4_ONCMY; Q27712, CPL1_PANAR; DR Q92088, CPM1_ONCMY; P46194, CPV1_BOVIN; O42145, CPV1_BRARE; DR P79690, CPV1_CARAU; P19098, CPV1_CHICK; P79699, CPV1_COTJA; DR O46512, CPV1_HORSE; P11511, CPV1_HUMAN; Q92111, CPV1_ICTPU; DR P28649, CPV1_MOUSE; P70091, CPV1_ORENI; Q92087, CPV1_ORYLA; DR Q29624, CPV1_PIG ; Q92112, CPV1_POEGU; Q29605, CPV1_RABIT; DR P22443, CPV1_RAT ; Q9XS28, CPV1_SHEEP; O73686, CPV2_CARAU; DR P79430, CPV2_PIG ; P79304, CPV3_PIG ; P14779, CPXB_BACME; DR P56654, CPZ2_MOUSE; P56655, CPZ3_MOUSE; P56656, CPZ4_MOUSE; DR P56657, CPZ5_MOUSE; O62671, CPZ6_CANFA; P79402, CPZ7_PIG ; DR O08394, CYPD_BACSU; O08336, CYPE_BACSU; // ID 1.14.14.2 DE Transferred entry: 1.14.14.1. // ID 1.14.14.3 DE Alkanal monooxygenase (FMN-linked). AN Bacterial luciferase. AN Aldehyde monooxygenase. CA RCHO + FMNH(2) + O(2) = RCOOH + FMN + H(2)O + light. CC -!- The reaction involves incorporation of a molecule of oxygen into CC reduced FMN, and subsequent reaction with the aldehyde to form an CC activated FMN.H(2)O complex which breaks down with emission of light. CC -!- The enzyme is highly specific for reduced FMN, and for long-chain CC aliphatic aldehydes with 8 carbons or more. PR PROSITE; PDOC00397; DR P18299, LUXA_KRYAS; P24113, LUXA_PHOPO; P24114, LUXA_VIBAB; DR P19907, LUXA_VIBFI; P07740, LUXA_VIBHA; P18300, LUXB_KRYAS; DR P12744, LUXB_PHOPO; P19908, LUXB_VIBFI; P07739, LUXB_VIBHA; DR P09140, LXA1_PHOLE; P19839, LXA1_PHOLU; P29238, LXA2_PHOLE; DR P23146, LXA2_PHOLU; P09141, LXB1_PHOLE; P19840, LXB1_PHOLU; DR P29239, LXB2_PHOLE; P23147, LXB2_PHOLU; // ID 1.14.14.4 DE Deleted entry. // ID 1.14.14.5 DE Alkanesulfonate monooxygenase. AN Sulfate starvation-induced protein 6. AN FMNH2-dependent aliphatic sulfonate monooxygenase. CA An alkanesufonate (R-CH(2)-SO(3)H) + FMNH(2) + O(2) = an aldehyde CA (R-CHO) + FMN + sulfite + H(2)O. CC -!- The enzyme from Escherichia coli catalyzes the desulfonation of a CC wide range of aliphatic sulfonates (unsubstituted C(1)- to C(14)- CC sulfonates as well as substituted C(2)-sulfonates). CC -!- Does not desulfonate taurine (2-aminoethanesulfonate) or aromatic CC sulfonates. CC -!- Does not use FMN as a bound cofactor. CC -!- Instead, it uses reduced FMN (i.e., FMNH(2)) as a substrate. CC -!- FMNH(2) is provided by SsuE, the associated FMN reductase CC (EC 1.5.1.29). DR Q9I1C2, MSUD_PSEAE; Q98CB9, SSD1_RHILO; Q98DT4, SSD2_RHILO; DR Q8UAE8, SSUD_AGRT5; P40402, SSUD_BACSU; Q89ER2, SSUD_BRAJA; DR Q9KHR3, SSUD_BUTSP; Q8XDD9, SSUD_ECO57; Q8FJ93, SSUD_ECOL6; DR P80645, SSUD_ECOLI; Q9HYG2, SSUD_PSEAE; Q88R95, SSUD_PSEPK; DR O85764, SSUD_PSEPU; Q87ZG3, SSUD_PSESM; Q9KHS2, SSUD_PSESP; DR Q8XZQ6, SSUD_RALSO; P59189, SSUD_SHIFL; Q8PP38, SSUD_XANAC; DR Q8ZB04, SSUD_YERPE; // ID 1.14.15.1 DE Camphor 5-monooxygenase. AN Camphor 5-exo-methylene hydroxylase. AN Cytochrome p450-cam. CA (+)-camphor + putidaredoxin + O(2) = (+)-exo-5-hydroxycamphor + oxidized CA putidaredoxin + H(2)O. CF Heme-thiolate. CC -!- Also acts on (-)-camphor and 1,2A-campholide, forming 5-exo-hydroxy- CC 1,2-campholide. PR PROSITE; PDOC00081; DR P00183, CPXA_PSEPU; // ID 1.14.15.2 DE Camphor 1,2-monooxygenase. AN 2,5-diketocamphane lactonizing enzyme. AN Camphor ketolactonase I. CA (+)-bornane-2,5-dione + reduced rubredoxin + O(2) = 5-oxo-1,2-campholide CA + oxidized rubredoxin + H(2)O. CF Iron. // ID 1.14.15.3 DE Alkane-1 monooxygenase. AN Alkane 1-hydroxylase. AN Lauric acid omega-hydroxylase. AN Omega-hydroxylase. AN Fatty acid omega-hydroxylase. CA Octane + reduced rubredoxin + O(2) = 1-octanol + oxidized rubredoxin + CA H(2)O. CC -!- Some enzyme of this group are heme-thiolated proteins (p450). CC -!- Also hydroxylates fatty acids in the omega-position. PR PROSITE; PDOC00081; DR P12691, ALKB_PSEOL; P08516, CP41_RAT ; P20816, CP42_RAT ; DR P20817, CP43_RAT ; P14579, CP45_RABIT; P14580, CP46_RABIT; DR P14581, CP47_RABIT; Q02928, CP4Y_HUMAN; // ID 1.14.15.4 DE Steroid 11-beta-monooxygenase. AN Steroid 11-beta-hydroxylase. AN Steroid 11-beta/18-hydroxylase. AN Cytochrome p450 XIB1. CA A steroid + reduced adrenal ferredoxin + O(2) = an 11-beta- CA hydroxysteroid + oxidized adrenal ferredoxin + H(2)O. CF Heme-thiolate. CC -!- Also hydroxylates steroids at the 18-position, and converts CC 18-hydroxycorticosterone into aldosterone. DI Adrenal hyperplasia IV; MIM:202010. PR PROSITE; PDOC00081; DR P15150, CPN1_BOVIN; Q64408, CPN1_CAVPO; P15538, CPN1_HUMAN; DR P97720, CPN1_MESAU; Q29527, CPN1_PAPHA; Q29552, CPN1_PIG ; DR Q92104, CPN1_RANCA; P15393, CPN1_RAT ; P51663, CPN1_SHEEP; DR P19099, CPN2_HUMAN; Q64658, CPN2_MESAU; P15539, CPN2_MOUSE; DR P30099, CPN2_RAT ; P30100, CPN3_RAT ; // ID 1.14.15.5 DE Corticosterone 18-monooxygenase. AN Corticosterone 18-hydroxylase. AN Corticosterone methyloxidase. CA Corticosterone + reduced adrenal ferredoxin + O(2) = CA 18-hydroxycorticosterone + oxidized adrenal ferredoxin + H(2)O. CF Heme-thiolate. DI Aldosterone deficiency I; MIM:203400. DI Aldosterone deficiency II; MIM:203410. PR PROSITE; PDOC00081; // ID 1.14.15.6 DE Cholesterol monooxygenase (side-chain cleaving). AN Cholesterol desmolase. AN Cholesterol side-chain cleavage enzyme. AN Cholesterol side-chain cleaving enzyme. AN Cytochrome p450(SCC). AN Cytochrome P-450scc. AN Cholesterol 20-22-desmolase. AN Cholesterol C20-22 desmolase. AN Steroid 20-22 desmolase. AN Steroid 20-22-lyase. CA Cholesterol + reduced adrenal ferredoxin + O(2) = pregnenolone + CA 4-methylpentanal + oxidized adrenal ferredoxin + H(2)O. CF Heme-thiolate. CC -!- The reaction proceeds in three stages, with hydroxylation at C-20 CC and C-22 preceding scission of the side-chain at C-20. PR PROSITE; PDOC00081; DR P00189, C11A_BOVIN; P79153, C11A_CAPHI; Q92045, C11A_DASAM; DR O46515, C11A_HORSE; P05108, C11A_HUMAN; Q9EPT4, C11A_MESAU; DR Q9QZ82, C11A_MOUSE; Q07217, C11A_ONCMY; P10612, C11A_PIG ; DR Q28827, C11A_RABIT; P14137, C11A_RAT ; P79202, C11A_SHEEP; // ID 1.14.15.7 DE Choline monooxygenase. CA Choline + O(2) + 2 reduced ferredoxin = betaine aldehyde hydrate + H(2)O + CA 2 oxidized ferredoxin. CF Magnesium; Iron-Sulfur. CC -!- Catalyzes the first step of glycine betaine synthesis. DR Q93XE1, CHMO_AMATR; Q9SZR0, CHMO_ARATH; Q9LKN0, CHMO_ATRHO; DR O22553, CHMO_BETVU; O04121, CHMO_SPIOL; // ID 1.14.16.1 DE Phenylalanine 4-monooxygenase. AN Phenylalanine 4-hydroxylase. AN Phenylalaninase. AN Phenylalanine hydroxylase. AN PAH. CA L-phenylalanine + tetrahydrobiopterin + O(2) = L-tyrosine + CA dihydrobiopterin + H(2)O. CC -!- The reaction involves an arene oxide which rearranges to give the CC phenolic hydroxy group. CC -!- This results in the hydrogen at C-4 migrating to C-3 and in part CC being retained, a process known as the NIH-shift. DI Phenylketonuria; MIM:261600. PR PROSITE; PDOC00316; DR P90925, PH4H_CAEEL; Q9A7V7, PH4H_CAUCR; P30967, PH4H_CHRVO; DR P17276, PH4H_DROME; P00439, PH4H_HUMAN; P16331, PH4H_MOUSE; DR P43334, PH4H_PSEAE; Q8XU39, PH4H_RALSO; P04176, PH4H_RAT ; DR Q98D72, PH4H_RHILO; Q9KLB8, PH4H_VIBCH; // ID 1.14.16.2 DE Tyrosine 3-monooxygenase. AN Tyrosine 3-hydroxylase. CA L-tyrosine + tetrahydropteridine + O(2) = 3,4-dihydroxy-L- CA phenylalanine + dihydropteridine + H(2)O. CF Iron. CC -!- Activated by phosphorylation, catalyzed by EC 2.7.1.128. PR PROSITE; PDOC00316; DR O42091, TY3H_ANGAN; P17289, TY3H_BOVIN; P90986, TY3H_CAEEL; DR P18459, TY3H_DROME; P07101, TY3H_HUMAN; P24529, TY3H_MOUSE; DR P11982, TY3H_PHASP; P04177, TY3H_RAT ; O17446, TY3H_SCHMA; // ID 1.14.16.3 DE Anthranilate 3-monooxygenase. AN Anthranilate 3-hydroxylase. AN Anthranilic hydroxylase. AN Anthranilic acid hydroxylase. CA Anthranilate + tetrahydropteridine + O(2) = 3-hydroxyanthranilate + CA dihydropteridine + H(2)O. CF Iron. // ID 1.14.16.4 DE Tryptophan 5-monooxygenase. AN Tryptophan 5-hydroxylase. CA L-tryptophan + tetrahydropteridine + O(2) = 5-hydroxy-L-tryptophan + CA dihydropteridine + H(2)O. CF Iron. CC -!- Activated by phosphorylation, catalyzed by a Ca(2+)-activated CC protein kinase. PR PROSITE; PDOC00316; DR P17276, PH4H_DROME; P70080, TPH1_CHICK; P17752, TPH1_HUMAN; DR P17532, TPH1_MOUSE; P17290, TPH1_RABIT; P09810, TPH1_RAT ; DR Q8IWU9, TPH2_HUMAN; Q8CGV2, TPH2_MOUSE; Q8CGU9, TPH2_RAT ; DR Q92142, TPH_XENLA ; // ID 1.14.16.5 DE Glyceryl-ether monooxygenase. AN Glyceryl-ether cleaving enzyme. AN Glyceryl etherase. CA 1-alkyl-sn-glycerol + tetrahydropteridine + O(2) = CA 1-hydroxyalkyl-sn-glycerol + dihydropteridine + H(2)O. CF Glutathione. CC -!- Requires phospholipids for full activity. CC -!- The product spontaneously breaks down to form a fatty aldehyde and CC glycerol. CC -!- Formerly EC 1.14.99.17. // ID 1.14.16.6 DE Mandelate 4-monooxygenase. AN L-mandelate 4-hydroxylase. AN Mandelic acid 4-hydroxylase. CA (S)-2-hydroxy-2-phenylacetate + tetrahydropteridine + O(2) = CA (S)-4-hydroxymandelate + dihydropteridine + H(2)O. CF Iron. // ID 1.14.17.1 DE Dopamine-beta-monooxygenase. AN Dopamine beta-hydroxylase. CA 3,4-dihydroxyphenethylamine + ascorbate + O(2) = noradrenaline + CA dehydroascorbate + H(2)O. CF Copper. CC -!- Stimulated by fumarate. PR PROSITE; PDOC00080; DR P15101, DOPO_BOVIN; P09172, DOPO_HUMAN; Q64237, DOPO_MOUSE; DR Q05754, DOPO_RAT ; // ID 1.14.17.2 DE Transferred entry: 1.14.18.1. // ID 1.14.17.3 DE Peptidylglycine monooxygenase. AN Peptidyl alpha-amidating enzyme. AN PAM AN Peptidyl-glycine alpha-amidating monooxygenase. AN Peptidylglycine 2-hydroxylase. CA Peptidylglycine + ascorbate + O(2) = peptidyl(2-hydroxyglycine) + CA dehydroascorbate + H(2)O. CF Copper. CC -!- Peptidylglycines with a neutral amino acid residue in the penultimate CC position are the best substrates for the enzyme. CC -!- The enzyme also catalyzes the dismutation of the product to CC glyoxylate and the corresponding desglycine peptide amide. CC -!- Involved in the final step of biosynthesis of alpha-melanotropin CC and related biologically active peptides. PR PROSITE; PDOC00080; DR P08478, AMD1_XENLA; P12890, AMD2_XENLA; P10731, AMD_BOVIN ; DR P19021, AMD_HUMAN ; P97467, AMD_MOUSE ; P14925, AMD_RAT ; // ID 1.14.18.1 DE Monophenol monooxygenase. AN Tyrosinase. AN Phenolase. AN Monophenol oxidase. AN Cresolase. CA L-tyrosine + L-DOPA + O(2) = L-DOPA + DOPAquinone + H(2)O. CF Copper. CC -!- A group of copper proteins that also catalyze the reaction of CC EC 1.10.3.1, if only 1,2-benzenediols are available as substrate. CC -!- Formerly EC 1.14.17.2. DI Albinism; MIM:203100. PR PROSITE; PDOC00398; DR O42713, TYRO_AGABI; Q00234, TYRO_ASPOR; P54834, TYRO_CANFA; DR P55024, TYRO_CHICK; Q08410, TYRO_COTJA; P55033, TYRO_FELCA; DR P14679, TYRO_HUMAN; P11344, TYRO_MOUSE; P00440, TYRO_NEUCR; DR P55025, TYRO_ORYLA; Q92396, TYRO_PODAN; Q04604, TYRO_RANNI; DR P33180, TYRO_RHIME; P55022, TYRO_STRAL; P07524, TYRO_STRAT; DR P06845, TYRO_STRGA; P55023, TYRO_STRLN; P55026, TYRO_TRISI; // ID 1.14.19.1 DE Stearoyl-CoA 9-desaturase. AN Stearoyl-CoA desaturase. AN Acyl-CoA desaturase. AN Fatty acid desaturase. AN Delta(9)-desaturase. CA Stearoyl-CoA + AH(2) + O(2) = oleoyl-CoA + A + 2 H(2)O. CF Iron. CC -!- The rat liver enzyme is an enzyme system involving cytochrome b5 and CC EC 1.6.2.2. CC -!- Formerly EC 1.14.99.5. PR PROSITE; PDOC00399; DR P13516, ACO1_MOUSE; P21147, ACO1_YEAST; P13011, ACO2_MOUSE; DR Q9TT94, ACOD_BOVIN; O00767, ACOD_HUMAN; Q64420, ACOD_MESAU; DR O02858, ACOD_PIG ; P07308, ACOD_RAT ; O62849, ACOD_SHEEP; // ID 1.14.19.2 DE Acyl-[acyl-carrier protein] desaturase. AN Stearyl-ACP desaturase. AN Stearyl acyl carrier protein desaturase. CA Stearoyl-[acyl-carrier protein] + AH(2) + O(2) = oleoyl-[acyl-carrier CA protein] + A + 2 H(2)O. CC -!- The enzyme from safflower is specific for stearoyl-CoA; that from CC Euglena acts on derivatives of a number of long-chain fatty acids. CC -!- Requires ferredoxin. CC -!- Formerly EC 1.14.99.6. PR PROSITE; PDOC00399; DR P29108, STAD_BRANA; P22243, STAD_CARTI; P32063, STAD_CORSA; DR P32061, STAD_CUCSA; O24428, STAD_ELAGV; Q42770, STAD_GOSHI; DR Q96456, STAD_HELAN; P32062, STAD_LINUS; Q43593, STAD_OLEEU; DR Q40731, STAD_ORYSA; P22337, STAD_RICCO; Q01753, STAD_SIMCH; DR Q41319, STAD_SOLCO; P46253, STAD_SOLTU; Q42807, STAD_SOYBN; DR P28645, STAD_SPIOL; Q01771, STAS_BRANA; // ID 1.14.19.3 DE Linoleoyl-CoA desaturase. AN Delta(6)-desaturase. AN Delta(6)-fatty acyl-CoA desaturase. AN Delta(6)-acyl CoA desaturase. AN Fatty acid delta(6)-desaturase. AN Fatty acid 6-desaturase. AN Linoleate desaturase. AN Linoleic desaturase. AN Linoleic acid desaturase. AN Linoleoyl CoA desaturase. AN Linoleoyl-coenzyme A desaturase. AN Long-chain fatty acid Delta(6)-desaturase. CA Linoleoyl-CoA + AH(2) + O(2) = gamma-linolenoyl-CoA + A + 2 H(2)O. CF Iron. CC -!- The rat liver enzyme is an enzyme system involving cytochrome b5 and CC EC 1.6.2.2. CC -!- Formerly EC 1.14.99.25. DR Q08871, LLCD_SYNY3; // ID 1.14.20.1 DE Deacetoxycephalosporin-C synthase. AN DAOCS. AN Penicillin N expandase. CA Penicillin N + 2-oxoglutarate + O(2) = deacetoxycephalosporin C + CA succinate + CO(2) + H(2)O. CC -!- Forms part of the penicillin biosynthesis pathway. DR Q03047, CEFE_NOCLA; P18548, CEFE_STRCL; P11935, EXPA_CEPAC; // ID 1.14.21.1 DE (S)-stylopine synthase. AN (S)-cheilanthifoline oxidase (methylenedioxy-bridge-forming). CA (S)-cheilanthifoline + NADPH + O(2) = (S)-stylopine + NADP(+) + 2 H(2)O. CF Heme-thiolate. CC -!- Catalyzes an oxidative reaction that does not incorporate oxygen CC into the product. CC -!- Forms the second methylenedioxy bridge of the protoberberine CC alkaloid stylopine from oxidative ring closure of adjacent phenolic CC and methoxy groups of cheilanthifoline. CC -!- Formerly EC 1.1.3.32. // ID 1.14.21.2 DE (S)-cheilanthifoline synthase. AN (S)-scoulerine oxidase (methylenedioxy-bridge-forming). CA (S)-scoulerine + NADPH + O(2) = (S)-cheilanthifoline + NADP(+) + 2 H(2)O. CF Heme-thiolate. CC -!- Catalyzes an oxidative reaction that does not incorporate oxygen CC into the product. CC -!- Forms the methylenedioxy bridge of the protoberberine alkaloid CC cheilanthifoline from oxidative ring closure of adjacent phenolic CC and methoxy groups of scoulerine. CC -!- Formerly EC 1.1.3.33. // ID 1.14.21.3 DE Berbamunine synthase. AN (S)-N-methylcoclaurine oxidase (C-O phenol-coupling). CA (S)-N-methylcoclaurine + (R)-N-methylcoclaurine + NADPH + O(2) = CA berbamunine + NADP(+) + 2 H(2)O. CF Heme-thiolate. CC -!- Forms the bisbenzylisoquinoline alkaloid berbamunine by phenol CC oxidation of N-methylcoclaurine without the incorporation of oxygen CC into the product. CC -!- Reaction of 2 molecules of (R)-N-methylcoclaurine gives the dimer CC guattagaumerine. CC -!- Formerly EC 1.1.3.34. PR PROSITE; PDOC00081; DR P47195, CP80_BERST; // ID 1.14.21.4 DE Salutaridine synthase. AN (R)-reticuline oxidase (C-C phenol-coupling). CA (R)-reticuline + NADPH + O(2) = salutaridine + NADP(+) + 2 H(2)O. CF Heme-thiolate. CC -!- Forms the morphinan alkaloid salutaridine by intramolecular phenol CC oxidation of reticuline without the incorporation of oxygen into the CC product. CC -!- Formerly EC 1.1.3.35. PR PROSITE; PDOC00081; // ID 1.14.21.5 DE (S)-canadine synthase. AN (S)-tetrahydrocolumbamine oxidase (methylenedioxy-bridge-forming). AN (S)-tetrahydroberberine synthase. CA (S)-tetrahydrocolumbamine + NADPH + O(2) = (S)-canadine + NADP(+) + CA 2 H(2)O. CF Heme-thiolate. CC -!- Catalyzes an oxidative reaction that does not incorporate oxygen into CC the product. CC -!- Oxidation of the methoxyphenol group of the alkaloid CC tetrahydrocolumbamine results in the formation of the methylenedioxy CC bridge of canadine. CC -!- Formerly EC 1.1.3.36. PR PROSITE; PDOC00081; // ID 1.14.99.1 DE Prostaglandin-endoperoxide synthase. AN Prostaglandin synthase. AN Prostaglandin synthetase. AN Prostaglandin G/H synthase. AN PG synthetase. CA Arachidonate + AH(2) + 2 O(2) = prostaglandin H2 + A + H(2)O. CC -!- Acts both as a dioxygenase and as a peroxidase. DR O62664, PGH1_BOVIN; P23219, PGH1_HUMAN; P22437, PGH1_MOUSE; DR Q63921, PGH1_RAT ; P05979, PGH1_SHEEP; O62698, PGH2_BOVIN; DR P70682, PGH2_CAVPO; P27607, PGH2_CHICK; O19183, PGH2_HORSE; DR P35354, PGH2_HUMAN; Q05769, PGH2_MOUSE; O62725, PGH2_MUSVI; DR O02768, PGH2_RABIT; P35355, PGH2_RAT ; P79208, PGH2_SHEEP; // ID 1.14.99.2 DE Kynurenine 7,8-hydroxylase. CA Kynurenate + AH(2) + O(2) = 7,8-dihydro-7,8-dihydroxykynurenate + A. // ID 1.14.99.3 DE Heme oxygenase (decyclizing). CA Heme + 3 AH(2) + O(2) = biliverdin + Fe(2+) + CO + 3 A + 3 H(2)O. CC -!- Requires NAD(P)H and EC 1.6.2.4. PR PROSITE; PDOC00512; DR P71119, HMUO_CORDI; P09601, HO1_HUMAN ; P14901, HO1_MOUSE ; DR P32394, HO1_PIG ; P06762, HO1_RAT ; P72849, HO1_SYNY3 ; DR P30519, HO2_HUMAN ; O70252, HO2_MOUSE ; P43242, HO2_RABIT ; DR P23711, HO2_RAT ; P74133, HO2_SYNY3 ; O70453, HO3_RAT ; DR P14791, HO_CHICK ; O73688, HO_FUGRU ; O78497, HO_GUITH ; DR P51271, HO_PORPU ; O19998, HO_RHOVL ; // ID 1.14.99.4 DE Progesterone monooxygenase. AN Progesterone hydroxylase. CA Progesterone + AH(2) + O(2) = testosterone acetate + A + H(2)O. CC -!- Has a wide specificity. CC -!- A single enzyme from Cylindrocarpon radicicola (EC 1.14.13.54) CC catalyzes both this reaction and that catalyzed by EC 1.14.99.12. // ID 1.14.99.5 DE Transferred entry: 1.14.19.1. // ID 1.14.99.6 DE Transferred entry: 1.14.19.2. // ID 1.14.99.7 DE Squalene monooxygenase. AN Squalene epoxidase. CA Squalene + AH(2) + O(2) = (S)-squalene-2,3-epoxide + A + H(2)O. CF FAD. CC -!- This enzyme, together with EC 5.4.99.7, was formerly known as CC squalene oxydocyclase. DR O65404, ER11_ARATH; O65727, ER11_BRANA; O65402, ER12_ARATH; DR O65726, ER12_BRANA; O65403, ER13_ARATH; Q92206, ERG1_CANAL; DR O13306, ERG1_CANGA; Q14534, ERG1_HUMAN; P52019, ERG1_MOUSE; DR O48651, ERG1_PANGI; P52020, ERG1_RAT ; P32476, ERG1_YEAST; // ID 1.14.99.8 DE Transferred entry: 1.14.14.1. // ID 1.14.99.9 DE Steroid 17-alpha-monooxygenase. AN Steroid 17-alpha-hydroxylase/17,20 lyase. AN Cytochrome p450 XVIIA1. AN Steroid 17-alpha-hydroxylase. CA A steroid + AH(2) + O(2) = a 17-alpha-hydroxysteroid + A + H(2)O. CF Heme-thiolate. DI Adrenal hyperplasia V; MIM:202110. PR PROSITE; PDOC00081; DR P05185, CPT7_BOVIN; Q64410, CPT7_CAVPO; P12394, CPT7_CHICK; DR Q95328, CPT7_HORSE; P05093, CPT7_HUMAN; O73853, CPT7_ICTPU; DR P70687, CPT7_MESAU; P27786, CPT7_MOUSE; P30437, CPT7_ONCMY; DR P70085, CPT7_ORYLA; P19100, CPT7_PIG ; O57525, CPT7_RANDY; DR P11715, CPT7_RAT ; Q29497, CPT7_SHEEP; Q92113, CPT7_SQUAC; // ID 1.14.99.10 DE Steroid 21-monooxygenase. AN Steroid 21-hydroxylase. AN Cytochrome p450 XXIA1. CA A steroid + AH(2) + O(2) = a 21-hydroxysteroid + A + H(2)O. CF Heme-thiolate. DI Adrenal hyperplasia III; MIM:201910. PR PROSITE; PDOC00081; DR P00191, CPS1_BOVIN; P08686, CPS1_HUMAN; P03940, CPS1_MOUSE; DR P15540, CPS1_PIG ; Q02390, CPS3_PIG ; // ID 1.14.99.11 DE Estradiol 6-beta-monooxygenase. AN Estradiol 6-beta-hydroxylase. CA Estradiol-17-beta + AH(2) + O(2) = 6-beta-hydroxyestradiol-17-beta + A + CA H(2)O. // ID 1.14.99.12 DE Androst-4-ene-3,17-dione monooxygenase. AN 4-androstene-3,17-dione monooxygenase. AN Androstene-3,17-dione hydroxylase. AN Androst-4-ene-3,17-dione 17-oxidoreductase. AN Androstenedione monooxygenase. CA Androst-4-ene-3,17-dione + AH(2) + O(2) = 3-oxo-13,17-secoandrost-4-eno- CA 17,13-alpha-lactone + A + H(2)O. CC -!- Has a wide specificity. CC -!- A single enzyme from Cylindrocarpon radicicola (EC 1.14.13.54) CC catalyzes both this reaction and that catalyzed by EC 1.14.99.4. // ID 1.14.99.13 DE Transferred entry: 1.14.13.23. // ID 1.14.99.14 DE Progesterone 11-alpha-monooxygenase. AN Progesterone 11-alpha-hydroxylase. CA Progesterone + AH(2) + O(2) = 11-alpha-hydroxyprogesterone + A + H(2)O. // ID 1.14.99.15 DE 4-methoxybenzoate monooxygenase (O-demethylating). AN 4-Methoxybenzoate O-demethylase. CA 4-methoxybenzoate + AH(2) + O(2) = 11-alpha-hydroxyprogesterone + A + CA H(2)O. CF Flavoprotein; Iron-sulfur. CC -!- The bacterial enzyme consists of a ferredoxin-type protein and an CC iron-sulfur flavoprotein (FMN). CC -!- Also acts on 4-ethoxybenzoate, N-methyl-4-aminobenzoate and toluate. CC -!- The fungal enzyme acts best on veratrate. // ID 1.14.99.16 DE Transferred entry: 1.14.13.72. // ID 1.14.99.17 DE Transferred entry: 1.14.16.5. // ID 1.14.99.18 DE CMP-N-acetylneuraminate monooxygenase. AN N-acetylneuraminate monooxygenase. AN Cytidine-5'-monophosphate-N-acetylneuraminic acid hydroxylase. AN CMP-Neu5Ac hydroxylase. CA CMP-N-acetylneuraminate + AH(2) + O(2) = CMP-N-glycoloylneuraminate + A + CA H(2)O. CF Iron. CC -!- Specific for the sugar nucleotide cytidine-5'-monophosphate- CC N-acetylneuraminic acid and not for the free N-acetylneuraminic CC acid sugar. CC -!- Accepts reducing equivalents from NADH and, to a lesser extent, CC from NADPH via the cytochrome b5 reductase: cytochrome b5 system. CC -!- Either NADPH or ascorbate can act as AH(2). // ID 1.14.99.19 DE Plasmenylethanolamine desaturase. AN Alkylacylglycerophosphoethanolamine desaturase. CA O-1-alkyl-2-acyl-sn-glycero-3-phosphoethanolamine + AH(2) + O(2) = CA O-1-alk-1-enyl-2-acyl-sn-glycero-3-phosphoethanolamine + A + 2 H(2)O. CF Magnesium. CC -!- Either NADPH or NADH can act as AH(2). CC -!- May involve cytochrome b5. CC -!- Requires ATP. // ID 1.14.99.20 DE Phylloquinone monooxygenase (2,3-epoxidizing). AN Phylloquinone epoxidase. CA Phylloquinone + AH(2) + O(2) = 2,3-epoxyphylloquinone + A + H(2)O. // ID 1.14.99.21 DE Latia-luciferin monooxygenase (demethylating). CA Latia luciferin + AH(2) + 2 O(2) = oxidized Latia luciferin + CO(2) + CA formate + A + H(2)O + light. CF Flavoprotein. CC -!- Latia luciferin is (E)-2-methyl-4-(2,6,6-trimethyl-1-cyclohex-1-yl)- CC 1-buten-1-ol formate. CC -!- The reaction possibly involves two enzymes, an oxygenase followed by CC a monooxygenase for the actual light-emitting step. // ID 1.14.99.22 DE Ecdysone 20-monooxygenase. CA Ecdysone + AH(2) + O(2) = 20-hydroxyecdysone + A + H(2)O. CF Heme-thiolate. CC -!- An enzyme from insect fat body or malpighian tubules. CC -!- NADPH can act as ultimate hydrogen donor. PR PROSITE; PDOC00081; // ID 1.14.99.23 DE 3-hydroxybenzoate 2-monooxygenase. AN 3-hydroxybenzoate 2-hydroxylase. CA 3-hydroxybenzoate + AH(2) + O(2) = 2,3-dihydroxybenzoate + A + H(2)O. // ID 1.14.99.24 DE Steroid 9-alpha-monooxygenase. AN Steroid 9-alpha-hydroxylase. CA Pregna-4,9(11)-diene-3,20-dione + AH(2) + O(2) = 9,11-alpha- CA epoxypregn-4-ene-3,20-dione + A + H(2)O. CF FMN; Iron-sulfur. CC -!- An enzyme system involving a flavoprotein (FMN) and two iron-sulfur CC proteins. // ID 1.14.99.25 DE Transferred entry: 1.14.19.3. // ID 1.14.99.26 DE 2-hydroxypyridine 5-monooxygenase. AN 2-Hydroxypyridine oxygenase. CA 2-hydroxypyridine + AH(2) + O(2) = 2,5-hydroxypyridine + A + H(2)O. CC -!- Also oxidizes 2,5-dihydroxypyridine, but does not act on CC 3-hydroxypyridine, 4-hydroxypyridine or 2,6-dihydroxypyridine. // ID 1.14.99.27 DE Juglone 3-monooxygenase. CA 5-hydroxy-1,4-naphthoquinone + AH(2) + O(2) = 3,5-dihydroxy-1,4- CA naphthoquinone + A + H(2)O. CC -!- Also acts on 1,4-naphthoquinone, naphthazarin and 2-chloro-1,4- CC naphthoquinone, but not on other related compounds. // ID 1.14.99.28 DE Linalool 8-monooxygenase. CA 3,7-dimethylocta-1,6-dien-3-ol + AH(2) + O(2) = (E)-3,7-dimethylocta- CA 1,6-dien-3,8-diol + A + H(2)O. CF Heme-thiolate. PR PROSITE; PDOC00081; DR Q59723, CPXO_PSEPU; // ID 1.14.99.29 DE Deoxyhypusine monooxygenase. AN Deoxyhypusine hydroxylase. CA Protein N(6)-(4-aminobutyl)-L-lysine + AH(2) + O(2) = protein N(6)- CA [(R)-4-amino-2-hydroxybutyl]-L-lysine + A + H(2)O. CC -!- Catalyzes the final step in the formation of the amino acid hypusine CC in eukaryotic initiation factor 5A (eIF-5A) (formerly eIF-4D). // ID 1.14.99.30 DE Carotene 7,8-desaturase. AN Zeta-carotene desaturase. CA Neurosporene + AH(2) + O(2) = lycopene + A + 2 H(2)O. CC -!- Also acts on zeta-carotene twice to give lycopene; on pro-zeta- CC carotene to give prolycopene; on beta-zeacarotene to give gamma- CC carotene. DR Q9R6X4, ZDS_ANASP ; Q38893, ZDS_ARATH ; Q9SMJ3, ZDS_CAPAN ; DR Q9SE20, ZDS_LYCES ; Q9ZTP4, ZDS_MAIZE ; O49901, ZDS_NARPS ; DR P74306, ZDS_SYNY3 ; Q9FV46, ZDS_TARER ; // ID 1.14.99.31 DE Myristoyl-CoA 11-(E) desaturase. CA Myristoyl-CoA + NAD(P)H + O(2) = (E)-11-tetradecenoyl-CoA + NAD(P)(+) + CA 2 H(2)O. CC -!- Involved in sex pheromone synthesis in Spodoptera littoralis. CC -!- (E)-11-tetradecenoyl-CoA is formed by stereospecific removal of the CC pro-(R) H at C-11 and the pro-(S) H at C-12. CC -!- EC 1.14.99.32 forms the (Z) isomer by stereospecific cleavage of CC pro-(R) H at C-11 and C-12. // ID 1.14.99.32 DE Myristoyl-CoA 11-(Z) desaturase. CA Myristoyl-CoA + NAD(P)H + O(2) = (Z)-11-tetradecenoyl-CoA + NAD(P)(+) + CA 2 H(2)O. CC -!- Involved in sex pheromone synthesis in Spodoptera littoralis. CC -!- (Z)-11-tetradecenoyl-CoA is formed by stereospecific removal of H CC from the pro-(R) positions at C-11 and C-12. CC -!- EC 1.14.99.32 forms the (E)-isomer by removing the pro-(R) H group CC at C-11 and the pro-(S) H group at C-12. // ID 1.14.99.33 DE Delta(12)-fatty acid dehydrogenase. AN Crepenynate synthase. AN Delta-12 fatty acid acetylenase. AN Linoleate delta(12)-fatty acid acetylenase (desaturase). CA Linoleate + AH(2) + O(2) = crepenynate + A + H(2)O. CF Iron. DR O81931, D12_CREAL ; // ID 1.14.99.34 DE Monoprenyl isoflavone epoxidase. AN Monoprenyl isoflavone monooxygenase. CA 7-O-methylluteone + NADPH + O(2) = dihydrofurano derivatives + CA NADP(+) + H(2)O. CF FAD. CC -!- The enzyme has a high specificity for monoprenyl isoflavone. CC -!- The product of the prenyl epoxidation reaction contains an oxygen CC atom derived from O(2), but not from H(2)O. It is slowly and CC nonenzymically converted into the corresponding dihydrofurano CC derivative. // ID 1.14.99.35 DE Thiophene-2-carbonyl-CoA monooxygenase. AN Thiophene-2-carboxyl-CoA dehydrogenase. AN Thiophene-2-carboxyl-CoA hydroxylase. AN Thiophene-2-carboxyl-CoA monooxygenase. CA Thiophene-2-carbonyl-CoA + AH(2) + O(2) = 5-hydroxythiophene-2-carbonyl-CoA + CA A + H(2)O. CF Molybdenum. CC -!- Highly specific for thiophene-2-carbonyl-CoA. CC -!- Tetrazolium salts can act as electron acceptors. // ID 1.14.99.36 DE Beta-carotene 15,15'-dioxygenase. AN Carotene 15,15'-dioxygenase. AN Carotene dioxygenase. CA Beta-carotene + O(2) = 2 retinal. CF Bile salts; Iron. CC -!- The reaction proceeds in three stages, epoxidation of the CC 15,15'-double bond, hydration of the double bond leading to ring CC opening, and oxidative cleavage of the diol formed (cf. EC CC 1.14.15.6). Thus only one atom of the dioxygen is incorporated CC into retinal. CC -!- Formerly EC 1.13.11.21 and EC 1.18.3.1. // ID 1.14.99.37 DE Taxadiene 5-alpha-hydroxylase. CA taxa-4,11-diene + AH(2) + O(2) = taxa-4(20),11-dien-5-alpha-ol + A + CA H(2)O. CC -!- Requires P-450. CC -!- The reaction includes rearrangement of the 4(5)-double bond to a CC 4(20)-double bond, possibly through allylic oxidation. // ID 1.15.1.1 DE Superoxide dismutase. CA 2 superoxide + 2 H(+) = O(2) + H(2)O(2). CF Copper and Zinc or Iron or Manganese. PR PROSITE; PDOC00082; PR PROSITE; PDOC00083; DR P22076, DESR_DESDE; Q94EG3, NEC1_NICLS; Q9SPV5, NEC1_NICPL; DR O50258, NLR_DESGI ; O67149, SOD1_AQUAE; Q42611, SOD1_BRAJU; DR O08461, SOD1_HALME; P09737, SOD1_HALN1; Q03303, SOD1_HALSG; DR Q03300, SOD1_HALVO; P14830, SOD1_LYCES; P93258, SOD1_MESCR; DR P28756, SOD1_ORYSA; P50058, SOD1_PLEBO; P53636, SOD1_SALTY; DR O66602, SOD2_AQUAE; Q42612, SOD2_BRAJU; O08460, SOD2_HALME; DR P09224, SOD2_HALN1; Q03299, SOD2_HALSG; Q03301, SOD2_HALVO; DR Q43779, SOD2_LYCES; O49044, SOD2_MESCR; P28757, SOD2_ORYSA; DR P29428, SOD2_PICAB; P50059, SOD2_PLEBO; P50060, SOD3_PLEBO; DR P23345, SOD4_MAIZE; P23346, SOD5_MAIZE; Q59081, SODC_ACTAC; DR P24702, SODC_ACTPL; Q9SQL5, SODC_ANACO; P24704, SODC_ARATH; DR Q9Y8D9, SODC_ASPFU; Q12548, SODC_ASPJA; P00442, SODC_BOVIN; DR P09678, SODC_BRAOC; O73872, SODC_BRARE; P15453, SODC_BRUAB; DR P58645, SODC_BRUME; P41962, SODC_BRUPA; P34697, SODC_CAEEL; DR O59924, SODC_CANAL; O22373, SODC_CAPAN; P80174, SODC_CARCR; DR O65768, SODC_CARPA; P20379, SODC_CAUCR; P33431, SODC_CAVPO; DR P28755, SODC_CERCA; O46412, SODC_CEREL; P80566, SODC_CHICK; DR Q90023, SODC_CHVP1; Q07182, SODC_CHYAM; O42724, SODC_DEBHA; DR Q9RU48, SODC_DEIRA; P54407, SODC_DROBS; Q95081, SODC_DROMD; DR P00444, SODC_DROME; Q95079, SODC_DROMI; Q95085, SODC_DROOB; DR Q95087, SODC_DROPB; Q95088, SODC_DROPE; Q95086, SODC_DROPS; DR Q95095, SODC_DROTO; P10791, SODC_DROVI; P41973, SODC_DROWI; DR P53635, SODC_ECOLI; Q59448, SODC_FRATU; Q27666, SODC_HAECO; DR Q59452, SODC_HAEDU; P25842, SODC_HAEPA; P81926, SODC_HALRO; DR P00443, SODC_HORSE; P34936, SODC_HORVU; P00441, SODC_HUMAN; DR Q07796, SODC_IPOBA; P81036, SODC_LAMCR; P53637, SODC_LEGPN; DR P11428, SODC_MAIZE; P08228, SODC_MOUSE; Q9CBI6, SODC_MYCLE; DR Q9AGW2, SODC_MYCPA; P96278, SODC_MYCTU; P57005, SODC_NEIMA; DR Q59623, SODC_NEIMB; P07509, SODC_NEUCR; P27082, SODC_NICPL; DR P24705, SODC_NPVAC; O12933, SODC_NPVOP; P80740, SODC_OLEEU; DR P24706, SODC_ONCVO; O22668, SODC_PANGI; P83129, SODC_PAROL; DR Q51853, SODC_PASHA; Q59689, SODC_PASMU; O49073, SODC_PAUKA; DR Q02610, SODC_PEA ; P00446, SODC_PHOLE; P04178, SODC_PIG ; DR P24669, SODC_PINSY; P11418, SODC_PRIGL; P09212, SODC_RABIT; DR P23417, SODC_RANCA; P07632, SODC_RAT ; O68901, SODC_SALTY; DR Q01137, SODC_SCHMA; P28758, SODC_SCHPO; P09670, SODC_SHEEP; DR O04996, SODC_SOLCS; P22233, SODC_SPIOL; P81163, SODC_STRHE; DR P13926, SODC_XENLA; P03946, SODC_XIPGL; P00445, SODC_YEAST; DR O65174, SODC_ZANAE; P82902, SODD_DEBHA; P15107, SODD_XENLA; DR P41963, SODE_BRUPA; P34461, SODE_CAEEL; P41974, SODE_DIRIM; DR P51547, SODE_HAECO; P08294, SODE_HUMAN; O09164, SODE_MOUSE; DR Q07449, SODE_ONCVO; P41975, SODE_RABIT; Q08420, SODE_RAT ; DR P16026, SODE_SCHMA; Q9P9L3, SODF_ACIAM; Q9Y8H8, SODF_AERPE; DR O67470, SODF_AQUAE; Q9X6W9, SODF_AQUPY; P21276, SODF_ARATH; DR O15905, SODF_BABBO; P53638, SODF_BACFR; O35023, SODF_BACSU; DR P37369, SODF_BORPE; P53639, SODF_CAMCO; P53640, SODF_CAMJE; DR P19685, SODF_COXBU; P09157, SODF_ECOLI; P34107, SODF_ENTHI; DR Q9ZKE6, SODF_HELPJ; P43312, SODF_HELPY; P31108, SODF_LEGPN; DR P23744, SODF_METJ ; P18868, SODF_METTH; Q60036, SODF_METTM; DR P17670, SODF_MYCTU; P22302, SODF_NICPL; P81527, SODF_PASPI; DR P09213, SODF_PHOLE; P50061, SODF_PLEBO; P19665, SODF_PORGI; DR P53641, SODF_PSEAE; P09223, SODF_PSEPU; O93724, SODF_PYRAE; DR Q9XD74, SODF_RHIME; O30970, SODF_RHOCA; Q92HJ3, SODF_RICCN; DR Q9ZD15, SODF_RICPR; P40726, SODF_SALTY; P28759, SODF_SOYBN; DR O51917, SODF_STRCO; Q08713, SODF_SULAC; P80857, SODF_SULSO; DR P18655, SODF_SYNP7; P77968, SODF_SYNY3; P19666, SODF_TETPY; DR P77928, SODG_PSEPU; Q59094, SODM_ACICA; Q9P4T6, SODM_AGABI; DR P17550, SODM_ALCEU; O81235, SODM_ARATH; Q92450, SODM_ASPFU; DR P28760, SODM_BACCA; P00449, SODM_BACST; P54375, SODM_BACSU; DR O30563, SODM_BORBU; P53642, SODM_BORPE; P41976, SODM_BOVIN; DR P28761, SODM_BRAFL; P57286, SODM_BUCAI; Q8K9V4, SODM_BUCAP; DR P31161, SODM_CAEEL; O13401, SODM_CANAL; P54712, SODM_CANFA; DR O49066, SODM_CAPAN; P49114, SODM_CAVPO; O96347, SODM_CHAFE; DR Q9PKA0, SODM_CHLMU; Q9Z9C4, SODM_CHLPN; Q42684, SODM_CHLRE; DR O84296, SODM_CHLTR; P42821, SODM_CORDI; P11419, SODM_DESDE; DR Q00637, SODM_DROME; Q8X7B2, SODM_ECO57; P00448, SODM_ECOLI; DR P22799, SODM_ENTAE; P28762, SODM_EPTST; Q92429, SODM_GANMI; DR O30826, SODM_HAEDU; P43725, SODM_HAEIN; O08459, SODM_HALHI; DR Q03302, SODM_HALMA; P35017, SODM_HEVBR; Q9XS41, SODM_HORSE; DR P28524, SODM_HORVU; P04179, SODM_HUMAN; P50911, SODM_LACLA; DR Q92BR6, SODM_LISIN; P28763, SODM_LISIV; P28764, SODM_LISMO; DR P09233, SODM_MAIZE; P09671, SODM_MOUSE; P47201, SODM_MYCAV; DR P53643, SODM_MYCCE; P53644, SODM_MYCCH; Q59519, SODM_MYCFO; DR P80582, SODM_MYCHA; P46728, SODM_MYCIT; P50912, SODM_MYCKA; DR P13367, SODM_MYCLE; O86165, SODM_MYCLP; P53645, SODM_MYCMA; DR P53646, SODM_MYCMR; P53647, SODM_MYCPA; P53648, SODM_MYCPH; DR P50913, SODM_MYCSC; P53649, SODM_MYCSM; P53650, SODM_MYCSZ; DR Q9Y783, SODM_NEUCR; P11796, SODM_NICPL; P53651, SODM_NOCAS; DR P41981, SODM_ONCVO; Q43008, SODM_ORYSA; P28765, SODM_PALVU; DR P28766, SODM_PARCL; Q59679, SODM_PASHA; Q9CPN6, SODM_PASMU; DR P27084, SODM_PEA ; O75007, SODM_PENCH; P28767, SODM_PETMA; DR P28768, SODM_PIG ; P80293, SODM_PROFR; P53652, SODM_PSEAE; DR P77929, SODM_PSEPU; P41982, SODM_RABIT; P36215, SODM_RANCA; DR P07895, SODM_RAT ; Q8Z2V9, SODM_SALTI; P43019, SODM_SALTY; DR Q9UQX0, SODM_SCHPO; O54086, SODM_STRA3; O33603, SODM_STRAI; DR O33605, SODM_STRAY; O54210, SODM_STRCB; P80733, SODM_STRGR; DR O54233, SODM_STRIN; O33686, SODM_STRMT; P09738, SODM_STRMU; DR O54263, SODM_STROR; Q8K6Y8, SODM_STRP3; Q8P0D4, SODM_STRP8; DR O33756, SODM_STRPA; Q59949, SODM_STRPN; O54266, SODM_STRPO; DR P77957, SODM_STRPY; O33783, SODM_STRSL; P53653, SODM_THEAQ; DR P09214, SODM_THETH; P53654, SODM_XANCP; P00447, SODM_YEAST; DR P53655, SODM_YEREN; P41977, SODN_CAEEL; P41978, SODN_MAIZE; DR P80735, SODN_STRCO; P80732, SODN_STRGR; P80734, SODN_STRSO; DR P41979, SODO_MAIZE; O78310, SODP_ARATH; P14831, SODP_LYCES; DR P41980, SODP_MAIZE; O65198, SODP_MEDSA; P93407, SODP_ORYSA; DR P11964, SODP_PEA ; P10792, SODP_PETHY; P29427, SODP_PICAB; DR P81082, SODP_PINPS; P24707, SODP_PINSY; P36214, SODP_POPTM; DR O04997, SODP_SOLCS; P07505, SODP_SPIOL; O65199, SODP_VITVI; DR O65175, SODP_ZANAE; // ID 1.15.1.2 DE Superoxide reductase. AN Neelaredoxin. AN Desulfoferrodoxin. CA Reduced rubredoxin + superoxide + 2 H(+) = rubredoxin + H(2)O(2). CF Iron. CC -!- Formerly EC 1.18.96.1. DR O29903, SOR_ARCFU ; Q58151, SOR_METJA ; Q9V098, SOR_PYRAB ; DR P82385, SOR_PYRFU ; O58810, SOR_PYRHO ; Q9WZC6, SOR_THEMA ; // ID 1.16.1.1 DE Mercury (II) reductase. AN Mercuric reductase. CA Hg + NADP(+) + H(+) = Hg(2+) + NADPH. PR PROSITE; PDOC00073; DR Q52109, MERA_ACICA; P94188, MERA_ALCSP; P16171, MERA_BACSR; DR P94702, MERA_ENTAG; P00392, MERA_PSEAE; Q51772, MERA_PSEFL; DR P08662, MERA_SERMA; Q54465, MERA_SHEPU; P08332, MERA_SHIFL; DR P08663, MERA_STAEP; P30341, MERA_STRLI; P17239, MERA_THIFE; // ID 1.16.1.2 DE Diferric-transferrin reductase. AN Transferrin reductase. CA Transferrin-[Fe(2+)](2) + NAD(+) = transferrin-[Fe(3+)](2) + NADH. // ID 1.16.1.3 DE Aquacobalamin reductase. AN Aquocobalamin reductase. AN Vitamin B(12A) reductase. AN NADH-linked aquacobalamin reductase. AN B(12A) reductase. AN NADH:cob(III)alamin oxidoreductase. CA 2 cob(II)alamin + NAD(+) = 2 aquacob(III)alamin + NADH. CF Flavoprotein. CC -!- Formerly EC 1.6.99.8. DR P23486, FRE_ECOLI ; Q9L6L9, FRE_SALTY ; // ID 1.16.1.4 DE Cob(II)alamin reductase. AN Vitamin B(12R) reductase. AN B(12R) reductase. AN NADH:cob(II)alamin oxidoreductase. CA 2 cob(I)alamin + NAD(+) = 2 cob(II)alamin + NADH. CF Flavoprotein. CC -!- Formerly EC 1.6.99.9. // ID 1.16.1.5 DE Aquacobalamin reductase (NADPH). AN Aquacobalamin (reduced nicotinamide adenine dinucleotide phosphate) AN reductase. AN NADPH-linked aquacobalamin reductase. AN NADPH:aquacob(III)alamin oxidoreductase. CA 2 cob(II)alamin + NADP(+) = 2 aquacob(III)alamin + NADPH. CF Flavoprotein. CC -!- Acts on aquacob(III)alamin and hydroxycobalamin, but not on CC cyanocobalamin. CC -!- Formerly EC 1.6.99.11. // ID 1.16.1.6 DE Cyanocobalamin reductase (cyanide-eliminating). AN Cyanocobalamin reductase. AN Cyanocobalamin reductase (NADPH, cyanide-eliminating). AN Cyanocobalamin reductase (NADPH; CN-eliminating). AN NADPH:cyanocob(III)alamin oxidoreductase (cyanide-eliminating). CA Cob(I)alamin + cyanide + NADP(+) = cyanocob(III)alamin + NADPH. CF Flavoprotein. CC -!- Formerly EC 1.6.99.12. // ID 1.16.1.7 DE Ferric-chelate reductase. AN Ferric chelate reductase. AN Iron chelate reductase. AN NADH:Fe(3+)-EDTA reductase. AN NADH:Fe(3+) oxidoreductase. CA 2 Fe(2+) + NAD(+) = 2 Fe(3+) + NADH. CF FAD. CC -!- Involved in the transport of iron across plant plasma membranes. CC -!- Formerly EC 1.6.99.13. DR P32791, FRE1_YEAST; P36033, FRE2_YEAST; Q08905, FRE3_YEAST; DR P53746, FRE4_YEAST; Q08908, FRE5_YEAST; Q12473, FRE6_YEAST; DR Q12333, FRE7_YEAST; P78588, FREL_CANAL; Q04800, FRP1_SCHPO; // ID 1.16.3.1 DE Ferroxidase. AN Ceruloplasmin. CA 4 Fe(2+) + 4 H(+) + O(2) = 4 Fe(3+) + 2 H(2)O. CF Copper. PR PROSITE; PDOC00076; DR P00450, CERU_HUMAN; Q61147, CERU_MOUSE; P13635, CERU_RAT ; // ID 1.17.1.1 DE CDP-4-dehydro-6-deoxyglucose reductase. AN CDP-4-keto-6-deoxyglucose reductase. CA CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)(+) + H(2)O = CA CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H. CC -!- Two proteins are involved but no partial reaction has been observed CC in the presence of either alone. // ID 1.17.3.1 DE Pteridine oxidase. CA 2-amino-4-hydroxypteridine + O(2) = 2-amino-4,7-dihydroxypteridine + (?). CC -!- Does not act on hypoxanthine. CC -!- Different from EC 1.2.3.2. // ID 1.17.4.1 DE Ribonucleoside-diphosphate reductase. AN Ribonucleotide reductase. CA 2'-deoxyribonucleoside diphosphate + oxidized thioredoxin + H(2)O = CA ribonucleoside diphosphate + reduced thioredoxin. CF Iron; ATP. PR PROSITE; PDOC00084; PR PROSITE; PDOC00317; DR O66503, RIR1_AQUAE; P42491, RIR1_ASFB7; P26685, RIR1_ASFM2; DR P50620, RIR1_BACSU; P32282, RIR1_BPT4 ; P79732, RIR1_BRARE; DR P57276, RIR1_BUCAI; Q8K9W3, RIR1_BUCAP; Q03604, RIR1_CAEEL; DR Q9PL93, RIR1_CHLMU; Q9Z6S5, RIR1_CHLPN; O84834, RIR1_CHLTR; DR O61065, RIR1_CRYPV; P48591, RIR1_DROME; P03190, RIR1_EBV ; DR P00452, RIR1_ECOLI; P43754, RIR1_HAEIN; P16782, RIR1_HCMVA; DR Q9ZLF9, RIR1_HELPJ; P55982, RIR1_HELPY; P08543, RIR1_HSV11; DR P09853, RIR1_HSV23; P52343, RIR1_HSV6U; P50641, RIR1_HSV7J; DR P50646, RIR1_HSVBC; P50642, RIR1_HSVE4; P28846, RIR1_HSVEB; DR Q01037, RIR1_HSVSA; P23921, RIR1_HUMAN; P07742, RIR1_MOUSE; DR P47473, RIR1_MYCGE; Q9CBQ0, RIR1_MYCLE; P78027, RIR1_MYCPN; DR P50640, RIR1_MYCTU; Q9UW15, RIR1_NEUCR; P50648, RIR1_PLAF4; DR P50647, RIR1_PLAFG; P50643, RIR1_PRVKA; P37426, RIR1_SALTY; DR P36602, RIR1_SCHPO; P74240, RIR1_SYNY3; O83972, RIR1_TREPA; DR O15909, RIR1_TRYBB; P20503, RIR1_VACCC; P12848, RIR1_VACCV; DR P32984, RIR1_VARV ; P09248, RIR1_VZVD ; P21524, RIR1_YEAST; DR O67475, RIR2_AQUAE; P50651, RIR2_ARATH; P42492, RIR2_ASFB7; DR P26713, RIR2_ASFM2; Q9KFH7, RIR2_BACHD; P50621, RIR2_BACSU; DR P11156, RIR2_BPT4 ; P79733, RIR2_BRARE; P57275, RIR2_BUCAI; DR Q8K9W4, RIR2_BUCAP; P42170, RIR2_CAEEL; Q9PL92, RIR2_CHLMU; DR Q9Z6S4, RIR2_CHLPN; O84835, RIR2_CHLTR; P42521, RIR2_DICDI; DR P48592, RIR2_DROME; P03175, RIR2_EBV ; P00453, RIR2_ECOLI; DR P43755, RIR2_HAEIN; Q9ZKC3, RIR2_HELPJ; P55983, RIR2_HELPY; DR P10224, RIR2_HSV11; P06474, RIR2_HSV1K; P03174, RIR2_HSV23; DR Q01319, RIR2_HSVBC; P50644, RIR2_HSVE4; P28847, RIR2_HSVEB; DR Q01038, RIR2_HSVSA; P31350, RIR2_HUMAN; O46310, RIR2_LEIAM; DR Q60561, RIR2_MESAU; P11157, RIR2_MOUSE; Q9XC20, RIR2_MYCGA; DR P47471, RIR2_MYCGE; Q9CBQ2, RIR2_MYCLE; P75461, RIR2_MYCPN; DR Q10840, RIR2_MYCTU; Q9C167, RIR2_NEUCR; P50650, RIR2_PLAF4; DR P50649, RIR2_PLAFG; P50645, RIR2_PRVKA; Q9QTF2, RIR2_RSIV ; DR P37427, RIR2_SALTY; P36603, RIR2_SCHPO; P07201, RIR2_SPISO; DR P32209, RIR2_SPVKA; P49730, RIR2_TOBAC; O83092, RIR2_TREPA; DR O15910, RIR2_TRYBB; P20493, RIR2_VACCC; P29883, RIR2_VACCP; DR P11158, RIR2_VACCV; P33799, RIR2_VARV ; P09247, RIR2_VZVD ; DR P09938, RIR2_YEAST; P39452, RIR3_ECOLI; Q08698, RIR3_SALTY; DR P21672, RIR3_YEAST; P37146, RIR4_ECOLI; P17424, RIR4_SALTY; DR P49723, RIR4_YEAST; // ID 1.17.4.2 DE Ribonucleoside-triphosphate reductase. AN Ribonucleotide reductase. CA 2'-deoxyribonucleoside triphosphate + oxidized thioredoxin + H(2)O = CA ribonucleoside triphosphate + reduced thioredoxin. CF Cobalt; ATP. PR PROSITE; PDOC00665; DR P07071, NRDD_BPT4 ; P28903, NRDD_ECOLI; P43752, NRDD_HAEIN; DR Q9L646, NRDD_SALTY; O64240, VG50_BPMD2; Q05262, VG50_BPML5; // ID 1.17.99.1 DE 4-cresol dehydrogenase (hydroxylating). AN p-cresol methylhydroxylase. AN p-cresol-(acceptor) oxidoreductase (hydroxylating). CA 4-cresol + acceptor + H(2)O = 4-hydroxybenzaldehyde + reduced CA acceptor. CF FAD. CC -!- Phenazine methosulfate can act as acceptor. CC -!- A quinone methide is probably formed as intermediate. CC -!- The first hydroxylation forms 4-hydroxybenzyl alcohol; a second CC hydroxylation converts this into 4-hydroxybenzaldehyde. DR P09788, DH4C_PSEPU; // ID 1.17.99.2 DE Ethylbenzene hydroxylase. AN Ethylbenzene dehydrogenase. CA Ethylbenzene + H(2)O + acceptor = (S)-1-phenylethanol + reduced CA acceptor. CF Molybdopterin; Iron-sulfur; Heme. CC -!- Involved in the anaerobic catabolism of ethylbenzene by CC denitrifying bacteria. CC -!- Ethylbenzene is the preferred substrate; the enzyme from some CC strains oxidizes propylbenzene, 1-ethyl-4-fluorobenzene, 3- CC methylpent-2-ene and ethylidenecyclohexane. CC -!- Toluene is not oxidized. CC -!- p-Benzoquinone or ferrocenium can act as electron acceptor. // ID 1.18.1.1 DE Rubredoxin--NAD(+) reductase. AN Rubredoxin reductase. AN Rubredoxin-nicotinamide adenine dinucleotide reductase. AN Dihydronicotinamide adenine dinucleotide-rubredoxin reductase. AN Reduced nicotinamide adenine dinucleotide-rubredoxin reductase. AN NADH-rubredoxin reductase. AN Rubredoxin-NAD reductase. AN NADH-rubredoxin oxidoreductase. CA Reduced rubredoxin + NAD(+) = oxidized rubredoxin + NADH. CF FAD; Iron. CC -!- The enzyme from Clostridium acetobutylicum reduces rubredoxin, CC ferricyanide and dichlorophenolindophenol, but not ferredoxin CC or flavodoxin. CC -!- The reaction does not occur when NADPH is substituted for NADH. CC -!- Formerly EC 1.6.7.2. DR P42454, RURE_ACICA; P17052, RURE_PSEOL; // ID 1.18.1.2 DE Ferredoxin--NADP(+) reductase. AN Adrenodoxin reductase. CA Reduced ferredoxin + NADP(+) = oxidized ferredoxin + NADPH. CF FAD. CC -!- Also acts on adrenodoxin. CC -!- Formerly EC 1.6.7.1, EC 1.6.99.4 and EC 1.6.99.10. DR P08165, ADRO_BOVIN; Q9V3T9, ADRO_DROME; P22570, ADRO_HUMAN; DR Q61578, ADRO_MOUSE; P56522, ADRO_RAT ; P82861, ADRO_SALFO; DR P21890, FENR_ANASO; P58558, FENR_ANASP; Q44549, FENR_ANAVA; DR Q44532, FENR_AZOVI; P57641, FENR_BUCAI; Q9Z615, FENR_BUCAP; DR P53991, FENR_CHLRE; Q00598, FENR_CYAPA; P28861, FENR_ECOLI; DR P41343, FENR_MESCR; P41344, FENR_ORYSA; P10933, FENR_PEA ; DR P28901, FENR_SHIFL; P00455, FENR_SPIOL; P00454, FENR_SPISP; DR Q93RE3, FENR_SYNEL; P31973, FENR_SYNP2; Q55318, FENR_SYNY3; DR O04977, FENR_TOBAC; P41346, FENR_VICFA; P41345, FENS_ORYSA; DR Q41014, FENS_PEA ; O04397, FENS_TOBAC; O23877, FENT_ORYSA; DR O32886, FPRA_MYCLE; O05783, FPRA_MYCTU; O33064, FPRB_MYCLE; DR Q10547, FPRB_MYCTU; // ID 1.18.1.3 DE Ferredoxin--NAD(+) reductase. CA Reduced ferredoxin + NAD(+) = oxidized ferredoxin + NADH. DR Q07946, BEDA_PSEPU; P07771, BENC_ACICA; P08087, BNZD_PSEPU; DR P37337, BPHG_BURCE; Q51603, CBDC_BURCE; P24134, FENR_STRGR; DR P77650, HCAD_ECOLI; Q52126, NDOR_PSEPU; Q03304, TMOF_PSEME; DR P13452, TODA_PSEPU; P21394, XYLA_PSEPU; P23101, XYLZ_PSEPU; // ID 1.18.1.4 DE Rubredoxin--NADP(+) reductase. AN Rubredoxin-nicotinamide adenine dinucleotide (phosphate) reductase. AN Rubredoxin-nicotinamide adenine. AN Dinucleotide phosphate reductase. AN NAD(P)-rubredoxin oxidoreductase. AN NAD(P)H-rubredoxin oxidoreductase. CA Reduced rubredoxin + NAD(P)(+) = oxidized rubredoxin + NAD(P)H. CF FAD. CC -!- The enzyme reduces a number of electron carriers, including CC benzyl viologen, menadione and 2,6-dichloroindophenol, but CC rubredoxin is the most efficient. CC -!- Ferredoxin is not utilized. // ID 1.18.3.1 DE Transferred entry: 1.12.7.2. // ID 1.18.6.1 DE Nitrogenase. CA 8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP = 8 oxidized ferredoxin + CA 2 NH(3) + 16 ADP + 16 phosphate. CF Iron-sulfur; Molybdenum or Vanadium. CC -!- Acetylene can also act as acceptor. CC -!- In the absence of other acceptors H(+) is reduced to H(2). PR PROSITE; PDOC00085; PR PROSITE; PDOC00580; DR P16266, ANFD_AZOVI; Q46082, ANFD_CLOHU; O68955, ANFD_HELGE; DR Q07933, ANFD_RHOCA; O68946, ANFG_AZOMA; O68943, ANFG_AZOPA; DR P16268, ANFG_AZOVI; Q46083, ANFG_CLOHU; Q46244, ANFG_CLOPA; DR Q07934, ANFG_RHOCA; O68940, ANFG_RHORU; P16267, ANFK_AZOVI; DR Q46084, ANFK_CLOHU; Q07935, ANFK_RHOCA; P22548, NIF4_CLOPA; DR Q44045, NIFD_ALCFA; P33177, NIFD_ANASL; P00464, NIFD_ANASP; DR P25313, NIFD_AZOBR; P07328, NIFD_AZOVI; P06121, NIFD_BRAJA; DR P06120, NIFD_BRASP; P00467, NIFD_CLOPA; O07642, NIFD_CYAA5; DR Q02452, NIFD_FRAAL; P77874, NIFD_HERSE; P00466, NIFD_KLEPN; DR P55170, NIFD_METBA; P51605, NIFD_METIV; P71526, NIFD_METMP; DR O27605, NIFD_METTH; P20620, NIFD_METTL; Q50788, NIFD_METTM; DR P52337, NIFD_NOSCO; Q00239, NIFD_PLEBO; P06769, NIFD_RHICP; DR P00465, NIFD_RHILT; P19066, NIFD_RHISN; P08717, NIFD_RHOCA; DR Q55029, NIFD_SYNP8; P06662, NIFD_THIFE; Q9ZIE4, NIFH_ACEDI; DR Q44044, NIFH_ALCFA; P33178, NIFH_ANASL; P17303, NIFH_AZOBR; DR P06117, NIFH_BRAJA; P00463, NIFH_BRASP; Q8KC92, NIFH_CHLTE; DR Q97ME5, NIFH_CLOAB; Q59270, NIFH_CLOCB; O07641, NIFH_CYAA5; DR P71156, NIFH_DESGI; P26249, NIFH_ENTAG; P08925, NIFH_FRAAL; DR Q47922, NIFH_FRASE; P46034, NIFH_FRASP; P77873, NIFH_HERSE; DR P00458, NIFH_KLEPN; Q58289, NIFH_METJA; Q50218, NIFH_METMP; DR Q50785, NIFH_METTM; P06119, NIFH_METVO; P26250, NIFH_NOSCO; DR Q09158, NIFH_NOSMU; Q51296, NIFH_NOSS6; P52336, NIFH_NOSSN; DR Q00240, NIFH_PLEBO; P00462, NIFH_RHIET; P20623, NIFH_RHILE; DR Q98AP7, NIFH_RHILO; P00461, NIFH_RHILT; P00460, NIFH_RHIME; DR P19068, NIFH_RHISN; P22921, NIFH_RHORU; O31183, NIFH_RHOSH; DR Q55028, NIFH_SYNP8; P06661, NIFH_THIFE; O34106, NIFH_TRIS1; DR P26254, NIFH_TRITH; P00468, NIFK_ANASP; P25314, NIFK_AZOBR; DR P07329, NIFK_AZOVI; P20621, NIFK_BRAJA; P06122, NIFK_BRASP; DR P11347, NIFK_CLOPA; O07643, NIFK_CYAA5; Q57118, NIFK_FRAAL; DR P77875, NIFK_HERSE; P09772, NIFK_KLEPN; P51754, NIFK_METBA; DR P71527, NIFK_METMP; O27606, NIFK_METTH; P20622, NIFK_METTL; DR P95296, NIFK_METTM; P19067, NIFK_RHISN; Q55030, NIFK_SYNP8; DR P15052, NIFK_THIFE; P00457, NIH1_ANASP; Q43886, NIH1_ANAVA; DR P26251, NIH1_AZOCA; P26248, NIH1_AZOCH; P00459, NIH1_AZOVI; DR P00456, NIH1_CLOPA; Q47917, NIH1_MASLA; P54799, NIH1_METBA; DR P51602, NIH1_METIV; O27602, NIH1_METTH; P25767, NIH1_METTL; DR Q9AKT8, NIH1_PAEAZ; P08718, NIH1_RHOCA; O30577, NIH2_ANASP; DR Q44484, NIH2_ANAVA; P26252, NIH2_AZOCA; P06118, NIH2_AZOCH; DR P15335, NIH2_AZOVI; P09552, NIH2_CLOPA; Q47921, NIH2_MASLA; DR P54800, NIH2_METBA; P08624, NIH2_METIV; O26739, NIH2_METTH; DR P08625, NIH2_METTL; Q9AKT4, NIH2_PAEAZ; Q07942, NIH2_RHOCA; DR P16269, NIH3_AZOVI; P09553, NIH3_CLOPA; P09554, NIH5_CLOPA; DR P09555, NIH6_CLOPA; P15332, VNFD_AZOCH; O68953, VNFD_AZOPA; DR O68954, VNFD_AZOSA; P16855, VNFD_AZOVI; P15333, VNFG_AZOCH; DR O68951, VNFG_AZOSA; P16857, VNFG_AZOVI; Q57302, VNFK_ANAVA; DR P15334, VNFK_AZOCH; O68949, VNFK_AZOPA; O68952, VNFK_AZOSA; DR P16856, VNFK_AZOVI; // ID 1.18.96.1 DE Transferred entry: 1.15.1.2. // ID 1.18.99.1 DE Transferred entry: 1.12.7.2. // ID 1.19.6.1 DE Nitrogenase (flavodoxin). CA 8 reduced flavodoxin(HQ) + 8 H(+) + N(2) + 16 ATP = 8 oxidized CA flavodoxin(SQ) + 2 NH(3) + 16 ADP + 16 phosphate. CF Iron-sulfur; Molybdenum. // ID 1.20.1.1 DE Phosphonate dehydrogenase. AN NAD:phosphite oxidoreductase. AN NAD-dependent phosphite dehydrogenas. AN Phosphite dehydrogenase. CA Phosphonate + NAD(+) + H(2)O = phosphate + NADH. CC -!- NADP(+) is a poor substitute for NAD(+) in the enzyme from CC Pseudomonas stutzeri WM88. PR PROSITE; PDOC00063; DR O69054, PTXD_PSEST; // ID 1.20.4.1 DE Arsenate reductase (glutaredoxin). CA Arsenate + reduced glutaredoxin = arsenite + oxidized glutaredoxin. CF Molybdenum. CC -!- The glutaredoxins catalyze glutathione-disulfide oxidoreductions CC and have a redox-active disulfide/dithiol in the active site CC (-Cys-Pro-Tyr-Cys-) that forms a disulfide bond in the oxidized CC form. CC -!- Glutaredoxins have a binding site for glutathione, which is CC required to reduce them to the dithiol form. CC -!- Thioredoxins reduced by NADPH and thioredoxin reductase can act as CC alternative substrates. CC -!- The enzyme is part of a system for detoxifying arsenate. CC -!- Although the arsenite formed is more toxic than arsenate, it can CC be extruded from some bacteria by EC 3.6.3.16. CC -!- In other organisms, arsenite can be methylated by EC 2.1.1.137 in CC a pathway to non-toxic organoarsenical compounds. CC -!- Formerly: EC 1.97.1.5. DR P08692, ARC1_ECOLI; P52147, ARC2_ECOLI; O50595, ARSC_ACIMU; DR Q9K8K8, ARSC_BACHD; P45947, ARSC_BACSU; P37311, ARSC_ECOLI; DR P44589, ARSC_HAEIN; P95354, ARSC_NEIGO; Q9JQU0, ARSC_NEIMA; DR P30330, ARSC_STAAN; Q01257, ARSC_STAXY; P74984, ARSC_YEREN; DR P52136, YFJU_ECOLI; // ID 1.20.4.2 DE Methylarsonate reductase. AN MMA(V) reductase. CA Methylarsonate + 2 glutathione = methylarsonite + oxidized glutathione. CC -!- The product, Me-As(OH)2 (methylarsonous acid), is biologically CC methylated by EC 2.1.1.138, to form cacodylic acid (dimethylarsinic CC acid). CC -!- Formerly: EC 1.97.1.7. // ID 1.20.98.1 DE Arsenate reductase (azurin). AN Arsenite oxidase. CA Arsenite + H(2)O + azurin(ox) = arsenate + azurin(red). CF Molybdopterin; Molybdenum; Iron-sulfur. CC -!- The enzyme also uses a c-type cytochrome or O(2) as acceptors. // ID 1.20.99.1 DE Arsenate reductase (donor). CA Arsenite + acceptor = arsenate + reduced acceptor. CC -!- Benzyl viologen can act as an acceptor. CC -!- Unlike EC 1.20.4.1 reduced glutaredoxin cannot serve as a CC reductant. CC -!- Formerly EC 1.97.1.6. // ID 1.21.3.1 DE Isopenicillin-N synthase. CA N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O(2) = CA isopenicillin N + 2 H(2)O. CC -!- Forms part of the penicillin biosynthesis pathway. DR P05189, IPNS_CEPAC; P05326, IPNS_EMENI; P16020, IPNS_FLASS; DR Q48739, IPNS_LYSLA; P27744, IPNS_NOCLA; P08703, IPNS_PENCH; DR P10621, IPNS_STRCL; Q53932, IPNS_STRCT; Q54243, IPNS_STRGR; DR P18286, IPNS_STRJU; P12438, IPNS_STRLP; // ID 1.21.3.2 DE Columbamine oxidase. AN Berberine synthase. CA 2 columbamine + O(2) = 2 berberine + 2 H(2)O. CF Iron. CC -!- Oxidation of the O-methoxyphenol structure forms the methylenedioxy CC group of berberine. CC -!- Formerly EC 1.1.3.26. // ID 1.21.3.3 DE Reticuline oxidase. AN Berberine-bridge-forming enzyme. AN Berberine bridge enzyme. AN Tetrahydroprotoberberine synthase. CA (S)-reticuline + O(2) = (S)-scoulerine + H(2)O(2). CF FAD. CC -!- The product of the reaction, (S)-scoulerine, is a precursor of CC protopine, protoberberine and benzophenanthridine alkaloid CC biosynthesis in plants. CC -!- Acts on (S)-reticuline and related compounds, converting the N- CC methyl group into the methylene bridge (`berberine bridge') of (S)- CC tetrahydroprotoberberines. CC -!- Formerly EC 1.5.3.9. PR PROSITE; PDOC00674; DR P30986, RETO_ESCCA; P93479, RETO_PAPSO; // ID 1.21.3.4 DE Sulochrin oxidase [(+)-bisdechlorogeodin-forming]. AN Sulochrin oxidase. CA 2 sulochrin + O(2) = 2 (+)-bisdechlorogeodin + 2 H(2)O. CC -!- Also acts on several diphenols and phenylenediamines, but has low CC affinity for these substrates. CC -!- Involved in the biosynthesis of mould metabolites related to the CC antibiotic griseofulvin. CC -!- Formerly EC 1.10.3.7. // ID 1.21.3.5 DE Sulochrin oxidase [(-)-bisdechlorogeodin-forming]. AN Sulochrin oxidase. CA 2 sulochrin + O(2) = 2 (-)-bisdechlorogeodin + 2 H(2)O. CC -!- Also acts on several diphenols and phenylenediamines, but has low CC affinity for these substrates. CC -!- Involved in the biosynthesis of mould metabolites related to the CC antibiotic griseofulvin. CC -!- Formerly EC 1.10.3.8. // ID 1.21.4.1 DE D-proline reductase (dithiol). CA 5-aminopentanoate + lipoate = D-proline + dihydrolipoate. CF Pyruvate. CC -!- Other dithiols can function as reducing agents. CC -!- Formerly EC 1.4.1.6 an EC 1.4.4.1. // ID 1.21.3.6 DE Sulochrin oxidase [(-)-bisdechlorogeodin-forming]. AN Sulochrin oxidase. CA 2 sulochrin + O(2) = 2 (-)-bisdechlorogeodin + 2 H(2)O. CC -!- Also acts on several diphenols and phenylenediamines, but has low CC affinity for these substrates. CC -!- Involved in the biosynthesis of mould metabolites related to the CC antibiotic griseofulvin. CC -!- Formerly EC 1.10.3.8. // ID 1.21.99.1 DE Beta-cyclopiazonate dehydrogenase. AN Beta-cyclopiazonate oxidocyclase. AN Beta-cyclopiazonic oxidocyclase. CA Beta-cyclopiazonate + acceptor = alpha-cyclopiazonate + reduced CA acceptor. CF FAD. CC -!- Cytochrome c and various dyes can act as acceptor. CC -!- Cyclopiazonate is a microbial toxin. CC -!- Formerly EC 1.3.99.9. // ID 1.97.1.1 DE Chlorate reductase. CA AH(2) + chlorate = A + H(2)O + chlorite. CC -!- Flavins or benzylviologen can act as acceptor. // ID 1.97.1.2 DE Pyrogallol hydroxyltransferase. AN Transhydroxylase. CA 1,2,3,5-tetrahydroxybenzene + 1,2,3-trihydroxybenzene = CA 1,3,5-trihydroxybenzene + 1,2,3,5-tetrahydroxybenzene. CF Molybdenum. CC -!- 1,2,3,5-tetrahydroxybenzene acts as a co-substrate for the conversion CC of pyrogallol into phloroglucinol, and for a number of similar CC isomerizations. CC -!- The enzyme is provisionally listed here, but might be considered as CC the basis for a new class in the transferases, analogous to the CC aminotransferases. DR P80563, PGTL_PELAC; P80564, PGTS_PELAC; // ID 1.97.1.3 DE Sulfur reductase. CA Reduction of elemental sulfur or polysulfide to H(2)S. CC -!- Sulfur can be reduced with hydrogen as donor in the presence of CC hydrogenase, or by photochemical reduction in the presence of CC phenosafranin. // ID 1.97.1.4 DE Formate acetyltransferase activating enzyme. AN [Pyruvate formate-lyase]-activating enzyme. AN PFL activase. CA S-adenosyl-L-methionine + dihydroflavodoxin + [formate CA acetyltransferase]-glycine = 5'-deoxyadenosine + methionine + CA flavodoxin + [formate acetyltransferase]-glycine-2-yl radical. CF Iron-sulfur. CC -!- A single glycine residue in EC 2.3.1.54 is oxidized to the CC corresponding radical by transfer of H from its CH(2) into AdoMet CC with concomitant cleavage of the latter. CC -!- The flavodoxin may be in the partially reduced, radical form. PR PROSITE; PDOC00834; DR P07075, NRDG_BPT4 ; P39329, NRDG_ECOLI; P45080, NRDG_HAEIN; DR Q9CM94, NRDG_PASMU; Q8Z138, NRDG_SALTI; Q9L645, NRDG_SALTY; DR Q9KM76, NRDG_VIBCH; Q46267, PFLA_CLOPA; P09374, PFLA_ECOLI; DR P43751, PFLA_HAEIN; Q9X767, PFLA_LISMO; O68575, PFLA_STRMU; DR P32675, PFLC_ECOLI; P75794, PFLE_ECOLI; // ID 1.97.1.5 DE Transferred entry: 1.20.4.1. // ID 1.97.1.6 DE Transferred entry: 1.20.99.1. // ID 1.97.1.7 DE Transferred entry: 1.20.4.2. // ID 1.97.1.8 DE Tetrachloroethene reductive dehalogenase. AN Tetrachloroethene reductase. CA Trichloroethene + chloride + acceptor = tetrachloroethene + CA reduced acceptor. CF Iron-sulfur. CC -!- This enzyme allows the common pollutant tetrachloroethene to CC support bacterial growth and is responsible for disposal of a CC number of chlorinated hydrocarbons by this organism. CC -!- The reaction occurs in the reverse direction. CC -!- The enzyme also reduces trichloroethene to dichloroethene. CC -!- Although the physiological reductant is unknown, the supply of CC reductant in some organisms is via reduced menaquinone, itself CC formed from molecular hydrogen, via EC 1.12.99.3. CC -!- Methyl viologen can act as electron donor. // ID 2.1.1.1 DE Nicotinamide N-methyltransferase. CA S-adenosyl-L-methionine + nicotinamide = S-adenosyl-L-homocysteine + CA 1-methylnicotinamide. PR PROSITE; PDOC00844; DR P40261, NNMT_HUMAN; O55239, NNMT_MOUSE; // ID 2.1.1.2 DE Guanidinoacetate N-methyltransferase. CA S-adenosyl-L-methionine + guanidoacetate = S-adenosyl-L-homocysteine + CA creatine. DI Guanidinoacetate methyltransferase deficiency; MIM:601240. DR Q14353, GAMT_HUMAN; O35969, GAMT_MOUSE; P10868, GAMT_RAT ; // ID 2.1.1.3 DE Thetin--homocysteine S-methyltransferase. CA Dimethylsulfonioacetate + L-homocysteine = S-methylthioglycolate + CA L-methionine. // ID 2.1.1.4 DE Acetylserotonin O-methyltransferase. AN Hydroxyindole O-methyltransferase. CA S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L- CA homocysteine + N-acetyl-5-methoxytryptamine. CC -!- Some other hydroxyindoles also act as acceptor, more slowly. DR P10950, HIOM_BOVIN; Q92056, HIOM_CHICK; P46597, HIOM_HUMAN; // ID 2.1.1.5 DE Betaine--homocysteine S-methyltransferase. CA Trimethylammonioacetate + L-homocysteine = dimethylglycine + CA L-methionine. CF Zinc. DR Q93088, BHMT_HUMAN; O35490, BHMT_MOUSE; Q95332, BHMT_PIG ; DR O09171, BHMT_RAT ; // ID 2.1.1.6 DE Catechol O-methyltransferase. CA S-adenosyl-L-methionine + catechol = S-adenosyl-L-homocysteine + CA guaiacol. CC -!- The mammalian enzymes act more rapidly on catecholamines such as CC adrenaline or noradrenaline than on catechols. DR P21964, COMT_HUMAN; O88587, COMT_MOUSE; Q99028, COMT_PIG ; DR P22734, COMT_RAT ; // ID 2.1.1.7 DE Nicotinate N-methyltransferase. CA S-adenosyl-L-methionine + nicotinate = S-adenosyl-L-homocysteine + CA 1-methylnicotinate. // ID 2.1.1.8 DE Histamine N-methyltransferase. CA S-adenosyl-L-methionine + histamine = S-adenosyl-L-homocysteine + CA N(T)-methylhistamine. DR P50135, HMT_HUMAN ; Q01984, HMT_RAT ; // ID 2.1.1.9 DE Thiol S-methyltransferase. CA S-adenosyl-L-methionine + a thiol = S-adenosyl-L-homocysteine + CA a thioether. CC -!- H(2)S and a variety of alkyl, aryl and heterocyclic thiols and CC hydroxy thiols can act as acceptors. // ID 2.1.1.10 DE Homocysteine S-methyltransferase. CA S-adenosyl-L-methionine + L-homocysteine = S-adenosyl-L-homocysteine + CA L-methionine. CC -!- The bacterial enzyme uses S-methylmethionine as donor more actively CC than S-adenosyl-L-methionine. DR Q47690, MMUM_ECOLI; // ID 2.1.1.11 DE Magnesium-protoporphyrin O-methyltransferase. CA S-adenosyl-L-methionine + magnesium protoporphyrin = S-adenosyl-L- CA homocysteine + magnesium protoporphyrin monomethyl ester. DR P26236, BCHM_RHOCA; Q55467, CHLM_SYNY3; // ID 2.1.1.12 DE Methionine S-methyltransferase. CA S-adenosyl-L-methionine + L-methionine = S-adenosyl-L-homocysteine + CA S-methyl-L-methionine. CF Zinc or Manganese. // ID 2.1.1.13 DE 5-methyltetrahydrofolate--homocysteine S-methyltransferase. AN Methionine synthase. AN Tetrahydropteroylglutamate methyltransferase. CA 5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + CA L-methionine. CF Cobalamin. CC -!- Acts on monoglutamate or triglutamate derivatives. CC -!- The bacterial enzyme requires S-adenosyl-L-methionine and reduced CC FAD. DR Q09582, METH_CAEEL; P13009, METH_ECOLI; Q99707, METH_HUMAN; DR Q49775, METH_MYCLE; O33259, METH_MYCTU; O33465, METH_PSEPU; DR P37586, METH_SALTY; Q55786, METH_SYNY3; // ID 2.1.1.14 DE 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase. AN Methionine synthase. AN Tetrahydropteroyltriglutamate methyltransferase. CA 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = CA tetrahydropteroyltri-L-glutamate + L-methionine. CC -!- Requires phosphate. CC -!- The enzyme from E.coli also requires a reducing system. DR Q9F187, METE_ALCEU; O67606, METE_AQUAE; O50008, METE_ARATH; DR Q9KFP1, METE_BACHD; P80877, METE_BACSU; Q8G651, METE_BIFLO; DR Q9AMV8, METE_BRAJA; P57142, METE_BUCAI; Q8KA71, METE_BUCAP; DR Q89B24, METE_BUCBP; Q9PN94, METE_CAMJE; P82610, METE_CANAL; DR Q42699, METE_CATRO; Q9AAW1, METE_CAUCR; Q39586, METE_CHLRE; DR Q8FQB2, METE_COREF; Q8NRB3, METE_CORGL; Q8X8L5, METE_ECO57; DR Q8FBM1, METE_ECOL6; P25665, METE_ECOLI; P45331, METE_HAEIN; DR Q9CG55, METE_LACLA; Q92AX9, METE_LISIN; Q8Y6K3, METE_LISMO; DR P93263, METE_MESCR; O05564, METE_MYCLE; O06584, METE_MYCTU; DR Q9JUT6, METE_NEIMA; Q9JZQ2, METE_NEIMB; P57843, METE_PASMU; DR P57703, METE_PSEAE; Q8XS05, METE_RALSO; Q98A73, METE_RHILO; DR Q8Z3B6, METE_SALTI; Q9L6N1, METE_SALTY; Q9UT19, METE_SCHPO; DR Q8EIM0, METE_SHEON; Q42662, METE_SOLSC; Q99WM1, METE_STAAM; DR Q8NY94, METE_STAAW; Q8CMP5, METE_STAEP; Q8E2V9, METE_STRA3; DR Q93J59, METE_STRCO; Q8CWX6, METE_STRMU; Q97S31, METE_STRPN; DR Q8DQT2, METE_STRR6; Q8DJY0, METE_SYNEL; Q9X112, METE_THEMA; DR Q9KRD8, METE_VIBCH; Q8KRG6, METE_VIBHA; Q87NA1, METE_VIBPA; DR Q8CWK1, METE_VIBVU; Q9PB72, METE_XYLFA; Q87BY8, METE_XYLFT; DR P05694, METE_YEAST; Q8ZAL3, METE_YERPE; // ID 2.1.1.15 DE Fatty-acid O-methyltransferase. CA S-adenosyl-L-methionine + a fatty acid = S-adenosyl-L-homocysteine + CA a fatty acid methyl ester. CC -!- Oleic acid is the most effective fatty acid acceptor. // ID 2.1.1.16 DE Methylene-fatty-acyl-phospholipid synthase. AN Unsaturated-phospholipid methyltransferase. AN Cyclopropane synthetase. CA S-adenosyl-L-methionine + phospholipid olefinic fatty acid = CA S-adenosyl-L-homocysteine + phospholipid methylene fatty acid. CC -!- The enzyme transfers a methyl group to the 10-position of a delta(9)- CC olefinic acyl chain in phosphatidylglycerol, phosphatidylinositol, CC or, more slowly, phosphatidylethanolamine; subsequent proton CC transfer produces a 10-methylene group (cf. EC 2.1.1.79). DR O74827, CHO1_SCHPO; P05375, PEM2_YEAST; // ID 2.1.1.17 DE Phosphatidylethanolamine N-methyltransferase. CA S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L- CA homocysteine + phosphatidyl-N-methylethanolamine. DR O74787, CHO2_SCHPO; P05374, PEM1_YEAST; Q9UBM1, PEMT_HUMAN; DR Q61907, PEMT_MOUSE; Q08388, PEMT_RAT ; Q05197, PMTA_RHOSH; // ID 2.1.1.18 DE Polysaccharide O-methyltransferase. CA S-adenosyl-L-methionine + 1,4-alpha-D-glucooligosaccharide = CA S-adenosyl-L-homocysteine + oligosaccharide containing 6-methyl-D- CA glucose units. // ID 2.1.1.19 DE Trimethylsulfonium--tetrahydrofolate N-methyltransferase. CA Trimethylsulfonium + tetrahydrofolate = dimethylsulfide + CA 5-methyltetrahydrofolate. // ID 2.1.1.20 DE Glycine N-methyltransferase. CA S-adenosyl-L-methionine + glycine = S-adenosyl-L-homocysteine + CA sarcosine. DR Q14749, GLMT_HUMAN; Q29555, GLMT_PIG ; Q29513, GLMT_RABIT; DR P13255, GLMT_RAT ; // ID 2.1.1.21 DE Methylamine--glutamate N-methyltransferase. AN N-methylglutamate synthase. CA Methylamine + L-glutamate = NH(3) + N-methyl-L-glutamate. // ID 2.1.1.22 DE Carnosine N-methyltransferase. CA S-adenosyl-L-methionine + carnosine = S-adenosyl-L-homocysteine + CA anserine. // ID 2.1.1.23 DE Transferred entry: 2.1.1.124, 2.1.1.125 and 2.1.1.126. // ID 2.1.1.24 DE Transferred entry: 2.1.1.77, 2.1.1.80 and 2.1.1.100. // ID 2.1.1.25 DE Phenol O-methyltransferase. CA S-adenosyl-L-methionine + phenol = S-adenosyl-L-homocysteine + anisole. CC -!- Acts on a wide variety of simple alkyl-, methoxy- and halo-phenols. // ID 2.1.1.26 DE Iodophenol O-methyltransferase. CA S-adenosyl-L-methionine + 2-iodophenol = S-adenosyl-L-homocysteine + CA 2-iodophenol methyl ether. // ID 2.1.1.27 DE Tyramine N-methyltransferase. CA S-adenosyl-L-methionine + tyramine = S-adenosyl-L-homocysteine + CA N-methyltyramine. CC -!- Has some activity on phenylethylamine analogs. // ID 2.1.1.28 DE Phenylethanolamine N-methyltransferase. AN Noradrenalin N-methyltransferase. CA S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L- CA homocysteine + N-methylphenylethanolamine. CC -!- Acts on various phenylethanolamines; converts noradrenalin into CC adrenalin. PR PROSITE; PDOC00844; DR P10938, PNMT_BOVIN; P11086, PNMT_HUMAN; P40935, PNMT_MOUSE; DR P10937, PNMT_RAT ; // ID 2.1.1.29 DE tRNA (cytosine-5-)-methyltransferase. CA S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA CA containing 5-methylcytosine. // ID 2.1.1.30 DE Deleted entry. // ID 2.1.1.31 DE tRNA (guanine-N(1)-)-methyltransferase. CA S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA CA containing N(1)-methylguanine. DR Q43963, TRMD_ACICA; Q8UBZ7, TRMD_AGRT5; Q8YQF1, TRMD_ANASP; DR O67463, TRMD_AQUAE; Q9KA15, TRMD_BACHD; O31741, TRMD_BACSU; DR O51641, TRMD_BORBU; Q8YJD7, TRMD_BRUME; P57476, TRMD_BUCAI; DR Q8K9F4, TRMD_BUCAP; P59518, TRMD_BUCBP; Q9PPJ4, TRMD_CAMJE; DR Q9ABM9, TRMD_CAUCR; Q9PL12, TRMD_CHLMU; Q9Z964, TRMD_CHLPN; DR Q8KD90, TRMD_CHLTE; O84030, TRMD_CHLTR; Q97I94, TRMD_CLOAB; DR Q8XJP7, TRMD_CLOPE; Q8NNX7, TRMD_CORGL; Q9RSW0, TRMD_DEIRA; DR P07020, TRMD_ECOLI; Q8R5Y4, TRMD_FUSNN; P43912, TRMD_HAEIN; DR Q9ZK66, TRMD_HELPJ; O25766, TRMD_HELPY; Q9CFB7, TRMD_LACLA; DR Q92AL6, TRMD_LISIN; Q8Y6A3, TRMD_LISMO; Q9RDV3, TRMD_MYCGA; DR P47683, TRMD_MYCGE; O33017, TRMD_MYCLE; P75132, TRMD_MYCPN; DR Q98Q98, TRMD_MYCPU; Q10797, TRMD_MYCTU; Q9JVL0, TRMD_NEIMA; DR Q9K0K4, TRMD_NEIMB; Q9CLE1, TRMD_PASMU; Q9HXQ1, TRMD_PSEAE; DR Q8Y0V8, TRMD_RALSO; Q98EE1, TRMD_RHILO; Q92L41, TRMD_RHIME; DR Q92JB6, TRMD_RICCN; Q9ZE37, TRMD_RICPR; Q8Z4I5, TRMD_SALTI; DR P36245, TRMD_SALTY; P36244, TRMD_SERMA; Q99UN0, TRMD_STAAM; DR Q8NX06, TRMD_STAAW; O69882, TRMD_STRCO; Q8K7X3, TRMD_STRP3; DR Q8P1F3, TRMD_STRP8; Q97RM4, TRMD_STRPN; Q9A0B6, TRMD_STRPY; DR P72828, TRMD_SYNY3; Q9X1Q5, TRMD_THEMA; Q8R5S2, TRMD_THETN; DR O83878, TRMD_TREPA; Q9PPS2, TRMD_UREPA; Q9KUF8, TRMD_VIBCH; DR Q8CWK5, TRMD_VIBVU; Q8PMY1, TRMD_XANAC; Q8PBC1, TRMD_XANCP; DR Q9PH37, TRMD_XYLFA; Q87F54, TRMD_XYLFT; Q8ZBU9, TRMD_YERPE; // ID 2.1.1.32 DE tRNA (guanine-N(2)-)-methyltransferase. AN N(2),N(2)-dimethylguanine tRNA methyltransferase. AN tRNA(guanine-26,N2-N2) methyltransferase. AN tRNA 2,2-dimethylguanosine-26 methyltransferase. AN tRNA(m(2,2)G26)dimethyltransferase. CA S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA CA containing N(2)-methylguanine. CC -!- In eukaryotic tRNAs two N(2)-guanine methylations occur, at the CC N(2)-methylguanine at position 10 and the N(2)-methylguanine at CC position 29. DR Q9YDY7, TRM1_AERPE; O67010, TRM1_AQUAE; Q9LFU5, TRM1_ARATH; DR O29443, TRM1_ARCFU; Q23270, TRM1_CAEEL; Q9VK89, TRM1_DROME; DR P57705, TRM1_HALN1; Q9NXH9, TRM1_HUMAN; Q8TGX6, TRM1_METAC; DR Q58356, TRM1_METJA; Q8PU28, TRM1_METMA; O27258, TRM1_METTH; DR Q9V1P3, TRM1_PYRAB; Q8ZWT5, TRM1_PYRAE; P81554, TRM1_PYRFU; DR O59493, TRM1_PYRHO; P20300, TRM1_PYRWO; Q9P804, TRM1_SCHPO; DR Q97ZH0, TRM1_SULSO; Q971V9, TRM1_SULTO; P57706, TRM1_THEAC; DR Q97AR2, TRM1_THEVO; P15565, TRM1_YEAST; Q9SRU7, TRM2_ARATH; // ID 2.1.1.33 DE tRNA (guanine-N(7)-)-methyltransferase. CA S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA CA containing N(7)-methylguanine. DR Q92G13, HEMK_RICCN; Q9ZCB3, HEMK_RICPR; Q12009, TRM8_YEAST; DR Q8UID4, TRMB_AGRT5; Q8YVX4, TRMB_ANASP; O66479, TRMB_AQUAE; DR Q8GXB7, TRMB_ARATH; Q8G9C6, TRMB_AZOSE; P59716, TRMB_BACAA; DR P59717, TRMB_BACCR; Q9K7U8, TRMB_BACHD; O34522, TRMB_BACSU; DR Q8A0X7, TRMB_BACTN; Q8G3T4, TRMB_BIFLO; Q89WA4, TRMB_BRAJA; DR Q8YEA9, TRMB_BRUME; Q8FXT6, TRMB_BRUSU; P57616, TRMB_BUCAI; DR Q8K927, TRMB_BUCAP; Q89A46, TRMB_BUCBP; Q23126, TRMB_CAEEL; DR Q9PN20, TRMB_CAMJE; P58088, TRMB_CAUCR; P59718, TRMB_CHLCV; DR Q9PL91, TRMB_CHLMU; Q9Z6S3, TRMB_CHLPN; O84836, TRMB_CHLTR; DR Q97FU9, TRMB_CLOAB; Q8XNB4, TRMB_CLOPE; Q897E6, TRMB_CLOTE; DR Q8FM11, TRMB_COREF; Q8NLS3, TRMB_CORGL; Q9RTS6, TRMB_DEIRA; DR O77263, TRMB_DROME; Q8FE22, TRMB_ECOL6; P32049, TRMB_ECOLI; DR P59719, TRMB_ENTFA; Q8R6G8, TRMB_FUSNN; P44648, TRMB_HAEIN; DR Q9ZL96, TRMB_HELPJ; O25443, TRMB_HELPY; Q9UBP6, TRMB_HUMAN; DR Q9CHI2, TRMB_LACLA; Q88WZ9, TRMB_LACPL; Q8F9Q1, TRMB_LEPIN; DR Q92B94, TRMB_LISIN; Q8Y6R8, TRMB_LISMO; Q9Z120, TRMB_MOUSE; DR P47589, TRMB_MYCGE; Q9F411, TRMB_MYCHO; Q9CCZ9, TRMB_MYCLE; DR Q8EWB6, TRMB_MYCPE; P75256, TRMB_MYCPN; Q98R44, TRMB_MYCPU; DR P96390, TRMB_MYCTU; Q9JU19, TRMB_NEIMA; Q9JZ24, TRMB_NEIMB; DR P59720, TRMB_NITEU; Q8EP25, TRMB_OCEIH; Q9CLC2, TRMB_PASMU; DR Q9I6B3, TRMB_PSEAE; Q88CS7, TRMB_PSEPK; Q88AF5, TRMB_PSESM; DR Q8Y1I7, TRMB_RALSO; Q98BJ3, TRMB_RHILO; Q92SI3, TRMB_RHIME; DR Q8Z3U1, TRMB_SALTI; Q8ZM40, TRMB_SALTY; Q96WV1, TRMB_SCHPO; DR Q8EBX8, TRMB_SHEON; Q99TB6, TRMB_STAAM; Q9KWZ4, TRMB_STAAU; DR Q8NW26, TRMB_STAAW; Q8CS43, TRMB_STAEP; Q8E1H8, TRMB_STRA3; DR P59721, TRMB_STRAW; Q9F305, TRMB_STRCO; Q8DVQ4, TRMB_STRMU; DR Q8NZU4, TRMB_STRP8; Q8DQV7, TRMB_STRPN; P58090, TRMB_STRPY; DR Q8DHH6, TRMB_SYNEL; P72546, TRMB_SYNP7; P73161, TRMB_SYNY3; DR Q9X027, TRMB_THEMA; O83477, TRMB_TREPA; Q9PQM2, TRMB_UREPA; DR Q9KUR2, TRMB_VIBCH; Q87LI7, TRMB_VIBPA; Q8DCC3, TRMB_VIBVU; DR Q8PHF4, TRMB_XANAC; Q8P631, TRMB_XANCP; Q9PF94, TRMB_XYLFA; DR Q87AE9, TRMB_XYLFT; Q8ZHE9, TRMB_YERPE; // ID 2.1.1.34 DE tRNA (guanosine-2'-O-)-methyltransferase. CA S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA CA containing 2'-O-methylguanosine. CC -!- Methylates the 2'-hydroxyl group of a guanosine present in a GG CC sequence. DR O67577, TRMH_AQUAE; P19396, TRMH_ECOLI; // ID 2.1.1.35 DE tRNA (uracil-5-)-methyltransferase. CA S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA CA containing thymine. PR PROSITE; PDOC00945; DR Q9PP92, TRMA_CAMJE; Q8X723, TRMA_ECO57; P23003, TRMA_ECOLI; DR P31812, TRMA_HAEIN; P55134, TRMA_NEIGO; Q9JT82, TRMA_NEIMA; DR Q9JYA0, TRMA_NEIMB; Q9CK32, TRMA_PASMU; Q9HV78, TRMA_PSEAE; DR Q9RHS9, TRMA_PSEFL; Q8Z313, TRMA_SALTI; P22038, TRMA_SALTY; DR Q9KVJ0, TRMA_VIBCH; Q8ZAA0, TRMA_YERPE; // ID 2.1.1.36 DE tRNA (adenine-N(1)-)-methyltransferase. CA S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA CA containing N(1)-methyladenine. CC -!- The enzymes from different sources are specific for different CC adenine residues in tRNA. // ID 2.1.1.37 DE DNA (cytosine-5-)-methyltransferase. CA S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA CA containing 5-methylcytosine. PR PROSITE; PDOC00089; DR Q9Y6K1, DM3A_HUMAN; O88508, DM3A_MOUSE; Q9UBC3, DM3B_HUMAN; DR O88509, DM3B_MOUSE; P34881, DNM1_ARATH; Q92072, DNM1_CHICK; DR P26358, DNM1_HUMAN; P13864, DNM1_MOUSE; Q27746, DNM1_PARLI; DR Q9Z330, DNM1_RAT ; // ID 2.1.1.38 DE O-demethylpuromycin O-methyltransferase. CA S-adenosyl-L-methionine + O-demethylpuromycin = S-adenosyl-L- CA homocysteine + puromycin. CC -!- Puromycin is the antibiotic derived from N(6)-dimethyladenosine by CC replacing the 3'-hydroxyl group with an amino group and acylating CC this with 4-O-methyltyrosine. DR P42712, DMPM_STRLP; // ID 2.1.1.39 DE Inositol 3-methyltransferase. AN Myo-inositol 1-O-methyltransferase. AN Inositol L-1-methyltransferase. AN Myo-inositol 1-methyltransferase. AN S-adenosylmethionine:myo-inositol 1-methyltransferase. AN S-adenosyl-L-methionine:myo-inositol 1-O-methyltransferase. CA S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + CA 1D-3-O-methyl-myo-inositol. // ID 2.1.1.40 DE Inositol 1-methyltransferase. AN Myo-inositol 3-O-methyltransferase. AN Inositol D-1-methyltransferase. AN S-adenosylmethionine:myo-inositol 3-methyltransferase. AN Inositol 3-O-methyltransferase. AN S-adenosyl-L-methionine:myo-inositol 3-O-methyltransferase. CA S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + CA 1D-1-O-methyl-myo-inositol. // ID 2.1.1.41 DE Sterol 24-C-methyltransferase. AN Delta(24)-methyltransferase. AN Delta(24)-sterol methyltransferase. AN Zymosterol-24-methyltransferase. AN S-adenosyl-4-methionine:sterol delta(24)-methyltransferase. AN SMT1. AN 24-sterol C-methyltransferase. AN S-adenosyl-L-methionine:delta(24(23))-sterol methyltransferase. AN Phytosterol methyltransferase. CA S-adenosyl-L-methionine + 5-alpha-cholest-8,24-dien-3-beta-ol = CA S-adenosyl-L-homocysteine + 24-methylene-5-alpha-cholest-8-en-3- CA beta-ol. CF Glutathione. CC -!- Acts on a range of sterols with a 24(25)-double bond in the CC sidechain. CC -!- While zymosterol is the preferred substrate it also acts on CC desmosterol, 5-alpha-cholesta-7,24-dien-3-beta-ol, 5-alpha- CC cholesta-5,7,24-trien-3-beta-ol, 4-alpha-methylzymosterol and CC others. CC -!- S-Adenosyl-L-methionine attacks the Si-face of the 24(25) double CC bond and the C-24 hydrogen is transferred to C-25 on the Re face CC of the double bond. DR O74198, ERG6_CANAL; O14321, ERG6_SCHPO; P25087, ERG6_YEAST; // ID 2.1.1.42 DE Luteolin O-methyltransferase. AN O-dihydric phenol methyltransferase. CA S-adenosyl-L-methionine + 5,7,3',4'-tetrahydroxyflavone = CA S-adenosyl-L-homocysteine + 5,7,4'-trihydroxy-3'-methoxyflavone. CC -!- Also acts on luteolin-7-O-beta-D-glucoside. // ID 2.1.1.43 DE Histone-lysine N-methyltransferase. AN Protein methylase III. CA S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + CA histone N(6)-methyl-L-lysine. DR Q96KQ7, BAT8_HUMAN; Q9Z148, BAT8_MOUSE; O60016, CLR4_SCHPO; DR Q04089, DOT1_YEAST; Q8TEK3, DOTL_HUMAN; Q9H9B1, HMT1_HUMAN; DR Q8WTS6, SET7_HUMAN; Q8VHL1, SET7_MOUSE; Q9VFK6, SET8_DROME; DR Q9NQR1, SET8_HUMAN; Q15047, SETB_HUMAN; O88974, SETB_MOUSE; DR O43463, SU91_HUMAN; O54864, SU91_MOUSE; Q9H5I1, SU92_HUMAN; DR Q9EQQ0, SU92_MOUSE; Q9FF80, SUV1_ARATH; O22781, SUV2_ARATH; DR Q9C5P4, SUV3_ARATH; Q8GZB6, SUV4_ARATH; O82175, SUV5_ARATH; DR Q8VZ17, SUV6_ARATH; Q9C5P1, SUV7_ARATH; Q9C5P0, SUV8_ARATH; DR Q9T0G7, SUV9_ARATH; P45975, SUV9_DROME; // ID 2.1.1.44 DE Dimethylhistidine N-methyltransferase. CA S-adenosyl-L-methionine + N(alpha),N(alpha)-dimethyl-L-histidine = CA S-adenosyl-L-homocysteine + N(alpha),N(alpha),N(alpha)-trimethyl-L- CA histidine. CC -!- Methylhistidine and histidine can also act as methyl acceptors, CC trimethylhistidine being formed in both cases. // ID 2.1.1.45 DE Thymidylate synthase. CA 5,10-methylenetetrahydrofolate + dUMP = dihydrofolate + dTMP. PR PROSITE; PDOC00086; DR Q05762, DRT1_ARATH; Q05763, DRT2_ARATH; Q23695, DRTS_CRIFA; DR P45350, DRTS_DAUCA; P16126, DRTS_LEIAM; P07382, DRTS_LEIMA; DR O81395, DRTS_MAIZE; Q27828, DRTS_PARTE; Q27713, DRTS_PLABA; DR P20712, DRTS_PLACH; P13922, DRTS_PLAFK; O02604, DRTS_PLAVI; DR P46103, DRTS_PLAVN; P51820, DRTS_SOYBN; Q07422, DRTS_TOXGO; DR Q27783, DRTS_TRYBB; Q27793, DRTS_TRYCR; O30397, TYSA_BACAM; DR O30394, TYSA_BACAT; Q59212, TYSA_BACLI; P42326, TYSA_BACSU; DR P54081, TYSB_BACAM; P11044, TYSB_BACSU; Q9P4T7, TYSY_AGABI; DR Q8UDS3, TYSY_AGRT5; O96650, TYSY_ASCSU; Q9K7B5, TYSY_BACHD; DR Q9ANR7, TYSY_BACMO; P07606, TYSY_BPPHT; P00471, TYSY_BPT4 ; DR Q8YI37, TYSY_BRUME; P57515, TYSY_BUCAI; Q8K9C3, TYSY_BUCAP; DR P59427, TYSY_BUCBP; P12461, TYSY_CANAL; Q9A6H0, TYSY_CAUCR; DR Q97EV3, TYSY_CLOAB; Q8FR47, TYSY_COREF; Q8NS38, TYSY_CORGL; DR P45351, TYSY_CRYNE; O76511, TYSY_DROME; P00470, TYSY_ECOLI; DR O62584, TYSY_ENCCU; Q8RGP6, TYSY_FUSNN; P44420, TYSY_HAEIN; DR P12462, TYSY_HSVAT; Q89940, TYSY_HSVE2; P06854, TYSY_HSVSA; DR P04818, TYSY_HUMAN; P90463, TYSY_KSHV ; P00469, TYSY_LACCA; DR P19368, TYSY_LACLA; Q92AD4, TYSY_LISIN; Q8Y626, TYSY_LISMO; DR Q8THH4, TYSY_METAC; Q9RAM7, TYSY_METFL; Q57931, TYSY_METJA; DR Q8TVL9, TYSY_METKA; Q8PXI1, TYSY_METMA; O26868, TYSY_METTH; DR P80305, TYSY_METTM; P07607, TYSY_MOUSE; Q9XC19, TYSY_MYCGA; DR P47469, TYSY_MYCGE; Q9CBW0, TYSY_MYCLE; P78029, TYSY_MYCPN; DR Q98Q31, TYSY_MYCPU; O33306, TYSY_MYCTU; O33380, TYSY_NEIGO; DR Q9JT57, TYSY_NEIMA; Q9JY72, TYSY_NEIMB; P57808, TYSY_PASMU; DR P13100, TYSY_PNECA; Q9I6F1, TYSY_PSEAE; Q8Y0U6, TYSY_RALSO; DR P45352, TYSY_RAT ; Q98KH9, TYSY_RHILO; Q92NQ5, TYSY_RHIME; DR Q8Z412, TYSY_SALTI; Q8ZMA9, TYSY_SALTY; Q8EH94, TYSY_SHEON; DR P48464, TYSY_SHIFL; Q99U61, TYSY_STAAM; P13954, TYSY_STAEP; DR Q8P1D1, TYSY_STRP8; Q97RW7, TYSY_STRPN; Q9A092, TYSY_STRPY; DR O66108, TYSY_VIBCH; Q87SA0, TYSY_VIBPA; Q8DER9, TYSY_VIBVU; DR P09249, TYSY_VZVD ; Q8D2N4, TYSY_WIGBR; Q8PP46, TYSY_XANAC; DR Q8PCE7, TYSY_XANCP; Q9PB13, TYSY_XYLFA; Q87BT4, TYSY_XYLFT; DR P06785, TYSY_YEAST; Q8ZHV1, TYSY_YERPE; Q9Z671, TYSY_ZYMMO; // ID 2.1.1.46 DE Isoflavone 4'-O-methyltransferase. CA S-adenosyl-L-methionine + isoflavone = S-adenosyl-L-homocysteine + CA 4'-O-methylisoflavone. // ID 2.1.1.47 DE Indole-3-pyruvate C-methyltransferase. AN Indolepyruvate C-methyltransferase. CA S-adenosyl-L-methionine + indole-3-pyruvate = S-adenosyl-L-homocysteine + CA (S)-beta-methylindole-3-pyruvate. // ID 2.1.1.48 DE rRNA (adenine-N(6)-)-methyltransferase. CA S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA CA containing N(6)-methyladenine. CC -!- Also methylates 2-aminoadenosine to 2-methylaminoadenosine. PR PROSITE; PDOC00871; DR P12038, ERM1_ENTFA; P06699, ERM1_STAAM; P02979, ERM2_STAAU; DR P13957, ERM3_STAAU; P13978, ERM4_STAAU; P09891, ERMA_ARTS3; DR P16898, ERMA_CORDI; P10738, ERMB_ECOLI; P20173, ERMB_ENTFA; DR Q03986, ERMD_BACLI; P07287, ERME_SACER; P10337, ERMF_BACFR; DR P06571, ERMG_BACSH; Q00014, ERMG_LACRE; Q04720, ERMJ_BACAN; DR P45438, ERMK_BACLI; P06572, ERMM_STAEP; P45439, ERMS_STRFR; DR Q02607, ERMU_BACFR; P13956, ERM_BACSU ; P21236, ERM_STRPN ; DR P06573, ERM_STRSA ; // ID 2.1.1.49 DE Amine N-methyltransferase. AN Nicotine N-methyltransferase. AN Tryptamine N-methyltransferase. AN Arylamine N-methyltransferase. CA S-adenosyl-L-methionine + an amine = S-adenosyl-L-homocysteine + CA a methylated amine. CC -!- A wide range of primary, secondary, and tertiary amines can act as CC acceptors, including tryptamine, aniline, nicotine and a variety CC of drugs and other xenobiotics. CC -!- Formerly EC 2.1.1.81. DR O95050, INMT_HUMAN; O97972, INMT_RABIT; // ID 2.1.1.50 DE Loganate O-methyltransferase. CA S-adenosyl-L-methionine + loganate = S-adenosyl-L-homocysteine + CA loganin. CC -!- Also acts on secologanate. CC -!- Methylates the 11-carboxyl group of the monoterpenoid loganate. // ID 2.1.1.51 DE rRNA (guanine-N(1)-)-methyltransferase. CA S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA CA containing N(1)-methylguanine. DR P36999, RRMA_ECOLI; // ID 2.1.1.52 DE rRNA (guanine-N(2)-)-methyltransferase. CA S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA CA containing N(2)-methylguanine. DR P57413, RSMC_BUCAI; Q8K9L5, RSMC_BUCAP; P39406, RSMC_ECOLI; DR P44453, RSMC_HAEIN; P42596, RSMD_ECOLI; // ID 2.1.1.53 DE Putrescine N-methyltransferase. CA S-adenosyl-L-methionine + putrescine = S-adenosyl-L-homocysteine + CA N-methylputrescine. PR PROSITE; PDOC01033; DR Q42963, PMT1_TOBAC; Q9SEH7, PMT2_TOBAC; Q9SEH5, PMT3_TOBAC; DR Q9SEH4, PMT4_TOBAC; // ID 2.1.1.54 DE Deoxycytidylate C-methyltransferase. CA 5,10-methylenetetrahydrofolate + dCMP = dihydrofolate + deoxy-5- CA methylcytidylate. CC -!- dCMP is methylated by formaldehyde in the presence of CC tetrahydrofolate. CC -!- CMP, dCTP and CTP can act as acceptor, more slowly. // ID 2.1.1.55 DE tRNA (adenine-N(6)-)-methyltransferase. CA S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA CA containing N(6)-methyladenine. // ID 2.1.1.56 DE mRNA (guanine-N(7)-)-methyltransferase. CA S-adenosyl-L-methionine + G(5')PPPR-RNA = S-adenosyl-L-homocysteine + CA m(7)G(5')PPPR-RNA. CC -!- Adds an N(7)-methylguanine cap to mRNA. CC -!- R may be guanosine or adenosine. DR O72908, MCES_FOWPV; Q08512, MCES_SPVKA; P20980, MCES_VACCC; DR P04318, MCES_VACCV; P33808, MCES_VARV ; Q9QB92, MCES_YABAM; // ID 2.1.1.57 DE mRNA (nucleoside-2'-O-)-methyltransferase. AN mRNA (adenosine-2'-O-)-methyltransferase. CA S-adenosyl-L-methionine + m7G(5')PPPR-RNA = S-adenosyl-L-homocysteine + CA m7G(5')PPPRM-RNA. CC -!- Adds an 2'-O-methylpurine cap to mRNA. CC -!- R may be guanosine or adenosine. CC -!- Formerly EC 2.1.1.58. DR P19748, PAP2_CAPVK; P15916, PAP2_FOWPV; P18628, PAP2_MYXVL; DR P23334, PAP2_SPVKA; P21033, PAP2_VACCC; P07617, PAP2_VACCV; DR P33052, PAP2_VARV ; // ID 2.1.1.58 DE Transferred entry: 2.1.1.57. // ID 2.1.1.59 DE [Cytochrome c]-lysine N-methyltransferase. CA S-adenosyl-L-methionine + [cytochrome c] L-lysine = S-adenosyl-L- CA homocysteine + [cytochrome c] N(6)-methyl-L-lysine. // ID 2.1.1.60 DE Calmodulin-lysine N-methyltransferase. CA S-adenosyl-L-methionine + calmodulin L-lysine = S-adenosyl-L- CA homocysteine + calmodulin N(6)-methyl-L-lysine. // ID 2.1.1.61 DE tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase. CA S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA CA containing 5-methylaminomethyl-2-thiouridylate. CC -!- Specific for the terminal methyl group of 5-methylaminomethyl-2- CC thiouridylate. DR Q8U9M5, TRMU_AGRT5; Q8YX56, TRMU_ANASP; O67274, TRMU_AQUAE; DR Q9KDF2, TRMU_BACHD; O35020, TRMU_BACSU; O51625, TRMU_BORBU; DR Q8YIL6, TRMU_BRUME; P57349, TRMU_BUCAI; Q8K9Q8, TRMU_BUCAP; DR P59460, TRMU_BUCBP; Q17440, TRMU_CAEEL; Q9PJ66, TRMU_CAMJE; DR P58074, TRMU_CAUCR; Q9PKA7, TRMU_CHLMU; Q9Z8A5, TRMU_CHLPN; DR O84289, TRMU_CHLTR; Q97GY2, TRMU_CLOAB; Q8XJH3, TRMU_CLOPE; DR Q8FQ01, TRMU_COREF; Q8NR24, TRMU_CORGL; Q9RTK1, TRMU_DEIRA; DR Q8X735, TRMU_ECO57; Q8CXZ8, TRMU_ECOL6; P25745, TRMU_ECOLI; DR P44551, TRMU_HAEIN; Q9ZJQ0, TRMU_HELPJ; O25893, TRMU_HELPY; DR O75648, TRMU_HUMAN; Q9CHA1, TRMU_LACLA; Q92BK1, TRMU_LISIN; DR Q8Y714, TRMU_LISMO; Q9DAT5, TRMU_MOUSE; P47537, TRMU_MYCGE; DR O33099, TRMU_MYCLE; Q8CXQ3, TRMU_MYCPE; P75365, TRMU_MYCPN; DR Q98Q11, TRMU_MYCPU; O53271, TRMU_MYCTU; Q9JTJ9, TRMU_NEIMA; DR Q9JYJ6, TRMU_NEIMB; Q8CXC7, TRMU_OCEIH; Q9CLA3, TRMU_PASMU; DR Q9I0L2, TRMU_PSEAE; Q8XVV4, TRMU_RALSO; Q98HL0, TRMU_RHILO; DR Q92MB5, TRMU_RHIME; Q92IL0, TRMU_RICCN; Q9ZDM1, TRMU_RICPR; DR Q8Z7G9, TRMU_SALTI; Q8ZPZ4, TRMU_SALTY; O13947, TRMU_SCHPO; DR Q8CX40, TRMU_SHEON; Q931Q6, TRMU_STAAM; Q99TM8, TRMU_STAAN; DR Q8NW84, TRMU_STAAW; Q8CSA5, TRMU_STAEP; Q8E2L9, TRMU_STRA3; DR O86583, TRMU_STRCO; Q8DRS4, TRMU_STRMU; Q8K5H5, TRMU_STRP3; DR Q8NZ00, TRMU_STRP8; Q97T38, TRMU_STRPN; P58075, TRMU_STRPY; DR Q8CWW0, TRMU_STRR6; Q8CWM0, TRMU_SYNEL; P73755, TRMU_SYNY3; DR Q9WYZ0, TRMU_THEMA; Q9PQ88, TRMU_UREPA; Q9KSX8, TRMU_VIBCH; DR Q87QL9, TRMU_VIBPA; Q8CWJ6, TRMU_VIBVU; Q8D397, TRMU_WIGBR; DR Q8PL08, TRMU_XANAC; Q8P9A1, TRMU_XANCP; Q9PDD9, TRMU_XYLFA; DR Q87DM0, TRMU_XYLFT; Q12093, TRMU_YEAST; Q8ZFQ5, TRMU_YERPE; DR Q8RAH7, TRU1_THETN; Q8R7F0, TRU2_THETN; // ID 2.1.1.62 DE mRNA (2'-O-methyladenosine-N(6)-)-methyltransferase. CA S-adenosyl-L-methionine + m(7)G(5')PPPAM = S-adenosyl-L-homocysteine + CA m(7)G(5')PPPM(6)AM. CC -!- mRNA containing an N(6),2'-O-dimethyladenosine cap. // ID 2.1.1.63 DE Methylated-DNA--[protein]-cysteine S-methyltransferase. AN 6-O-methylguanine-DNA methyltransferase. AN O-6-methylguanine-DNA-alkyltransferase. CA DNA (containing 6-O-methylguanine) + [protein]-L-cysteine = DNA (without CA 6-O-methylguanine) + protein S-methyl-L-cysteine. CC -!- This protein is involved in the repair of alkylated DNA. It acts only CC on the alkylated DNA (cf. EC 3.2.2.20 and EC 3.2.2.21). CC -!- Since the acceptor protein is the 'enzyme' itself and the S-methyl-L- CC cysteine derivative formed is relatively stable, the reaction is not CC catalytic. PR PROSITE; PDOC00320; DR P19220, ADAB_BACSU; P06134, ADA_ECOLI ; Q10630, ADA_MYCTU ; DR P26189, ADA_SALTY ; P29177, MGMT_BOVIN; P26186, MGMT_CRIGR; DR P16455, MGMT_HUMAN; P26187, MGMT_MOUSE; P24528, MGMT_RAT ; DR P26188, MGMT_YEAST; P11742, OGT_BACSU ; P09168, OGT_ECOLI ; DR P44687, OGT_HAEIN ; P52982, OGT_MYCLE ; Q9ZET8, OGT_MYCPA ; DR Q10627, OGT_MYCTU ; P37429, OGT_SALTY ; // ID 2.1.1.64 DE 3-demethylubiquinone-9 3-O-methyltransferase. CA S-adenosyl-L-methionine + 3-demethylubiquinone-9 = S-adenosyl-L- CA homocysteine + ubiquinone-9. DR Q8UA66, UBIG_AGRT5; Q8YJ98, UBIG_BRUME; Q9A9X1, UBIG_CAUCR; DR Q8XE29, UBIG_ECO57; P17993, UBIG_ECOLI; Q9JWE6, UBIG_NEIMA; DR Q9JXI7, UBIG_NEIMB; Q9CMI6, UBIG_PASMU; Q9HZ63, UBIG_PSEAE; DR Q8Y0Z5, UBIG_RALSO; Q98G87, UBIG_RHILO; Q92MK1, UBIG_RHIME; DR Q92H07, UBIG_RICCN; Q9ZCT9, UBIG_RICPR; Q8Z560, UBIG_SALTI; DR P37431, UBIG_SALTY; Q9KSJ9, UBIG_VIBCH; Q8PK00, UBIG_XANAC; DR Q8P8H2, UBIG_XANCP; Q9PAM5, UBIG_XYLFA; Q87BG5, UBIG_XYLFT; DR Q8ZGR6, UBIG_YERPE; // ID 2.1.1.65 DE Licodione 2'-O-methyltransferase. CA S-adenosyl-L-methionine + licodione = S-adenosyl-L-homocysteine + CA 2'-O-methyllicodione. CC -!- As well as licodione (1-(2,4-dihydroxyphenyl)-3-(4-hydroxyphenyl)- CC 1,3-propanedione), the 2''-hydroxy-derivative and isoliquiritigenin CC can act as acceptor, more slowly. // ID 2.1.1.66 DE rRNA (adenosine-2'-O-)-methyltransferase. AN RNA-pentose methylase. AN Thiostrepton-resistance methylase. CA S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA CA containing a single residue of 2'-O-methyladenosine. DR P18644, TSNR_STRCN; P52393, TSNR_STRLU; // ID 2.1.1.67 DE Thiopurine S-methyltransferase. CA S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + CA a thiopurine S-methylether. CC -!- Also acts, more slowly, on thiopyrimidines and aromatic thiols. CC -!- Not identical with EC 2.1.1.9. DR P51580, TPMT_HUMAN; O55060, TPMT_MOUSE; Q9QX22, TPMT_MUSSP; DR O86262, TPMT_PSESJ; Q9Z0T0, TPMT_RAT ; Q9KSN0, TPMT_VIBCH; // ID 2.1.1.68 DE Caffeate O-methyltransferase. CA S-adenosyl-L-methionine + 3,4-dihydroxy-trans-cinnamate = CA S-adenosyl-L-homocysteine + 3-methoxy-4-hydroxy-trans-cinnamate. CC -!- 3,4-dihydroxybenzaldehyde and catechol can act as acceptor, more CC slowly. DR Q9XGW0, COM1_OCIBA; Q43046, COM1_POPKI; Q00763, COM1_POPTM; DR Q9XGV9, COM2_OCIBA; Q41086, COM2_POPTM; Q43047, COM3_POPKI; DR Q9FQY8, COMT_CAPAN; O81646, COMT_CAPCH; Q8W013, COMT_CATRO; DR O23760, COMT_CLABR; Q8LL87, COMT_COFCA; Q9SWC2, COMT_EUCGL; DR P46484, COMT_EUCGU; Q06509, COMT_MAIZE; P28002, COMT_MEDSA; DR Q43609, COMT_PRUDU; Q8GU25, COMT_ROSCH; O82054, COMT_SACOF; DR Q43239, COMT_ZINEL; // ID 2.1.1.69 DE 5-hydroxyfuranocoumarin 5-O-methyltransferase. CA S-adenosyl-L-methionine + 5-hydroxyfuranocoumarin = S-adenosyl-L- CA homocysteine + 5-methoxyfuranocoumarin. CC -!- Converts bergaptol into bergapten. CC -!- Methylates the 5-hydroxyl of some hydroxy- and methylcoumarins, but CC has little activity on non-coumarin phenols. // ID 2.1.1.70 DE 8-hydroxyfuranocoumarin 8-O-methyltransferase. CA S-adenosyl-L-methionine + 8-hydroxyfuranocoumarin = S-adenosyl-L- CA homocysteine + 8-methoxyfuranocoumarin. CC -!- Converts xanthotoxol into xanthotoxin. CC -!- Methylates the 8-hydroxyl of some hydroxy- and methylcoumarins, but CC has little activity on non-coumarin phenols. // ID 2.1.1.71 DE Phosphatidyl-N-methylethanolamine N-methyltransferase. CA S-adenosyl-L-methionine + phosphatidyl-N-methylethanolamine = CA S-adenosyl-L-homocysteine + phosphatidyl-N-dimethylethanolamine. CC -!- Also catalyzes the transfer of a further methylgroup, producing CC phosphatidylcholine. // ID 2.1.1.72 DE Site-specific DNA-methyltransferase (adenine-specific). AN N-6 adenine-specific DNA methylase. AN Modification methylase. AN Restriction-modification system. CA S-adenosyl-L-methionine + DNA adenine = S-adenosyl-L-homocysteine + CA DNA 6-methylaminopurine. CC -!- This is a large group of enzymes, the majority of which, with CC enzymes of similar site specificity listed as EC 3.1.21.3, CC EC 3.1.21.4 and EC 3.1.21.5, form so-called restriction- CC modification systems. CC -!- See the REBASE database for a complete list of these enzymes: CC http://www.neb.com/rebase/ PR PROSITE; PDOC00087; DR P21311, DMA7_ECOLI; P12427, DMA_BPT2 ; P04392, DMA_BPT4 ; DR P00475, DMA_ECOLI ; P44431, DMA_HAEIN ; P55893, DMA_SALTY ; DR P45454, DMA_SERMA ; O33844, DMA_TREPA ; Q08318, DMA_VIBCH ; DR P50179, ML21_LACLC; P50178, ML22_LACLC; P34720, MT1A_MORBO; DR P34721, MT1B_MORBO; P04043, MT21_STRPN; P09358, MT22_STRPN; DR P25240, MT57_ECOLI; P25201, MTA1_ACICA; P58284, MTA1_AZOBR; DR O30570, MTB1_BRUAB; P22772, MTB3_BACAR; P33563, MTBB_BACSU; DR P43423, MTC1_BACST; Q45971, MTC1_CAUCR; Q01511, MTC1_CHVN1; DR P42828, MTC1_COREQ; P31118, MTC2_CHVP1; P10835, MTC3_CHVN1; DR P00472, MTE1_ECOLI; P04393, MTE5_ECOLI; P14827, MTEC_ENTCL; DR P14871, MTF1_FLAOK; P20590, MTH1_HAEIN; P29538, MTH1_HAEPA; DR P00473, MTH2_HAEHA; P43871, MTH3_HAEIN; P50193, MTHB_HAEPH; DR P17744, MTHC_HAEIN; P44414, MTHD_HAEIN; P25238, MTK1_KLEPN; DR P35516, MTL1_LACLA; P50190, MTM1_MICAM; P23192, MTM2_MORBO; DR Q58015, MTM3_METJA; P43641, MTMU_MYCSP; P24582, MTN3_NEILA; DR P05103, MTP7_PSEAE; P00474, MTPS_PROST; P52284, MTR1_CHVN6; DR P14751, MTR1_RHOSH; O30569, MTS1_RHIME; Q53609, MTS1_STRAL; DR P29347, MTS1_STRSA; P29749, MTT8_THETH; P14385, MTTA_THEAQ; DR P43422, MTV1_BACST; Q03055, MTV1_VIBS3; P96188, MTX1_XANCR; DR P10484, T1M1_ECOLI; P75436, T1MD_MYCPN; Q47282, T1ME_ECOLI; DR Q57168, T1MH_HAEIN; Q60297, T1MH_METJA; P08957, T1MK_ECOLI; DR Q47163, T1MP_ECOLI; P07989, T1M_SALPO ; P40813, T1M_SALTY ; DR P25239, T257_ECOLI; P71366, T3MH_HAEIN; P08763, T3MO_BPP1 ; DR P12364, T3MO_ECOLI; P40814, T3MO_SALTY; Q07605, T4BA_BACCO; DR Q49400, Y184_MYCGE; Q9CNN7, Y390_PASMU; Q87DS5, Y606_XYLFT; DR P75561, YB08_MYCPN; P75451, YB11_MYCPN; Q50290, YB98_MYCPN; DR Q9PDL1, YD68_XYLFA; P39199, YFCB_ECOLI; P45106, YFCB_HAEIN; DR P39201, YFCB_SALTY; P39200, YFCB_VIBAN; Q9JYC0, YG55_NEIMB; DR Q9I347, YG78_PSEAE; P28638, YHDJ_ECOLI; Q9JTA1, YJ12_NEIMA; DR Q9KQ83, YL18_VIBCH; P51715, YO13_BPHP1; // ID 2.1.1.73 DE Site-specific DNA-methyltransferase (cytosine-specific). AN C-5 cytosine-specific DNA methylase. AN Modification methylase. AN Restriction-modification system. CA S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + CA DNA 5-methylcytosine. CC -!- This is a large group of enzymes, the majority of which, with CC enzymes of similar site specificity listed as EC 3.1.21.3, CC EC 3.1.21.4 and EC 3.1.21.5, form so-called restriction- CC modification systems. CC -!- See the REBASE database for a complete list of these enzymes: CC http://www.neb.com/rebase/ PR PROSITE; PDOC00088; DR P11876, DCM_ECOLI ; Q57983, MT51_METJA; Q58600, MT52_METJA; DR O52702, MTA1_ACEPA; P31974, MTA1_ARTLU; P94147, MTA1_RUEGE; DR P34882, MTAA_SYNP2; P34883, MTAB_SYNP2; P34905, MTB1_BACBR; DR P13906, MTB1_BACSH; P10283, MTB1_BREEP; P25262, MTB1_HERAU; DR Q59603, MTB1_NEIGO; Q59605, MTB5_NEIGO; P43420, MTB6_BACSP; DR P19888, MTBA_BACAR; P09389, MTBB_BPSPB; P17044, MTBF_BACSU; DR P05795, MTBP_BACSU; P06530, MTBR_BACSU; P09915, MTBR_BPRH1; DR P00476, MTBS_BPSPR; P36216, MTC1_CHVI3; P25263, MTC1_HERAU; DR P25264, MTC2_HERAU; P05302, MTD1_DESDN; P24600, MTD1_HERAU; DR Q9RLM4, MTD1_NEIMC; P25265, MTD2_HERAU; P50185, MTD5_DACSA; DR P25266, MTE1_HERAU; P05101, MTE2_ECOLI; P50196, MTE8_ECOLI; DR P34906, MTF1_FUSNU; Q59606, MTF7_NEIGO; P25282, MTG1_HAEGA; DR P25267, MTG1_HERAU; P25283, MTG2_HAEGA; P05102, MTH1_HAEHA; DR O30868, MTH2_HAEAE; P15446, MTH2_HAEPA; P20589, MTH3_HAEAE; DR P45000, MTH5_HAEIN; P50192, MTHA_HAEPH; P29567, MTHT_METTF; DR P11408, MTM1_MORSP; P31033, MTM4_NEIGO; P50188, MTN1_NOCAE; DR P50182, MTN4_NEILA; P24581, MTNX_NEILA; O33481, MTP1_PSYTA; DR P08455, MTP2_NEIGO; P09795, MTS1_SALIN; O31073, MTS1_STRAH; DR P34879, MTS2_SHISO; P16668, MTS3_STAAU; P23737, MTS9_STAAU; DR P34877, MTSA_LACLC; P34878, MTSB_LACLC; P15840, MTSI_SPISQ; DR P52311, MTX2_XANOR; // ID 2.1.1.74 DE Methylenetetrahydrofolate--tRNA-(uracil-5-)-methyltransferase DE (FADH-oxidizing). AN Folate-dependent ribothymidyl synthase. CA 5,10-methylenetetrahydrofolate + tRNA U(psi)C + FADH(2) = CA tetrahydrofolate + tRNA T(psi)C + FAD. // ID 2.1.1.75 DE Apigenin 4'-O-methyltransferase. AN Flavonoid O-methyltransferase. CA S-adenosyl-L-methionine + 5,7,4'-trihydroxyflavone = CA S-adenosyl-L-homocysteine + 4'-methoxy-5,7-dihydroxyflavone. CC -!- Converts apigenin into acacetin. CC -!- Naringenin (5,7,4'-trihydroxyflavonone) can also act as acceptor, CC more slowly. // ID 2.1.1.76 DE Quercetin 3-O-methyltransferase. AN Flavonol 3-O-methyltransferase. CA S-adenosyl-L-methionine + 3,5,7,3',4'-pentahydroxyflavone = CA S-adenosyl-L-homocysteine + 3-methoxy-5,7,3',4'-tetrahydroxyflavone. CC -!- Specific for quercetin. Related enzymes bring about the 3-O- CC methylation of other flavonols, such as galangin and kaempferol. DR Q9FK25, OMT1_ARATH; P59049, OMT1_CHRAE; Q42653, OMT2_CHRAE; // ID 2.1.1.77 DE Protein-L-isoaspartate(D-aspartate) O-methyltransferase. AN Protein L-isoaspartyl methyltransferase. AN Protein D-aspartate methyltransferase. AN Protein beta-aspartate O-methyltransferase. AN L-isoaspartyl protein carboxyl methyltransferase. CA S-adenosyl-L-methionine + protein L-beta-aspartate = S-adenosyl-L- CA homocysteine + protein L-beta-aspartate methyl ester. CC -!- D-aspartate (but not L-aspartate) residues in proteins can also act CC as acceptors. CC -!- Formerly EC 2.1.1.24. PR PROSITE; PDOC00985; DR O30199, PIM1_ARCFU; Q8TT93, PIM1_METAC; O27962, PIM2_ARCFU; DR Q8TT94, PIM2_METAC; Q9YDA1, PIMT_AERPE; Q42539, PIMT_ARATH; DR P15246, PIMT_BOVIN; Q92047, PIMT_BRARE; Q27873, PIMT_CAEEL; DR Q9A6T6, PIMT_CAUCR; Q27869, PIMT_DROME; Q8FEJ8, PIMT_ECOL6; DR P24206, PIMT_ECOLI; Q9ZKC2, PIMT_HELPJ; P56133, PIMT_HELPY; DR P22061, PIMT_HUMAN; Q57636, PIMT_METJA; Q8TYL4, PIMT_METKA; DR Q8PW90, PIMT_METMA; O26915, PIMT_METTH; P23506, PIMT_MOUSE; DR P45683, PIMT_PSEAE; Q9UXX0, PIMT_PYRAB; Q8ZYN0, PIMT_PYRAE; DR Q8TZR3, PIMT_PYRFU; O59534, PIMT_PYRHO; P22062, PIMT_RAT ; DR O08249, PIMT_RHIME; Q8Z474, PIMT_SALTI; Q8ZMF9, PIMT_SALTY; DR Q56308, PIMT_THEMA; Q9KUI8, PIMT_VIBCH; Q87LQ6, PIMT_VIBPA; DR Q8DC56, PIMT_VIBVU; Q43209, PIMT_WHEAT; Q8ZBQ0, PIMT_YERPE; // ID 2.1.1.78 DE Isoorientin 3'-O-methyltransferase. CA S-adenosyl-L-methionine + isoorientin = S-adenosyl-L-homocysteine + CA isoscoparin. CC -!- Also acts on isoorientin 2''-O-rhamnoside. CC -!- Involved in the biosynthesis of flavones. // ID 2.1.1.79 DE Cyclopropane-fatty-acyl-phospholipid synthase. AN Cyclopropane synthetase. AN Unsaturated-phospholipid methyltransferase. AN Cyclopropane fatty acid synthase. AN CFA synthase. CA S-adenosyl-L-methionine + phospholipid olefinic fatty acid = CA S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid. CC -!- Adds a methylene group across the 9,10 position of a delta(9)- CC olefinic acyl chain in phosphatidylethanolamine or, more slowly, CC phosphatidylglycerol or phosphatidylinositol forming a cyclopropane CC derivative (cf. EC 2.1.1.16). DR Q11195, CFA1_MYCTU; Q49807, CFA2_MYCLE; Q11196, CFA2_MYCTU; DR P45509, CFA_CITFR ; P30010, CFA_ECOLI ; // ID 2.1.1.80 DE Protein-glutamate O-methyltransferase. AN Methyl-accepting chemotaxis protein O-methyltransferase. CA S-adenosyl-L-methionine + protein L-glutamate = S-adenosyl-L- CA homocysteine + protein L-glutamate methyl ester. CC -!- Forms ester groups with L-glutamate residues in a number of membrane CC proteins. CC -!- Formerly EC 2.1.1.24. DR Q9KCB8, CHER_BACHD; P31105, CHER_BACSU; O51069, CHER_BORBU; DR P45676, CHER_CAMJE; P07364, CHER_ECOLI; P21824, CHER_ENTAE; DR Q92DX0, CHER_LISIN; Q9XDE8, CHER_LISMO; P07801, CHER_SALTY; DR Q9WYT5, CHER_THEMA; Q57508, CHER_VIBAN; Q9X9K2, CHER_VIBPA; DR O87131, CHR1_PSEAE; Q9KQ06, CHR1_VIBCH; Q9I6V7, CHR2_PSEAE; DR Q9KS61, CHR2_VIBCH; Q9KKL3, CHR3_VIBCH; P31759, FRZF_MYXXA; // ID 2.1.1.81 DE Transferred entry: 2.1.1.49. // ID 2.1.1.82 DE 3-methylquercetin 7-O-methyltransferase. AN Flavonol 7-O-methyltransferase. CA S-adenosyl-L-methionine + 3',4',5,7-tetrahydroxy-3-methoxyflavone = CA S-adenosyl-L-homocysteine + 3',4',5-trihydroxy-3,7-dimethoxyflavone. CC -!- Involved with EC 2.1.1.76 and EC 2.1.1.83 in the methylation of CC quercetin to 3,7,4'-trimethylquercetin in Chrysosplenium americanum. CC -!- Does not act on flavones, dihydroflavonols, or their glucosides. // ID 2.1.1.83 DE 3,7-dimethylquercetin 4'-O-methyltransferase. AN Flavonol 4'-O-methyltransferase. CA S-adenosyl-L-methionine + 3',4',5-trihydroxy-3,7-dimethoxyflavone = CA S-adenosyl-L-homocysteine + 3',5-dihydroxy-3,4',7-trimethoxyflavone. CC -!- 3,7-dimethylquercetin can also act as acceptor. CC -!- Involved with EC 2.1.1.76 and EC 2.1.1.82 in the methylation of CC quercetin to 3,7,4'-trimethylquercetin in Chrysosplenium americanum. CC -!- Does not act on flavones, dihydroflavonols, or their glucosides. // ID 2.1.1.84 DE Methylquercetagetin 6-O-methyltransferase. AN Flavonol 6-O-methyltransferase. CA S-adenosyl-L-methionine + 3',4',5,6-tetrahydroxy-3,7-dimethoxyflavone = CA S-adenosyl-L-homocysteine + 3',4',5-trihydroxy-3,6,7-trimethoxyflavone. CC -!- Also methylates 3,7,3'-trimethylquercetagetin at the 6-position. CC -!- Does not act on flavones, dihydroflavonols, or their glucosides. CC -!- From Chrysosplenium americanum. // ID 2.1.1.85 DE Protein-histidine N-methyltransferase. AN Protein methylase IV. CA S-adenosyl-L-methionine + protein L-histidine = S-adenosyl-L- CA homocysteine + protein N-methyl-L-histidine. CC -!- Highly specific for histidine residues, for example in actin. // ID 2.1.1.86 DE Tetrahydromethanopterin S-methyltransferase. AN Tetrahydromethanopterin methyltransferase. CA 5-methyl-5,6,7,8-tetrahydromethanopterin + 2-mercaptoethanesulfonate = CA 5,6,7,8-tetrahydromethanopterin + 2-(methylthio)ethanesulfonate. CC -!- Involved in the formation of methane from CO in Methanobacterium CC thermoautotrophicum. DR Q58261, MTRA_METJA; O32867, MTRA_METKA; O59640, MTRA_METMA; DR O27227, MTRA_METTH; P80184, MTRA_METTM; Q58260, MTRB_METJA; DR O32866, MTRB_METKA; P80655, MTRB_METMA; O27228, MTRB_METTH; DR Q59584, MTRB_METTM; Q58259, MTRC_METJA; O32865, MTRC_METKA; DR O59638, MTRC_METMA; O27229, MTRC_METTH; P80185, MTRC_METTM; DR Q58258, MTRD_METJA; O32864, MTRD_METKA; P80653, MTRD_METMA; DR O27230, MTRD_METTH; P80183, MTRD_METTM; Q49176, MTRE_METFE; DR Q58257, MTRE_METJA; Q49606, MTRE_METKA; P80651, MTRE_METMA; DR O27231, MTRE_METTH; P80186, MTRE_METTM; Q50830, MTRE_METVA; DR Q58262, MTRF_METJA; P80654, MTRF_METMA; O27226, MTRF_METTH; DR Q50773, MTRF_METTM; Q58263, MTRG_METJA; O32868, MTRG_METKA; DR P80656, MTRG_METMA; O27225, MTRG_METTH; Q50774, MTRG_METTM; DR Q58264, MTRH_METJA; O32869, MTRH_METKA; P80650, MTRH_METMA; DR O27224, MTRH_METTH; P80187, MTRH_METTM; P80652, TM2A_METMA; // ID 2.1.1.87 DE Pyridine N-methyltransferase. CA S-adenosyl-L-methionine + pyridine = S-adenosyl-L-homocysteine + CA N-methylpyridinium. // ID 2.1.1.88 DE 8-hydroxyquercetin 8-O-methyltransferase. AN Flavonol 8-O-methyltransferase. CA S-adenosyl-L-methionine + 3,3',4',5,7,8-hexahydroxyflavone = CA S-adenosyl-L-homocysteine + 3,3',4',5,7-pentahydroxy-8-methoxyflavone. CC -!- Also acts on 8-hydroxykaempferol, but not on the glycosides of CC 8-hydroxyflavonols. CC -!- An enzyme from the flower buds of Lotus corniculatus. // ID 2.1.1.89 DE Tetrahydrocolumbamine 2-O-methyltransferase. CA S-adenosyl-L-methionine + 5,8,13,13A-tetrahydrocolumbamine = CA S-adenosyl-L-homocysteine + tetrahydropalmatine. CC -!- Involved in the biosynthesis of the berberine alkaloids. // ID 2.1.1.90 DE Methanol--5-hydroxybenzimidazolylcobamide Co-methyltransferase. CA Methanol + 5-hydroxybenzimidazolylcobamide = Co-methyl-Co-5- CA hydroxybenzimidazolylcob(I)amide + H(2)O. CC -!- The enzyme from methanosarcina barkeri contains 3-4 molecules of CC bound 5-hydroxybenzimidazolylcobamide which act as methyl acceptor. CC -!- Inactivated by oxygen and other oxidizing agents, and reactivated by CC catalytic amounts of ATP and hydrogen. // ID 2.1.1.91 DE Isobutyraldoxime O-methyltransferase. AN Aldoxime methyltransferase. CA S-adenosyl-L-methionine + 2-methylpropanal oxime = S-adenosyl-L- CA homocysteine + 2-methylpropanal O-methyloxime. CC -!- Oximes of C(4) to C(6) aldehydes can act as acceptors. CC -!- The most active substrate is 2-methylbutyraldoxime. // ID 2.1.1.92 DE Bergaptol O-methyltransferase. CA S-adenosyl-L-methionine + bergaptol = S-adenosyl-L-homocysteine + CA O-methylbergaptol. // ID 2.1.1.93 DE Xanthotoxol O-methyltransferase. CA S-adenosyl-L-methionine + xanthotoxol = S-adenosyl-L-homocysteine + CA O-methylxanthotoxol. CC -!- Also acts on 5-hydroxyxanthotoxin, forming isopimpinellin. // ID 2.1.1.94 DE 11-O-demethyl-17-O-deacetylvindoline O-methyltransferase. CA S-adenosyl-L-methionine + 11-O-demethyl-17-O-deacetylvindoline = CA S-adenosyl-L-homocysteine + 17-O-deacetylvindoline. CC -!- Involved in the biosynthesis of vindoline from tabersonine in CC Catharanthus roseus. // ID 2.1.1.95 DE Tocopherol O-methyltransferase. CA S-adenosyl-L-methionine + gamma-tocopherol = S-adenosyl-L-homocysteine + CA alpha-tocopherol. DR Q9ZSK1, GTOM_ARATH; // ID 2.1.1.96 DE Thioether S-methyltransferase. CA S-adenosyl-L-methionine + dimethyl sulfide = S-adenosyl-L-homocysteine + CA trimethylsulfonium. CC -!- Also acts on dimethyl selenide, dimethyl telluride, diethyl sulfide, CC 1,4-dithiane and many other thioethers. PR PROSITE; PDOC00844; DR P40936, TEMT_MOUSE; // ID 2.1.1.97 DE 3-hydroxyanthranilate 4-C-methyltransferase. CA S-adenosyl-L-methionine + 3-hydroxyanthranilate = S-adenosyl-L- CA homocysteine + 3-hydroxy-4-methylanthranilate. CC -!- Involved in the biosynthesis of the antibiotic actinomycin in CC Streptomyces antibioticus. // ID 2.1.1.98 DE Diphthine synthase. CA S-adenosyl-L-methionine + 2-(3-carboxy-3-aminopropyl)-L-histidine = CA S-adenosyl-L-homocysteine + 2-[3-carboxy-3-(methylammonio)propyl]-L- CA histidine. CC -!- 2-[3-carboxy-3-(methylammonio)propyl]-L-histidine and the CC corresponding dimethyl compound can also act as acceptors. CC -!- The trimethylated product, diphthine, is converted into diphthamide CC by EC 6.3.2.22. DR P32469, DPH5_YEAST; // ID 2.1.1.99 DE 16-methoxy-2,3-dihydro-3-hydroxytabersonine N-methyltransferase. CA S-adenosyl-L-methionine + 16-methoxy-2,3-dihydro-3-hydroxytabersonine = CA S-adenosyl-L-homocysteine + deacetoxyvindoline. CC -!- Involved in the biosynthesis of vindoline from tabersonine in CC Catharanthus roseus. // ID 2.1.1.100 DE Protein-S isoprenylcysteine O-methyltransferase. AN Isoprenylcysteine carboxylmethyltransferase. AN Prenylcysteine carboxyl methyltransferase. AN Prenylated protein carboxyl methyltransferase. CA S-adenosyl-L-methionine + protein C-terminal S-farnesyl-L-cysteine = CA S-adenosyl-L-homocysteine + protein C-terminal S-farnesyl-L-cysteine CA methyl ester. CC -!- C-terminal S-geranylgeranylcysteine and S-geranylcysteine residues CC are also methylated, more slowly. CC -!- Formerly EC 2.1.1.24. DR O60725, ICMT_HUMAN; Q9EQK7, ICMT_MOUSE; Q9WVM4, ICMT_RAT ; DR O12947, ICMT_XENLA; P87014, MAM4_SCHPO; P32584, ST14_YEAST; // ID 2.1.1.101 DE Macrocin O-methyltransferase. CA S-adenosyl-L-methionine + macrocin = S-adenosyl-L-homocysteine + tylosin. CC -!- The 3-hydroxyl group of a 2-O-methyl-6-deoxy-D-allose residue in the CC macrolide antibiotic macrocin acts as methyl acceptor; also converts CC lactenosin into desmyocin. CC -!- Not identical with EC 2.1.1.102. // ID 2.1.1.102 DE Demethylmacrocin O-methyltransferase. CA S-adenosyl-L-methionine + demethylmacrocin = S-adenosyl-L-homocysteine + CA macrocin. CC -!- The 2-hydroxyl group of a 6-deoxy-D-allose residue in CC demethylmacrocin acts as methyl acceptor. CC -!- Not identical with EC 2.1.1.101. // ID 2.1.1.103 DE Phosphoethanolamine N-methyltransferase. CA S-adenosyl-L-methionine + ethanolamine phosphate = S-adenosyl-L- CA homocysteine + N-methylethanolamine phosphate. CC -!- The enzyme may catalyze the transfer of two further methyl groups CC to the product. DR Q9M571, PEAM_SPIOL; Q9FR44, PEM1_ARATH; Q944H0, PEM2_ARATH; DR Q9C6B9, PEM3_ARATH; // ID 2.1.1.104 DE Caffeoyl-CoA O-methyltransferase. AN Trans-caffeoyl-CoA 3-O-methyltransferase. CA S-adenosyl-L-methionine + caffeoyl-CoA = S-adenosyl-L-homocysteine + CA feruloyl-CoA. DR Q9C9W3, CAM1_ARATH; O81185, CAM1_EUCGL; Q9XGD6, CAM1_MAIZE; DR O65862, CAM1_POPTR; O24144, CAM1_TOBAC; Q9C9W4, CAM2_ARATH; DR Q9SWB8, CAM2_EUCGL; Q9XGD5, CAM2_MAIZE; O65922, CAM2_POPTR; DR O24149, CAM2_TOBAC; Q9C5D7, CAM3_ARATH; O24150, CAM3_TOBAC; DR O49499, CAM4_ARATH; O24151, CAM4_TOBAC; O04899, CAM5_TOBAC; DR Q42945, CAM6_TOBAC; Q9SLP8, CAMT_CITNA; O04854, CAMT_EUCGU; DR Q40313, CAMT_MEDSA; O65162, CAMT_MESCR; P28034, CAMT_PETCR; DR P81081, CAMT_PINPS; Q9ZTT5, CAMT_PINTA; P93711, CAMT_POPKI; DR Q43095, CAMT_POPTM; Q8H9B6, CAMT_SOLTU; Q43161, CAMT_STELP; DR Q43237, CAMT_VITVI; Q41720, CAMT_ZINEL; // ID 2.1.1.105 DE N-benzoyl-4-hydroxyanthranilate 4-O-methyltransferase. CA S-adenosyl-L-methionine + N-benzoyl-4-hydroxyanthranilate = S-adenosyl- CA L-homocysteine + N-benzoyl-4-methoxyanthranilate. CC -!- Involved in the biosynthesis of phytoalexins. // ID 2.1.1.106 DE Tryptophan 2-C-methyltransferase. CA S-adenosyl-L-methionine + L-tryptophan = S-adenosyl-L-homocysteine + CA L-2-methyltryptophan. CC -!- D-tryptophan and indole-3-pyruvate can also act as acceptors, more CC slowly. // ID 2.1.1.107 DE Uroporphyrin-III C-methyltransferase. AN Urogen III methylase. AN SUMT. AN Uroporphyrinogen III methylase. CA 2 S-adenosyl-L-methionine + uroporphyrin III = 2 S-adenosyl-L- CA homocysteine + sirohydrochlorin. CC -!- Involved in the biosynthesis of siroheme and cobalamin. PR PROSITE; PDOC00656; DR P57500, CYSG_BUCAI; P11098, CYSG_ECOLI; P57001, CYSG_NEIMA; DR P95370, CYSG_NEIMB; P25924, CYSG_SALTY; Q59294, HEM4_CLOJO; DR P09127, HEMX_ECOLI; Q51887, HEMX_PROMI; P42437, NASF_BACSU; DR Q51701, NIRE_PARDE; P29928, SUMT_BACME; O19889, SUMT_CYACA; DR P29564, SUMT_METIV; P21631, SUMT_PSEDE; P37725, SUMT_PSEFL; DR O74468, SUMT_SCHPO; P42451, SUMT_SYNP7; Q55749, SUMT_SYNY3; DR P36150, SUMT_YEAST; // ID 2.1.1.108 DE 6-hydroxymellein O-methyltransferase. CA S-adenosyl-L-methionine + 6-hydroxymellein = S-adenosyl-L-homocysteine + CA 6-methoxymellein. CC -!- 3,4-dehydro-6-hydroxymellein can also act as acceptor. CC -!- 6-methoxymellein is a phytoalexin produced by carrot tissue. // ID 2.1.1.109 DE Demethylsterigmatocystin 6-O-methyltransferase. CA S-adenosyl-L-methionine + 6-demethylsterigmatocystin = S-adenosyl- CA L-homocysteine + sterigmatocystin. CC -!- Dihydrodemethylsterigmatocystin can also act as acceptor. CC -!- Involved in the biosynthesis of aflatoxins in fungi. // ID 2.1.1.110 DE Sterigmatocystin 7-O-methyltransferase. CA S-adenosyl-L-methionine + sterigmatocystin = S-adenosyl-L-homocysteine + CA 7-O-methylsterigmatocystin. CC -!- Dihydrosterigmatocystin can also act as acceptor. CC -!- Involved in the biosynthesis of aflatoxins in fungi. DR P55790, OMTA_ASPFL; Q12120, OMTA_ASPPA; // ID 2.1.1.111 DE Anthranilate N-methyltransferase. CA S-adenosyl-L-methionine + anthranilate = S-adenosyl-L-homocysteine + CA N-methylanthranilate. CC -!- Involved in the biosynthesis of acridine alkaloids in plant tissues. // ID 2.1.1.112 DE Glucuronoxylan 4-O-methyltransferase. CA S-adenosyl-L-methionine + glucuronoxylan D-glucuronate = S-adenosyl- CA L-homocysteine + glucuronoxylan 4-O-methyl-D-glucuronate. // ID 2.1.1.113 DE Site-specific DNA-methyltransferase (cytosine-N(4)-specific). AN N(4)-cytosine-specific DNA methylase. AN Modification methylase. AN Restriction-modification system. CA S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine CA + DNA N(4)-methylcytosine. CC -!- This is a large group of enzymes, the majority of which, with CC enzymes of similar site specificity listed as EC 3.1.21.3, CC EC 3.1.21.4 and EC 3.1.21.5, form so-called restriction- CC modification systems. CC -!- See the REBASE database for a complete list of these enzymes: CC http://www.neb.com/rebase/ PR PROSITE; PDOC00088; DR P70802, MTA1_ANASP; P23941, MTB1_BACAM; P70986, MTB1_BACST; DR O68556, MTB1_BACSU; P18051, MTB2_BACAM; Q45489, MTB2_BACSU; DR Q04845, MTC1_CITFR; P14243, MTC9_CITFR; P29568, MTHZ_METTF; DR Q58392, MTM1_METJA; Q58843, MTM2_METJA; Q58893, MTM5_METJA; DR Q58606, MTM6_METJA; P14244, MTMV_MICVA; O59647, MTMW_METWO; DR P11409, MTP2_PROVU; O52692, MTS1_STRCS; O52513, MTS1_STRFI; DR P14230, MTSM_SERMA; P30774, MTX1_XANCC; // ID 2.1.1.114 DE Hexaprenyldihydroxybenzoate methyltransferase. AN 3,4-dihydroxy-5-hexaprenylbenzoate methyltransferase. AN Dihydroxyhexaprenylbenzoate methyltransferase. AN DHHB methyltransferase. AN DHHB-Mt. CA S-adenosyl-L-methionine + 3-hexaprenyl-4,5-dihydroxybenzoate = CA S-adenosyl-L-homocysteine + 3-hexaprenyl-4-hydroxy-5-methoxybenzoate. CC -!- Involved in the pathway of ubiquinone synthesis. DR O49354, COQ3_ARATH; O93995, COQ3_CANAL; Q9NZJ6, COQ3_HUMAN; DR Q63159, COQ3_RAT ; O74421, COQ3_SCHPO; P27680, COQ3_YEAST; // ID 2.1.1.115 DE (R,S)-1-benzyl-1,2,3,4-tetrahydroisoquinoline N-methyltransferase. AN (R,S)-tetrahydrobenzylisoquinoline N-methyltransferase. AN Norreticuline N-methyltransferase. CA S-adenosyl-L-methionine + (R,S)-1-benzyl-1,2,3,4-tetrahydroisoquinoline = CA S-adenosyl-L-homocysteine + N-methyl-(R,S)-1-benzyl-1,2,3,4- CA tetrahydroisoquinoline. CC -!- Broad substrate specificity for (R,S)-1-benzyl-1,2,3,4- CC tetrahydroisoquinolines; including coclaurine, norcoclaurine, CC isococlaurine, norarmepavine, norreticuline and tetrahydropapaverine. CC -!- Both R- and S-enantiomers are methylated. CC -!- Participates in the pathway leading to benzylisoquinoline alkaloid CC synthesis in plants. The physiological substrate is likely to be CC coclaurine. CC -!- Was earlier termed norreticuline N-methyltransferase. However, CC norreticuline has not been found to occur in nature and that name CC does not reflect the broad specificity of the enzyme for (R,S)-1- CC benzyl-1,2,3,4-tetrahydroisoquinolines. // ID 2.1.1.116 DE 3'-hydroxy-N-methyl-(S)-coclaurine 4'-O-methyltransferase. CA S-adenosyl-L-methionine + 3'-hydroxy-N-methyl-(S)-coclaurine = CA S-adenosyl-L-homocysteine + (S)-reticuline. CC -!- Involved in isoquinoline alkaloid metabolism in plants. CC -!- Has also been shown to catalyze the methylation of (R,S)- CC laudanosoline, (S)-3'-hydroxycoclaurine and (R,S)-7-O- CC methylnoraudanosoline. DR Q9LEL5, 4OMT_COPJA; // ID 2.1.1.117 DE (S)-scoulerine 9-O-methyltransferase. CA S-adenosyl-L-methionine + (S)-scoulerine = S-adenosyl-L-homocysteine + CA (S)-tetrahydrocolumbamine. CC -!- The product of this reaction is a precursor for protoberberine CC alkaloids in plants. DR Q39522, SMT_COPJA ; // ID 2.1.1.118 DE Columbamine O-methyltransferase. CA S-adenosyl-L-methionine + columbamine = S-adenosyl-L-homocysteine + CA palmatine. CC -!- The product of this reaction is a protoberberine alkaloid that is CC widely distributed in the plant kingdom. CC -!- Distinct in specificity from EC 2.1.1.88. // ID 2.1.1.119 DE 10-hydroxydihydrosanguinarine 10-O-methyltransferase. CA S-adenosyl-L-methionine + 10-hydroxydihydrosanguinarine = S-adenosyl-L- CA homocysteine + dihydrochelirubine. CC -!- Part of the pathway for synthesis of benzophenanthridine alkaloids CC in plants. // ID 2.1.1.120 DE 12-hydroxydihydrochelirubine 12-O-methyltransferase. CA S-adenosyl-L-methionine + 12-hydroxydihydrochelirubine = S-adenosyl-L- CA homocysteine + dihydromacarpine. CC -!- Part of the pathway for synthesis of benzophenanthridine alkaloid CC macarpine in plants. // ID 2.1.1.121 DE 6-O-methylnorlaudanosoline 5'-O-methyltransferase. CA S-adenosyl-L-methionine + 6-O-methylnorlaudanosoline = S-adenosyl-L- CA homocysteine + nororientaline. CC -!- Nororientaline is a precursor of the alkaloid papaverine. // ID 2.1.1.122 DE (S)-tetrahydroprotoberberine N-methyltransferase. AN Tetrahydroprotoberberine cis-N-methyltransferase. CA S-adenosyl-L-methionine + (S)-7,8,13,14-tetrahydroprotoberberine = CA S-adenosyl-L-homocysteine + cis-N-methyl-(S)-7,8,13,14- CA tetrahydroprotoberberine. CC -!- Involved in the biosynthesis of isoquinoline alkaloids in plants. // ID 2.1.1.123 DE [Cytochrome-c]-methionine S-methyltransferase. CA S-adenosyl-L-methionine + [cytochrome c]-methionine = S-adenosyl-L- CA homocysteine + [cytochrome c]-S-methyl-methionine. // ID 2.1.1.124 DE [Cytochrome-c]-arginine N-methyltransferase. CA S-adenosyl-L-methionine + [cytochrome c]-arginine = S-adenosyl-L- CA homocysteine + [cytochrome c]-N-methyl-arginine. CC -!- Formerly EC 2.1.1.23. // ID 2.1.1.125 DE Histone-arginine N-methyltransferase. AN Histone protein methylase. AN Protein-arginine N-methyltransferase. AN Protein methylase I. CA S-adenosyl-L-methionine + histone-arginine = S-adenosyl-L-homocysteine + CA histone-N-methyl-arginine. CC -!- Forms the N(w)-monomethyl- and the N(w),N'(w)-dimethyl-, but not CC the N(w),N(w)-dimethyl-arginine derivatives. CC -!- The name protein methylase I is misleading since it has been used for CC a number of enzymes with different specificities. CC -!- Formerly EC 2.1.1.23. // ID 2.1.1.126 DE [Myelin basic protein]-arginine N-methyltransferase. AN Myelin basic protein methylase. AN Protein-arginine N-methyltransferase. AN Protein methylase I. CA S-adenosyl-L-methionine + [myelin basic protein]-arginine = S-adenosyl-L- CA homocysteine + [myelin basic protein]-N-methyl-arginine. CC -!- Forms the N(w)-monomethyl-, N(w),N'(w)-dimethyl- and N(w),N(w)- CC dimethyl-arginine derivatives. CC -!- The name protein methylase I is misleading since it has been used for CC a number of enzymes with different specificities. CC -!- Formerly EC 2.1.1.23. // ID 2.1.1.127 DE [Ribulose-bisphosphate-carboxylase]-lysine N-methyltransferase. AN Ribulose-bisphosphate-carboxylase/oxygenase N-methyltransferase. AN RuBisCO methyltransferase. AN RuBisCO LSMT. CA S-adenosyl-L-methionine + [ribulose-1,5-bisphosphate-carboxylase]- CA lysine = S-adenosyl-L-homocysteine + [ribulose-1,5-bisphosphate- CA carboxylase]-N(6)-methyl-L-lysine. CC -!- The enzyme methylates Lys-14 in the large subunits of hexadecameric CC higher plant EC 4.1.1.39. DR Q9XI84, RBMT_ARATH; Q43088, RBMT_PEA ; P94026, RBMT_TOBAC; // ID 2.1.1.128 DE (R,S)-norcoclaurine 6-O-methyltransferase. CA S-adenosyl-L-methionine + (R,S)-norcoclaurine = S-adenosyl-L-homocysteine CA + (R,S)-coclaurine. CC -!- Norcoclaurine is 6,7-dihydroxy-1-[(4-hydroxyphenyl)methyl]-1,2,3,4- CC tetrahydroisoquinoline. CC -!- The enzyme will also catalyze the 6-O-methylation of (R,S)- CC norlaudanosoline to form 6-O-methyl-norlaudanosoline, but this CC alkaloid has not been found to occur in plants. DR Q9LEL6, 6OMT_COPJA; // ID 2.1.1.129 DE Inositol 4-methyltransferase. AN Myo-inositol 4-O-methyltransferase. AN S-adenosyl-L-methionine:myo-inositol 4-O-methyltransferase. AN Myo-inositol 6-O-methyltransferase. CA S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + CA 1D-4-O-methyl-myo-inositol. CC -!- The enzyme from Vigna umbellata is highly specific for S-adenosyl-L- CC methionine. CC -!- The enzyme also methylates 1L-1,2,4/3,5-cyclohexanepentol, 2,4,6/3,5- CC pentahydroxycyclohexanone, D,L-2,3,4,6/5-pentacyclohexanone and 2,2'- CC anhydro-2-C-hydroxymethyl-myo-inositol, but at lower rates than that CC of myo-inositol. CC -!- Formerly EC 2.1.1.134. DR P45986, IMT1_MESCR; // ID 2.1.1.130 DE Precorrin-2 C20-methyltransferase. AN S-adenosyl-L-methionine--precorrin-2 methyltransferase. CA S-adenosyl-L-methionine + precorrin-2 = S-adenosyl-L-homocysteine + CA precorrin-3A. DR Q05593, CBIL_SALTY; Q10677, COBI_MYCTU; P21639, COBI_PSEDE; // ID 2.1.1.131 DE Precorrin-3B C17-methyltransferase. AN Precorrin-3 methyltransferase. AN Precorrin-3 methylase. CA S-adenosyl-L-methionine + precorrin-3B = S-adenosyl-L-homocysteine + CA precorrin 4. DR Q05590, CBIH_SALTY; O29534, COBJ_ARCFU; Q58223, COBJ_METJA; DR O27454, COBJ_METTH; P21640, COBJ_PSEDE; // ID 2.1.1.132 DE Precorrin-6Y C5,15-methyltransferase (decarboxylating). AN Precorrin-6 methyltransferase. AN Precorrin-6Y methylase. CA 2 S-adenosyl-L-methionine + precorrin-6Y = 2 S-adenosyl-L-homocysteine + CA precorrin-8X + CO(2). CC -!- The enzyme from Pseudomonas denitrificans has S-adenosyl-L- CC methionine-dependent methyltransferase and decarboxylase activities. DR Q05629, CBIE_SALTY; Q58917, COBL_METJA; Q10671, COBL_MYCTU; DR P21921, COBL_PSEDE; // ID 2.1.1.133 DE Precorrin-4 C11-methyltransferase. AN Precorrin-3 methylase. CA S-adenosyl-L-methionine + precorrin-4 = S-adenosyl-L-homocysteine + CA precorrin 5. CC -!- Catalyzes the methylation of C-11 in precorrin-4 to form precorrin-5. DR Q05630, CBIF_SALTY; Q10672, COBM_MYCTU; P21922, COBM_PSEDE; DR O68100, COBM_RHOCA; Q53138, COBM_RHOER; // ID 2.1.1.134 DE Transferred entry: 2.1.1.129. // ID 2.1.1.135 DE [Methionine synthase]-cobalamin methyltransferase (cob(II)alamin DE reducing). AN Methionine synthase cob(II)alamin reductase (methylating). AN Methionine synthase reductase. CA [Methionine synthase]-cob(II)alamin + NADPH + S-adenosyl methionine = CA [methionine synthase]-methylcob(I)alamin + S-adenosylhomocysteine + CA NADP(+). CF Flavoprotein. CC -!- Electrons are probably transferred from NADPH to FAD to FMN. DR Q17574, MTRR_CAEEL; Q9UBK8, MTRR_HUMAN; // ID 2.1.1.136 DE Chlorophenol O-methyltransferase. AN Halogenated phenol O-methyltransferase. AN Trichlorophenol O-methyltransferase. CA S-adenosyl-L-methionine + trichlorophenol = S-adenosyl-L-homocysteine + CA trichloroanisole. CC -!- The enzyme from Trichoderma virgatum, when cultured in the presence CC of halogenated phenol, also acts on a range of mono-, di- and CC trichlorophenols. // ID 2.1.1.137 DE Arsenite methyltransferase. CA S-adenosyl-L-methionine + arsenite = S-adenosyl-L-homocysteine + CA methylarsonate. CC -!- An enzyme of the biotransformation pathway that forms CC methylarsonate from inorganic arsenite. // ID 2.1.1.138 DE Methylarsonite methyltransferase. CA S-adenosyl-L-methionine + methylarsonite = S-adenosyl-L-homocysteine + CA dimethylarsinate. CC -!- The dimethylarsinic acid formed is a less toxic product in the CC pathway that starts with and biotransforms toxic arsenate. // ID 2.1.1.139 DE 3'-demethylstaurosporine O-methyltransferase. AN 3'-demethoxy-3'-hydroxystaurosporine O-methyltransferase. AN Staurosporine synthase. CA S-adenosyl-L-methionine + 3'-demethylstaurosporine = S-adenosyl-L- CA homocysteine + staurosporine. CC -!- Catalyzes the final step in the biosynthesis of staurosporine, an CC alkaloidal antibiotic that is a potent inhibitor of protein kinases, CC especially protein kinase C. // ID 2.1.1.140 DE (S)-coclaurine-N-methyltransferase. CA S-adenosyl-L-methionine + (S)-coclaurine = S-adenosyl-L-homocysteine + CA (S)-N-methylcoclaurine. CC -!- The enzyme is specific for the (S)-isomer of coclaurine. CC -!- Norcoclaurine can also act as an acceptor. // ID 2.1.1.141 DE Jasmonate O-methyltransferase. AN Jasmonic acid carboxyl methyltransferase. CA S-adenosyl-L-methionine + jasmonate = S-adenosyl-L-homocysteine + CA methyljasmonate. CC -!- 9,10-Dihydrojasmonic acid is a poor substrate for the enzyme. CC -!- The enzyme does not convert 12-oxo-phytodienoic acid (a precursor CC of jasmonic acid), salicylic acid, benzoic acid, linolenic acid or CC cinnamic acid into their corresponding methyl esters. CC -!- Enzyme activity is inhibited by the presence of divalent cations, CC e.g., Ca(2+), Cu(2+), Mg(2+) and Zn(2+). // ID 2.1.1.142 DE Cycloartenol 24-C-methyltransferase. AN Sterol C-methyltransferase. CA S-adenosyl-L-methionine + cycloartenol = S-adenosyl-L-homocysteine + CA (24R)-24-methylcycloarta-8,25-dien-3-beta-ol. CC -!- S-Adenosyl-L-methionine methylates the Si face of the 24(25)- CC double bond with elimination of a hydrogen atom from the pro-Z CC methyl group at C-25. // ID 2.1.1.143 DE 24-methylenesterol C-methyltransferase. AN SMT2. AN 24-methylenelophenol C-24(1)-methyltransferase. CA S-adenosyl-L-methionine + 24-methylenelophenol = S-adenosyl-L- CA homocysteine + (Z)-24-ethylidenelophenol. CC -!- This is the second methylation step of plant sterol biosynthesis CC (cf EC 2.1.1.142). // ID 2.1.1.144 DE Trans-aconitate 2-methyltransferase. CA S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine + CA (E)-3-(methoxycarbonyl)pent-2-enedioate. CC -!- Also catalyzes the formation of the methyl monoester of cis- CC aconitate, isocitrate and citrate, but more slowly. CC -!- While the enzyme from Escherichia coli forms (E)-3- CC (methoxycarbonyl)-pent-2-enedioate as the product, that from CC Saccharomyces cerevisiae forms (E)-2-(methoxycarbonylmethyl) CC butenedioate and is therefore classified as a separate enzyme CC (cf. EC 2.1.1.145). DR Q8UH15, TAM_AGRT5 ; Q8YI91, TAM_BRUME ; Q9RX93, TAM_DEIRA ; DR Q8XAZ2, TAM_ECO57 ; P76145, TAM_ECOLI ; O53698, TAM_MYCTU ; DR Q9I0S1, TAM_PSEAE ; Q98K73, TAM_RHILO ; Q92RC5, TAM_RHIME ; DR Q9K3T2, TAM_STRCO ; Q8ZDP7, TAM_YERPE ; // ID 2.1.1.145 DE Trans-aconitate 3-methyltransferase. CA S-adenosyl-L-methionine + trans-aconitate = S-adenosyl-L-homocysteine CA + (E)-2-(methoxycarbonylmethyl)butenedioate. CC -!- Also catalyzes the formation of the methyl monoester of CC cis-aconitate, isocitrate and citrate, but more slowly. CC -!- While the enzyme from Saccharomyces cerevisiae forms (E)-2- CC (methoxycarbonylmethyl)butenedioate as the product, that from CC Escherichia coli forms (E)-3-(methoxycarbonyl)-pent-2-enedioate CC and is therefore classified as a separate enzyme (cf. CC EC 2.1.1.144). // ID 2.1.1.146 DE (Iso)eugenol O-methyltransferase. CA S-adenosyl-L-methionine + isoeugenol = S-adenosyl-L-homocysteine + CA isomethyleugenol. CC -!- Acts on eugenol and chavicol as well as isoeugenol. // ID 2.1.1.147 DE Corydaline synthase. CA S-adenosyl-L-methionine + palmatine + 2 NADP(H) = S-adenosyl-L- CA homocysteine + corydaline + 2 NADP(+). CC -!- Also acts on 7,8-dihydropalmatine. // ID 2.1.2.1 DE Glycine hydroxymethyltransferase. AN Serine hydroxymethyltransferase. AN Serine aldolase. AN Threonine aldolase. AN Serine hydroxymethylase. CA 5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + CA L-serine. CF Pyridoxal-phosphate. CC -!- Also catalyzes the reaction of glycine with acetaldehyde to form CC L-threonine, and with 4-trimethylammoniobutanal to form 3-hydroxy- CC N(6),N(6),N(6)-trimethyl-L-lysine. PR PROSITE; PDOC00090; DR O53441, GLA1_MYCTU; Q9HTE9, GLA1_PSEAE; Q88R12, GLA1_PSEPK; DR Q88AD1, GLA1_PSESM; Q8Y1G1, GLA1_RALSO; Q983B6, GLA1_RHILO; DR Q92QU6, GLA1_RHIME; Q9KTG1, GLA1_VIBCH; Q87RR2, GLA1_VIBPA; DR Q8DFC9, GLA1_VIBVU; O53615, GLA2_MYCTU; Q9I138, GLA2_PSEAE; DR Q88Q27, GLA2_PSEPK; Q87WC1, GLA2_PSESM; Q8XTQ1, GLA2_RALSO; DR Q98A81, GLA2_RHILO; Q92XS8, GLA2_RHIME; Q8Z2Z9, GLA2_SALTI; DR Q9KMP4, GLA2_VIBCH; Q87I03, GLA2_VIBPA; Q8D7G5, GLA2_VIBVU; DR Q9HVI7, GLA3_PSEAE; O85718, GLYA_ACIRA; P34894, GLYA_ACTAC; DR Q9YAH7, GLYA_AERPE; Q8YMW8, GLYA_ANASP; O66776, GLYA_AQUAE; DR O29406, GLYA_ARCFU; Q9K6G4, GLYA_BACHD; P39148, GLYA_BACSU; DR O51547, GLYA_BORBU; P24060, GLYA_BRAJA; Q8G1F1, GLYA_BRUSU; DR P57376, GLYA_BUCAI; Q8K9P2, GLYA_BUCAP; P59432, GLYA_BUCBP; DR P24531, GLYA_CAMJE; Q9A8J6, GLYA_CAUCR; Q9PJW0, GLYA_CHLMU; DR Q9Z831, GLYA_CHLPN; O84439, GLYA_CHLTR; Q97GV1, GLYA_CLOAB; DR Q8XJ32, GLYA_CLOPE; Q8FQR1, GLYA_COREF; Q93PM7, GLYA_CORGL; DR P50434, GLYA_CORS1; Q9RYB2, GLYA_DEIRA; Q8XA55, GLYA_ECO57; DR P00477, GLYA_ECOLI; P43844, GLYA_HAEIN; Q9HPY5, GLYA_HALN1; DR Q9ZMP7, GLYA_HELPJ; P56089, GLYA_HELPY; P34895, GLYA_HYPME; DR Q9CHW7, GLYA_LACLA; Q927V4, GLYA_LISIN; Q8Y4B2, GLYA_LISMO; DR Q8TK94, GLYA_METAC; P50435, GLYA_METEX; Q58992, GLYA_METJA; DR Q8TZ19, GLYA_METKA; Q8PZQ0, GLYA_METMA; O27433, GLYA_METTH; DR P50436, GLYA_METTM; P47634, GLYA_MYCGE; Q9X794, GLYA_MYCLE; DR P78011, GLYA_MYCPN; Q98QM2, GLYA_MYCPU; Q9XB01, GLYA_NEIGO; DR Q9XAY7, GLYA_NEIMA; P56990, GLYA_NEIMB; Q9XAZ1, GLYA_NEIMC; DR Q8EM73, GLYA_OCEIH; P57830, GLYA_PASMU; Q9V1B2, GLYA_PYRAB; DR Q8ZYF9, GLYA_PYRAE; Q8U039, GLYA_PYRFU; O59347, GLYA_PYRHO; DR Q92GH7, GLYA_RICCN; O08370, GLYA_RICPR; P06192, GLYA_SALTY; DR Q8EBN8, GLYA_SHEON; Q99SE5, GLYA_STAAM; Q8CRN3, GLYA_STAEP; DR O86565, GLYA_STRCO; Q8K7H8, GLYA_STRP3; Q8P122, GLYA_STRP8; DR Q97R16, GLYA_STRPN; Q99ZP1, GLYA_STRPY; Q8DPZ0, GLYA_STRR6; DR Q9UWT5, GLYA_SULSO; Q971K4, GLYA_SULTO; Q8DH33, GLYA_SYNEL; DR P77962, GLYA_SYNY3; Q9HI38, GLYA_THEAC; Q9WZH9, GLYA_THEMA; DR Q8R887, GLYA_THETN; Q97CQ5, GLYA_THEVO; O83349, GLYA_TREPA; DR Q8D253, GLYA_WIGBR; Q8PPE3, GLYA_XANAC; Q8PCN4, GLYA_XANCP; DR Q9PET2, GLYA_XYLFA; Q87AS2, GLYA_XYLFT; Q8ZCR1, GLYA_YERPE; DR P50432, GLYC_CAEEL; O13426, GLYC_CANAL; O62585, GLYC_ENCCU; DR P34896, GLYC_HUMAN; P50431, GLYC_MOUSE; P34898, GLYC_NEUCR; DR P07511, GLYC_RABIT; Q10104, GLYC_SCHPO; P35623, GLYC_SHEEP; DR P37291, GLYC_YEAST; O13972, GLYD_SCHPO; O13425, GLYM_CANAL; DR P49357, GLYM_FLAPR; P34897, GLYM_HUMAN; P34899, GLYM_PEA ; DR P14519, GLYM_RABIT; P50433, GLYM_SOLTU; P37292, GLYM_YEAST; DR P49358, GLYN_FLAPR; // ID 2.1.2.2 DE Phosphoribosylglycinamide formyltransferase. AN 5'-phosphoribosylglycinamide transformylase. AN GAR transformylase. AN GART. AN 2-amino-N-ribosylacetamide 5'-phosphate transformylase. AN GAR formyltransferase. AN Glycinamide ribonucleotide transformylase. AN GAR TFase. AN 5,10-methenyltetrahydrofolate:2-amino-N-ribosylacetamide AN ribonucleotide transformylase. CA 10-formyltetrahydrofolate + N(1)-(5-phospho-D-ribosyl)glycinamide = CA tetrahydrofolate + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide. PR PROSITE; PDOC00319; DR P21872, PUR2_CHICK; Q26255, PUR2_CHITE; P00967, PUR2_DROME; DR P16340, PUR2_DROPS; P22102, PUR2_HUMAN; Q64737, PUR2_MOUSE; DR P52422, PUR3_ARATH; P12040, PUR3_BACSU; P08179, PUR3_ECOLI; DR P43846, PUR3_HAEIN; Q9UUK7, PUR3_SCHPO; Q42805, PUR3_SOYBN; DR P52423, PUR3_VIGUN; P04161, PUR3_YEAST; // ID 2.1.2.3 DE Phosphoribosylaminoimidazolecarboxamide formyltransferase. AN 5-amino-4-imidazolecarboxamide ribonucleotide transformylase. AN 10-formyltetrahydrofolate:5'-phosphoribosyl-5-amino-4-imidazolecarboxamide AN formyltransferase. AN 5'-phosphoribosyl-5-amino-4-imidazolecarboxamide formyltransferase. AN 5-amino-1-ribosyl-4-imidazolecarboxamide 5'-phosphate transformylase. AN 5-amino-4-imidazolecarboxamide ribotide transformylase. AN Aminoimidazolecarboxamide ribonucleotide transformylase. AN AICAR transformylase. AN AICAR formyltransferase. CA 10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D- CA ribosyl)imidazole-4-carboxamide = tetrahydrofolate + CA 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. DR P54113, PU91_YEAST; P38009, PU92_YEAST; Q8UBM8, PUR9_AGRT5; DR Q8YSJ2, PUR9_ANASP; O67775, PUR9_AQUAE; Q9KF53, PUR9_BACHD; DR P12048, PUR9_BACSU; Q8A155, PUR9_BACTN; Q8G6B1, PUR9_BIFLO; DR Q89WU7, PUR9_BRAJA; Q8YJ53, PUR9_BRUME; P57143, PUR9_BUCAI; DR Q8KA70, PUR9_BUCAP; Q89B23, PUR9_BUCBP; Q9PNY2, PUR9_CAMJE; DR Q9ABY4, PUR9_CAUCR; P31335, PUR9_CHICK; Q8KFK6, PUR9_CHLTE; DR Q46480, PUR9_CHRVI; Q97J91, PUR9_CLOAB; Q8XMK2, PUR9_CLOPE; DR Q892X3, PUR9_CLOTE; Q9RHX6, PUR9_CORAM; Q8FR29, PUR9_COREF; DR Q8NS21, PUR9_CORGL; Q9RW01, PUR9_DEIRA; Q8X611, PUR9_ECO57; DR Q8FB68, PUR9_ECOL6; P15639, PUR9_ECOLI; Q8REV6, PUR9_FUSNN; DR P43852, PUR9_HAEIN; P31939, PUR9_HUMAN; Q9CFG0, PUR9_LACLA; DR Q88U29, PUR9_LACPL; Q8F3W6, PUR9_LEPIN; Q92AP3, PUR9_LISIN; DR Q8Y6C5, PUR9_LISMO; Q9CWJ9, PUR9_MOUSE; Q9Z5H5, PUR9_MYCLE; DR Q9RAJ5, PUR9_MYCPA; P71553, PUR9_MYCTU; Q9JUQ8, PUR9_NEIMA; DR Q9JZM7, PUR9_NEIMB; Q8CXK7, PUR9_OCEIH; P57828, PUR9_PASMU; DR Q9HUV9, PUR9_PSEAE; Q88DK3, PUR9_PSEPK; Q87VR9, PUR9_PSESM; DR Q8Y232, PUR9_RALSO; Q98ES7, PUR9_RHILO; Q92KX6, PUR9_RHIME; DR Q8Z335, PUR9_SALTI; P26978, PUR9_SALTY; O74928, PUR9_SCHPO; DR Q8EJM1, PUR9_SHEON; Q99V24, PUR9_STAAM; Q8NX88, PUR9_STAAW; DR Q8CT27, PUR9_STAEP; Q8E7W6, PUR9_STRA3; Q9KY50, PUR9_STRCO; DR Q8DWK8, PUR9_STRMU; Q8K8Y6, PUR9_STRP3; Q8P310, PUR9_STRP8; DR Q97T99, PUR9_STRPN; Q8DRM1, PUR9_STRR6; Q9F1T4, PUR9_STRSU; DR Q8DIN5, PUR9_SYNEL; P74741, PUR9_SYNY3; Q9X0X6, PUR9_THEMA; DR Q8RC55, PUR9_THETN; Q9KV80, PUR9_VIBCH; Q87KT0, PUR9_VIBPA; DR Q8DD06, PUR9_VIBVU; Q8D244, PUR9_WIGBR; Q8PQ19, PUR9_XANAC; DR Q8PD47, PUR9_XANCP; Q9PC10, PUR9_XYLFA; Q87D58, PUR9_XYLFT; DR Q8ZAR3, PUR9_YERPE; // ID 2.1.2.4 DE Glycine formimidoyltransferase. AN Formiminoglycine formiminotransferase. AN FIG formiminotransferase. AN Glycine formiminotransferase. CA 5-formimidoyltetrahydrofolate + glycine = tetrahydrofolate + CA N-formimidoylglycine. // ID 2.1.2.5 DE Glutamate formimidoyltransferase. AN Glutamate formiminotransferase. AN Glutamate formyltransferase. AN Formiminoglutamic acid transferase. AN Formiminoglutamic formiminotransferase. CA 5-formimidoyltetrahydrofolate (or 5-formyltetrahydrofolate) + CA L-glutamate = tetrahydrofolate + N-formimidoyl-L-glutamate (or CA N-formyl-L-glutamate). CF Pyridoxal-phosphate. CC -!- In eukaryotes occurs as a bifunctional enzyme also having CC EC 4.3.1.4 activity. CC -!- Formerly EC 2.1.2.6. DI Formiminotransferase deficiency (figluuria); MIM:229100. DR O95954, FTCD_HUMAN; Q91XD4, FTCD_MOUSE; P53603, FTCD_PIG ; DR O88618, FTCD_RAT ; // ID 2.1.2.6 DE Transferred entry: 2.1.2.5. // ID 2.1.2.7 DE D-alanine hydroxymethyltransferase. AN 2-methylserine hydroxymethyltransferase. CA 5,10-methylenetetrahydrofolate + D-alanine + H(2)O = tetrahydrofolate + CA 2-methylserine. CC -!- Also acts on 2-hydroxymethylserine. // ID 2.1.2.8 DE Deoxycytidylate hydroxymethyltransferase. AN Deoxycytidylate hydroxymethylase. AN dCMP hydroxymethylase. CA 5,10-methylenetetrahydrofolate + H(2)O + deoxycytidylate = CA tetrahydrofolate + 5-hydroxymethyldeoxycytidylate. DR P18029, DCHM_BPT2 ; P08773, DCHM_BPT4 ; P18030, DCHM_BPT6 ; // ID 2.1.2.9 DE Methionyl-tRNA formyltransferase. AN N(10)-formyltetrahydrofolic-methionyl-transfer ribonucleic AN transformylase. AN Formylmethionyl-transfer ribonucleic synthetase. AN Methionyl ribonucleic formyltransferase. AN Methionyl-tRNA Met formyltransferase. AN Methionyl-tRNA transformylase. AN Methionyl-transfer RNA transformylase. AN Methionyl-transfer ribonucleate methyltransferase. AN Methionyl-transfer ribonucleic transformylase. CA 10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) + H(2)O = CA tetrahydrofolate + N-formylmethionyl-tRNA(fMet). PR PROSITE; PDOC00319; DR Q8UID0, FMT_AGRT5 ; Q8YRI6, FMT_ANASP ; O67890, FMT_AQUAE ; DR Q9K9Y6, FMT_BACHD ; P94463, FMT_BACSU ; O51091, FMT_BORBU ; DR O77480, FMT_BOVIN ; Q8YDB3, FMT_BRUME ; P57564, FMT_BUCAI ; DR Q8K974, FMT_BUCAP ; P59557, FMT_BUCBP ; Q9PJ28, FMT_CAMJE ; DR Q9ABE9, FMT_CAUCR ; Q9PJL2, FMT_CHLMU ; Q9Z7Q5, FMT_CHLPN ; DR Q8KCG8, FMT_CHLTE ; O84535, FMT_CHLTR ; O05101, FMT_CLOAB ; DR Q8XJL3, FMT_CLOPE ; Q8NQ47, FMT_CORGL ; Q9RRQ3, FMT_DEIRA ; DR Q8X8F1, FMT_ECO57 ; P23882, FMT_ECOLI ; Q8RDM3, FMT_FUSNN ; DR P44787, FMT_HAEIN ; Q9ZK72, FMT_HELPJ ; P56461, FMT_HELPY ; DR Q96DP5, FMT_HUMAN ; Q9CEE9, FMT_LACLA ; Q92AI5, FMT_LISIN ; DR Q8Y676, FMT_LISMO ; Q9D799, FMT_MOUSE ; P47605, FMT_MYCGE ; DR Q9CCQ0, FMT_MYCLE ; P75235, FMT_MYCPN ; Q98RG4, FMT_MYCPU ; DR P71674, FMT_MYCTU ; Q9JWY9, FMT_NEIMA ; Q9K1K6, FMT_NEIMB ; DR P57949, FMT_PASMU ; O85732, FMT_PSEAE ; Q8Y3A8, FMT_RALSO ; DR Q98D53, FMT_RHILO ; Q92SH5, FMT_RHIME ; O33509, FMT_RICAK ; DR O33508, FMT_RICAM ; O33510, FMT_RICAU ; O33520, FMT_RICCA ; DR O33519, FMT_RICCN ; O33523, FMT_RICFE ; O33535, FMT_RICMO ; DR O33543, FMT_RICPA ; P50932, FMT_RICPR ; O33545, FMT_RICRH ; DR O33544, FMT_RICRI ; O33575, FMT_RICSI ; O33582, FMT_RICTY ; DR Q8Z1X0, FMT_SALTI ; Q8ZLM6, FMT_SALTY ; Q9UTG6, FMT_SCHPO ; DR Q99UQ2, FMT_STAAM ; Q8NX18, FMT_STAAW ; Q9L0Y6, FMT_STRCO ; DR Q8K6E8, FMT_STRP3 ; Q8P003, FMT_STRP8 ; Q97PA6, FMT_STRPN ; DR Q99YM7, FMT_STRPY ; Q55163, FMT_SYNY3 ; Q9WYZ8, FMT_THEMA ; DR P43523, FMT_THETH ; Q8R9T1, FMT_THETN ; O83737, FMT_TREPA ; DR Q9PQ27, FMT_UREPA ; O87726, FMT_VIBAL ; Q9KVU4, FMT_VIBCH ; DR Q87KD4, FMT_VIBPA ; Q8DDE4, FMT_VIBVU ; Q8D259, FMT_WIGBR ; DR Q8PG21, FMT_XANAC ; Q8P4G0, FMT_XANCP ; Q9PEV1, FMT_XYLFA ; DR Q87AR0, FMT_XYLFT ; P32785, FMT_YEAST ; Q8ZJ80, FMT_YERPE ; // ID 2.1.2.10 DE Aminomethyltransferase. AN Glycine-cleavage system T-protein. AN Tetrahydrofolate aminomethyltransferase. CA (6S)-tetrahydrofolate + S-aminomethyldihydrolipoylprotein = CA (6R)-5,10-methylenetetrahydrofolate + NH(3) + dihydrolipoylprotein. CC -!- A component, with EC 1.4.4.2, of the glycine cleavage system, CC formerly known as glycine synthase. DI Nonketotic hyperglycinemia type I; MIM:238300. DR Q9YBA2, GCST_AERPE; Q8YNF7, GCST_ANASP; O67441, GCST_AQUAE; DR O65396, GCST_ARATH; Q9K934, GCST_BACHD; P54378, GCST_BACSU; DR Q89YZ6, GCST_BACTN; P25285, GCST_BOVIN; Q9TSZ7, GCST_CANFA; DR P28337, GCST_CHICK; Q8KBJ9, GCST_CHLTE; Q8XD32, GCST_ECO57; DR Q8FE65, GCST_ECOL6; P27248, GCST_ECOLI; O49849, GCST_FLAAN; DR P49363, GCST_FLAPR; O23936, GCST_FLATR; Q9HPJ7, GCST_HALN1; DR P48728, GCST_HUMAN; Q8F935, GCST_LEPIN; Q92C06, GCST_LISIN; DR Q8Y7D5, GCST_LISMO; P93256, GCST_MESCR; O32955, GCST_MYCLE; DR Q10376, GCST_MYCTU; Q9JVP2, GCST_NEIMA; Q9K0L8, GCST_NEIMB; DR Q8CXD9, GCST_OCEIH; P49364, GCST_PEA ; Q9HTX5, GCST_PSEAE; DR Q88CI7, GCST_PSEPK; Q88AS0, GCST_PSESM; Q9UZP8, GCST_PYRAB; DR Q8U185, GCST_PYRFU; O58888, GCST_PYRHO; Q8XUA0, GCST_RALSO; DR Q8XG67, GCST_SALTY; O14110, GCST_SCHPO; Q8EIQ8, GCST_SHEON; DR P54260, GCST_SOLTU; Q99TV7, GCST_STAAM; Q8CSF4, GCST_STAEP; DR O86567, GCST_STRCO; Q8DKV6, GCST_SYNEL; P54261, GCST_SYNY3; DR Q9WY54, GCST_THEMA; Q8RCV9, GCST_THETN; Q8PI37, GCST_XANAC; DR Q8P6T8, GCST_XANCP; Q9PGW5, GCST_XYLFA; Q87EZ6, GCST_XYLFT; DR P48015, GCST_YEAST; Q8ZHI6, GCST_YERPE; // ID 2.1.2.11 DE 3-methyl-2-oxobutanoate hydroxymethyltransferase. AN Alpha-ketoisovalerate hydroxymethyltransferase. AN Dehydropantoate hydroxymethyltransferase. AN Ketopantoate hydroxymethyltransferase. CA 5,10-methylenetetrahydrofolate + 3-methyl-2-oxobutanoate = CA tetrahydrofolate + 2-dehydropantoate. DR Q9I3C3, PAN1_PSEAE; Q9HV70, PAN2_PSEAE; Q9YE97, PANB_AERPE; DR Q8UA91, PANB_AGRT5; Q8YWS8, PANB_ANASP; O67783, PANB_AQUAE; DR Q9KC87, PANB_BACHD; P52996, PANB_BACSU; Q9AMS0, PANB_BRAJA; DR Q8YFD0, PANB_BRUME; P57293, PANB_BUCAI; Q8K9U6, PANB_BUCAP; DR Q9PIK1, PANB_CAMJE; Q8KCS2, PANB_CHLTE; Q97F39, PANB_CLOAB; DR Q8FUA5, PANB_COREF; Q9X712, PANB_CORGL; Q9RR81, PANB_DEIRA; DR Q8X929, PANB_ECO57; Q8FL30, PANB_ECOL6; P31057, PANB_ECOLI; DR Q9Y7B6, PANB_EMENI; Q9HPT6, PANB_HALN1; Q9ZM56, PANB_HELPJ; DR O25698, PANB_HELPY; Q8EZ98, PANB_LEPIN; Q92AA6, PANB_LISIN; DR Q8Y601, PANB_LISMO; Q9CBT0, PANB_MYCLE; Q10505, PANB_MYCTU; DR Q9L7B2, PANB_MYCVN; Q9JUY0, PANB_NEIMA; Q9JZW6, PANB_NEIMB; DR Q8ELF4, PANB_OCEIH; Q9ZEP8, PANB_PSEFL; Q9V0E1, PANB_PYRAB; DR Q8ZT69, PANB_PYRAE; Q8U1R2, PANB_PYRFU; O58665, PANB_PYRHO; DR Q8XW45, PANB_RALSO; Q98NC9, PANB_RHILO; Q92NN1, PANB_RHIME; DR Q8Z9D2, PANB_SALTI; Q8ZRR0, PANB_SALTY; Q09672, PANB_SCHPO; DR Q8EIG9, PANB_SHEON; Q931E6, PANB_STAAM; Q99R38, PANB_STAAN; DR Q8CR20, PANB_STAEP; Q9RKS2, PANB_STRCO; Q97W44, PANB_SULSO; DR Q974Y0, PANB_SULTO; Q8DM44, PANB_SYNEL; P52997, PANB_SYNY3; DR Q9X251, PANB_THEMA; Q9KUD0, PANB_VIBCH; Q87LV2, PANB_VIBPA; DR Q8DC11, PANB_VIBVU; Q8D2A5, PANB_WIGBR; Q8PLL1, PANB_XANAC; DR Q8P9T0, PANB_XANCP; Q9PGR9, PANB_XYLFA; Q87EW0, PANB_XYLFT; DR P38122, PANB_YEAST; Q8ZBK8, PANB_YERPE; // ID 2.1.3.1 DE Methylmalonyl-CoA carboxyltransferase. AN Transcarboxylase. CA (S)-2-methyl-3-oxopropanoyl-CoA + pyruvate = propanoyl-CoA + CA oxaloacetate. CF Biotin; Cobalt; Zinc. PR PROSITE; PDOC00167; // ID 2.1.3.2 DE Aspartate carbamoyltransferase. AN Aspartate transcarbamylase. AN Carbamylaspartotranskinase. AN ATCase. CA Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L- CA aspartate. PR PROSITE; PDOC00091; DR Q43086, PYB1_PEA ; Q43087, PYB2_PEA ; Q43064, PYB3_PEA ; DR P20054, PYR1_DICDI; P05990, PYR1_DROME; P27708, PYR1_HUMAN; DR P08955, PYR1_MESAU; Q09794, PYR1_SCHPO; Q91437, PYR1_SQUAC; DR P07259, PYR1_YEAST; Q9YBD4, PYRB_AERPE; Q8UFT9, PYRB_AGRT5; DR Q8YWD2, PYRB_ANASP; O66726, PYRB_AQUAE; P49077, PYRB_ARATH; DR O30130, PYRB_ARCFU; P41008, PYRB_BACCL; Q9K9V6, PYRB_BACHD; DR P05654, PYRB_BACSU; Q8YC62, PYRB_BRUME; P57450, PYRB_BUCAI; DR Q8K9H9, PYRB_BUCAP; Q9PNJ6, PYRB_CAMJE; Q9A5K4, PYRB_CAUCR; DR Q8KBI7, PYRB_CHLTE; Q97FS3, PYRB_CLOAB; Q8XL59, PYRB_CLOPE; DR Q8FT39, PYRB_COREF; Q8NQ38, PYRB_CORGL; Q9RVC0, PYRB_DEIRA; DR P00479, PYRB_ECOLI; Q9L4T8, PYRB_ENTFA; Q8RG89, PYRB_FUSNN; DR Q9HHN4, PYRB_HALN1; Q9ZM81, PYRB_HELPJ; O25716, PYRB_HELPY; DR Q9CF79, PYRB_LACLA; Q9L4N6, PYRB_LACLC; Q60252, PYRB_LACLE; DR P77883, PYRB_LACPL; Q92AH0, PYRB_LISIN; Q8Y662, PYRB_LISMO; DR Q8THL2, PYRB_METAC; Q58976, PYRB_METJA; Q8TVB2, PYRB_METKA; DR Q8PXK5, PYRB_METMA; O27464, PYRB_METTH; Q9CCR5, PYRB_MYCLE; DR P71808, PYRB_MYCTU; Q9JQU5, PYRB_NEIMA; Q59653, PYRB_PSEAE; DR P56585, PYRB_PSEFL; Q59711, PYRB_PSEPU; Q934T0, PYRB_PSYT1; DR P77918, PYRB_PYRAB; Q8ZYH7, PYRB_PYRAE; Q8U373, PYRB_PYRFU; DR O58451, PYRB_PYRHO; Q8Y1L2, PYRB_RALSO; Q98M86, PYRB_RHILO; DR Q92QL5, PYRB_RHIME; P08420, PYRB_SALTY; P19910, PYRB_SERMA; DR Q99UR8, PYRB_STAAM; Q9KXR2, PYRB_STRCO; Q8P1G1, PYRB_STRP8; DR Q97QE2, PYRB_STRPN; Q9A0C8, PYRB_STRPY; Q8DPH9, PYRB_STRR6; DR Q55338, PYRB_SULAC; Q9UX08, PYRB_SULSO; Q970X2, PYRB_SULTO; DR Q8DIM4, PYRB_SYNEL; P74163, PYRB_SYNY3; Q9HKM2, PYRB_THEAC; DR P96079, PYRB_THEAQ; P96111, PYRB_THEMA; Q8R9R5, PYRB_THETN; DR Q97B29, PYRB_THEVO; Q04595, PYRB_TREDE; Q9KP66, PYRB_VIBCH; DR Q87LF8, PYRB_VIBPA; P96174, PYRB_VIBS2; Q8DCF6, PYRB_VIBVU; DR Q8D293, PYRB_WIGBR; Q8PII1, PYRB_XANAC; Q8P767, PYRB_XANCP; DR Q9PBB8, PYRB_XYLFA; Q87C22, PYRB_XYLFT; Q8ZB39, PYRB_YERPE; // ID 2.1.3.3 DE Ornithine carbamoyltransferase. AN Ornithine transcarbamylase. AN Citrulline phosphorylase. AN OTCase. AN OTC. CA Carbamoyl phosphate + L-ornithine = phosphate + L-citrulline. CC -!- The plant enzyme also catalyzes the reactions of EC 2.1.3.6, CC EC 2.7.2.2 and EC 3.5.3.12, thus acting as putrescine synthase, CC converting agmatine and ornithine into putrescine and citrulline CC respectively. DI Ornithine transcarbamylase deficiency; MIM:311250. PR PROSITE; PDOC00091; DR P04391, OTC1_ECOLI; Q08016, OTC1_SALTY; P06960, OTC2_ECOLI; DR P18186, OTCA_BACSU; P57449, OTCA_BUCAI; P59100, OTCA_BUCAP; DR Q59283, OTCA_CORGL; O08322, OTCA_LACPL; Q02095, OTCA_MYCBO; DR Q9CC11, OTCA_MYCLE; P94991, OTCA_MYCTU; P11724, OTCA_PSEAE; DR Q02047, OTCA_PSESH; Q55497, OTCA_SYNY3; P96108, OTCA_THEMA; DR P96134, OTCA_THETH; P96172, OTCA_VIBS2; P11726, OTCC_AERPU; DR O86132, OTCC_BACLI; Q46169, OTCC_CLOPE; P44770, OTCC_HAEIN; DR P75473, OTCC_MYCPN; Q01322, OTCC_NEICI; Q01323, OTCC_NEIFL; DR P21302, OTCC_NEIGO; Q01324, OTCC_NEILA; Q9JTI4, OTCC_NEIMA; DR Q9JYI3, OTCC_NEIMB; Q01325, OTCC_NEIME; Q01326, OTCC_NEIMU; DR Q01327, OTCC_NEIPO; P57876, OTCC_PASMU; P08308, OTCC_PSEAE; DR P11727, OTCC_PSEPU; P23752, OTCC_PSESH; O31018, OTCC_RHIET; DR Q8P052, OTCC_STRP3; P16964, OTCC_STRPY; P81682, OTCX_STAEP; DR O50039, OTC_ARATH ; O29013, OTC_ARCFU ; P11066, OTC_ASPNG ; DR Q00291, OTC_ASPTE ; P11803, OTC_EMENI ; Q48296, OTC_HALN1 ; DR P00480, OTC_HUMAN ; Q58291, OTC_METJA ; O27495, OTC_METTH ; DR P11725, OTC_MOUSE ; P14995, OTC_PACTA ; Q43814, OTC_PEA ; DR O19072, OTC_PIG ; O93656, OTC_PYRAB ; Q51742, OTC_PYRFU ; DR O58457, OTC_PYRHO ; P31326, OTC_RANCA ; P00481, OTC_RAT ; DR P31317, OTC_SCHPO ; P78605, OTC_TRAHI ; P05150, OTC_YEAST ; // ID 2.1.3.4 DE Deleted entry. // ID 2.1.3.5 DE Oxamate carbamoyltransferase. AN Oxamic transcarbamylase. CA Carbamoyl phosphate + oxamate = phosphate + oxalureate. // ID 2.1.3.6 DE Putrescine carbamoyltransferase. CA Carbamoyl phosphate + putrescine = phosphate + N-carbamoylputrescine. CC -!- The plant enzyme also catalyzes the reactions of EC 2.1.3.3, CC EC 2.7.2.2 and EC 3.5.3.12, thus acting as putrescine synthase, CC converting agmatine and ornithine into putrescine and citrulline CC respectively. // ID 2.1.3.7 DE 3-hydroxymethylcephem carbamoyltransferase. CA Carbamoyl phosphate + a 3-hydroxymethylceph-3-em-4-carboxylate = CA phosphate + a 3-carbamoyloxymethylcephem. CC -!- Acts on a wide range of 3-hydroxymethylcephems (a subclass of the CC cephalosporin antibiotics). CC -!- Activated by ATP. // ID 2.1.3.8 DE Lysine carbamoyltransferase. AN Lysine transcarbamylase. CA Carbamoyl phosphate + L-lysine = phosphate + L-homocitrulline. CC -!- Not identical with EC 2.1.3.3. // ID 2.1.4.1 DE Glycine amidinotransferase. AN L-arginine:glycine amidinotransferase. CA L-arginine + glycine = L-ornithine + guanidoacetate. CC -!- Canavanine can act instead of arginine. CC -!- Formerly EC 2.6.2.1. DR P50440, GATM_HUMAN; Q9D964, GATM_MOUSE; P50441, GATM_PIG ; DR P50442, GATM_RAT ; // ID 2.1.4.2 DE Scyllo-inosamine-4-phosphate amidinotransferase. AN Inosamine-phosphate amidinotransferase. AN L-arginine:inosamine-P-amidinotransferase. AN Inosamine-P amidinotransferase. AN L-arginine:inosamine phosphate amidinotransferase. CA L-arginine + 1-amino-1-deoxy-scyllo-inositol 4-phosphate = L-ornithine + CA 1-guanidino-1-deoxy-scyllo-inositol 4-phosphate. CC -!- 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol 6-phosphate, CC streptamine phosphate and 2-deoxystreptamine phosphate can also act CC as acceptor. CC -!- Canavanine can act as donor. DR Q54258, STB1_STRGA; P08078, STB1_STRGR; Q54264, STB2_STRGA; DR P29780, STB2_STRGR; // ID 2.2.1.1 DE Transketolase. AN Glycoaldehyde transferase. CA Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose CA 5-phosphate + D-xylulose 5-phosphate. CF Thiamine pyrophosphate. CC -!- Wide specificity for both reactants, e.g. converts hydroxypyruvate CC and R-CHO into CO(2) and R-CHOH-CO-CH(2)OH. CC -!- Transketolase from Alcaligenes faecalis shows high activity with CC D-erythrose as acceptor. DI Wernicke-Korsakoff syndrome; MIM:277730. PR PROSITE; PDOC00635; DR O94039, TKT1_CANAL; P27302, TKT1_ECOLI; Q12630, TKT1_KLULA; DR P57927, TKT1_PASMU; P58333, TKT1_RHIME; P23254, TKT1_YEAST; DR P33570, TKT2_ECOLI; P51854, TKT2_HUMAN; P57958, TKT2_PASMU; DR P56900, TKT2_RHIME; P33315, TKT2_YEAST; Q42677, TKT7_CRAPL; DR Q42675, TKTA_CRAPL; P21725, TKTC_ALCEU; Q42676, TKTC_CRAPL; DR Q58092, TKTC_METJA; Q43848, TKTC_SOLTU; Q58094, TKTN_METJA; DR P21726, TKTP_ALCEU; O67642, TKT_AQUAE ; Q9KAD7, TKT_BACHD ; DR P45694, TKT_BACSU ; P57195, TKT_BUCAI ; Q8KA26, TKT_BUCAP ; DR P43757, TKT_HAEIN ; P29401, TKT_HUMAN ; P40142, TKT_MOUSE ; DR P47312, TKT_MYCGE ; P46708, TKT_MYCLE ; P75611, TKT_MYCPN ; DR O06811, TKT_MYCTU ; P34736, TKT_PICST ; P50137, TKT_RAT ; DR Q52723, TKT_RHOCA ; P29277, TKT_RHOSH ; P22976, TKT_STRPN ; DR O83571, TKT_TREPA ; P51010, TKT_XANFL ; // ID 2.2.1.2 DE Transaldolase. AN Dihydroxyacetone transferase. AN Glycerone transferase. CA Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose CA 4-phosphate + D-fructose 6-phosphate. PR PROSITE; PDOC00741; DR Q9W1G0, TAL1_DROME; P37837, TAL1_HUMAN; P34214, TAL1_KLULA; DR Q93092, TAL1_MOUSE; P17440, TAL1_PICJA; Q9EQS0, TAL1_RAT ; DR O42700, TAL1_SCHPO; O88018, TAL1_STRCO; P15019, TAL1_YEAST; DR P48993, TAL2_ANASP; P48983, TAL2_NOSPU; Q9XAC0, TAL2_STRCO; DR P53228, TAL2_YEAST; P17441, TAL3_PICJA; P80427, TALA_CARMA; DR P78258, TALA_ECOLI; Q9CKL0, TALA_PASMU; Q8Z4T0, TALA_SALTI; DR Q8ZN83, TALA_SALTY; P30148, TALB_ECOLI; Q9CKH9, TALB_PASMU; DR Q8XG45, TALB_SALTY; Q8U7I5, TAL_AGRT5 ; P58561, TAL_ANASP ; DR P51778, TAL_ANAVA ; O66520, TAL_AQUAE ; Q9K6E4, TAL_BACHD ; DR P19669, TAL_BACSU ; P57194, TAL_BUCAI ; Q8KA27, TAL_BUCAP ; DR Q9PIL5, TAL_CAMJE ; Q9A2F1, TAL_CAUCR ; Q9PK80, TAL_CHLMU ; DR Q9Z998, TAL_CHLPN ; O84315, TAL_CHLTR ; Q97JD9, TAL_CLOAB ; DR Q9RUP6, TAL_DEIRA ; P45055, TAL_HAEIN ; Q9ZJC5, TAL_HELPJ ; DR P56108, TAL_HELPY ; Q9S0X4, TAL_METAM ; Q58370, TAL_METJA ; DR P55193, TAL_MYCLE ; O06812, TAL_MYCTU ; Q9JSU1, TAL_NEIMA ; DR Q9K139, TAL_NEIMB ; Q9I047, TAL_PSEAE ; Q8Y014, TAL_RALSO ; DR Q98EV0, TAL_RHILO ; Q99YJ2, TAL_STRPY ; P72797, TAL_SYNY3 ; DR Q9HKI3, TAL_THEAC ; Q9WYD1, TAL_THEMA ; Q97AZ4, TAL_THEVO ; DR Q9KLW8, TAL_VIBCH ; Q8ZIN2, TAL_YERPE ; // ID 2.2.1.3 DE Formaldehyde transketolase. AN Dihydroxyacetone synthase. AN DHAS. AN Glycerone synthase. CA D-xylulose 5-phosphate + formaldehyde = glyceraldehyde 3-phosphate + CA glycerone. CF Thiamine pyrophosphate. CC -!- Also converts hydroxypyruvate and formaldehyde into glycerone and CC CO(2). CC -!- Not identical with EC 2.2.1.1. PR PROSITE; PDOC00635; DR P06834, DAS_PICAN ; // ID 2.2.1.4 DE Acetoin--ribose-5-phosphate transaldolase. AN 1-deoxy-D-altro-heptulose 7-phosphate synthetase. CA 3-hydroxybutan-2-one + D-ribose 5-phosphate = acetaldehyde + 1-deoxy- CA D-altro-heptulose 7-phosphate. CF Thiamine pyrophosphate. // ID 2.2.1.5 DE 2-hydroxy-3-oxoadipate synthase. AN 2-hydroxy-3-oxoadipate synthetase. AN 2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating). AN Alpha-ketoglutaric-glyoxylic carboligase. AN Oxoglutarate: glyoxylate carboligase. CA 2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO(2). CF Thiamine pyrophosphate. CC -!- The product decarboxylates to 5-hydroxy-4-oxopentanoate. CC -!- The enzyme can decarboxylate 2-oxoglutarate. CC -!- Acetaldehyde can replace glyoxylate. CC -!- Formerly EC 4.1.3.15. // ID 2.2.1.6 DE Acetolactate synthase. AN Alpha-acetohydroxy acid synthetase. AN Alpha-acetohydroxyacid synthase. AN Alpha-acetolactate synthase. AN Alpha-acetolactate synthetase. AN Acetohydroxy acid synthetase. AN Acetohydroxyacid synthase. AN Acetolactate pyruvate-lyase (carboxylating). AN Acetolactic synthetase. CA 2 pyruvate = 2-acetolactate + CO(2). CF Thiamine pyrophosphate. CC -!- The reaction shown is in the pathway of biosynthesis of valine. CC -!- the enzyme can also transfer the acetaldehyde from pyruvate to 2- CC oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known CC as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of CC isoleucine. CC -!- Formerly EC 4.1.3.18. PR PROSITE; PDOC00166; DR P27818, ILV1_BRANA; P09342, ILV1_TOBAC; P14874, ILV2_BRANA; DR P09114, ILV2_TOBAC; P27819, ILV3_BRANA; P25605, ILV6_YEAST; DR P17597, ILVB_ARATH; P37251, ILVB_BACSU; P42463, ILVB_CORGL; DR O19929, ILVB_CYACA; P08142, ILVB_ECOLI; Q09129, ILVB_ENTAE; DR O78518, ILVB_GUITH; P27696, ILVB_KLEPN; Q04524, ILVB_KLETE; DR Q02137, ILVB_LACLA; Q57725, ILVB_METJA; Q59498, ILVB_MYCAV; DR O33112, ILVB_MYCLE; O53250, ILVB_MYCTU; P31594, ILVB_PORPU; DR P36620, ILVB_SCHPO; P27868, ILVB_SPIPL; P07342, ILVB_YEAST; DR P00892, ILVG_ECOLI; Q50613, ILVG_MYCTU; O67703, ILVH_AQUAE; DR O28555, ILVH_ARCFU; P37252, ILVH_BACSU; P57320, ILVH_BUCAI; DR O85294, ILVH_BUCAP; Q9TLY1, ILVH_CYACA; P00894, ILVH_ECOLI; DR Q9MS98, ILVH_GALSU; O78451, ILVH_GUITH; P45260, ILVH_HAEIN; DR Q02140, ILVH_LACLA; Q57625, ILVH_METJA; O27492, ILVH_METTH; DR Q59499, ILVH_MYCAV; O33113, ILVH_MYCLE; O53249, ILVH_MYCTU; DR P51230, ILVH_PORPU; P21622, ILVH_SALTY; Q55141, ILVH_SYNY3; DR P57321, ILVI_BUCAI; O85293, ILVI_BUCAP; Q9RQ65, ILVI_BUCSC; DR P00893, ILVI_ECOLI; P45261, ILVI_HAEIN; P40811, ILVI_SALTY; DR P13048, ILVM_ECOLI; P08143, ILVN_ECOLI; Q04789, ILVX_BACSU; // ID 2.2.1.7 DE 1-deoxy-D-xylulose 5-phosphate synthase. AN 1-deoxy-D-xylulose-5-phosphate pyruvate-lyase (carboxylating). AN DXP-synthase. CA Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose CA 5-phosphate + CO(2). CF Thiamine pyrophosphate. CC -!- The enzyme forms part of an alternative nonmevalonate pathway CC for terpenoid biosynthesis. CC -!- Formerly EC 4.1.3.37. PR PROSITE; PDOC00635; DR Q9F1V2, DXS1_KITGR; Q9X7W3, DXS1_STRCO; Q8VUR8, DXS2_KITGR; DR Q8CJP7, DXS2_STRCO; Q8UHD7, DXS_AGRT5 ; Q8YZ80, DXS_ANASP ; DR O67036, DXS_AQUAE ; Q38854, DXS_ARATH ; Q9K971, DXS_BACHD ; DR P54523, DXS_BACSU ; Q8YFM2, DXS_BRUME ; Q8G292, DXS_BRUSU ; DR P57536, DXS_BUCAI ; Q8K9A1, DXS_BUCAP ; Q9PIH8, DXS_CAMJE ; DR O78328, DXS_CAPAN ; Q9A6M5, DXS_CAUCR ; Q9PK62, DXS_CHLMU ; DR Q9Z6J9, DXS_CHLPN ; Q8KFI9, DXS_CHLTE ; O84335, DXS_CHLTR ; DR Q97HD5, DXS_CLOAB ; Q8XJE1, DXS_CLOPE ; Q8FPI2, DXS_COREF ; DR Q8NPB2, DXS_CORGL ; Q9RUB5, DXS_DEIRA ; Q8XE76, DXS_ECO57 ; DR Q8FKB9, DXS_ECOL6 ; P77488, DXS_ECOLI ; Q8R639, DXS_FUSNN ; DR P45205, DXS_HAEIN ; Q9ZM94, DXS_HELPJ ; O25121, DXS_HELPY ; DR Q8F153, DXS_LEPIN ; Q92BZ0, DXS_LISIN ; Q8Y7C1, DXS_LISMO ; DR Q50000, DXS_MYCLE ; Q8EWX7, DXS_MYCPE ; O07184, DXS_MYCTU ; DR Q9JW13, DXS_NEIMA ; Q9JXV7, DXS_NEIMB ; O22567, DXS_ORYSA ; DR P57848, DXS_PASMU ; Q9KGU7, DXS_PSEAE ; Q8XX95, DXS_RALSO ; DR Q985Y3, DXS_RHILO ; Q92RJ1, DXS_RHIME ; P26242, DXS_RHOCA ; DR Q8Z8X3, DXS_SALTI ; Q8ZRD1, DXS_SALTY ; Q8EGR9, DXS_SHEON ; DR Q9RBN6, DXS_STRC1 ; Q8DL74, DXS_SYNEL ; Q9R6S7, DXS_SYNLE ; DR Q8GAA0, DXS_SYNP7 ; P73067, DXS_SYNY3 ; Q9X291, DXS_THEMA ; DR Q8RAC5, DXS_THETN ; O83796, DXS_TREPA ; Q9KTL3, DXS_VIBCH ; DR Q87RU0, DXS_VIBPA ; Q8DFA3, DXS_VIBVU ; Q8D357, DXS_WIGBR ; DR Q8PJG7, DXS_XANAC ; Q8P815, DXS_XANCP ; Q9PB95, DXS_XYLFA ; DR Q87C03, DXS_XYLFT ; Q8ZC45, DXS_YERPE ; // ID 2.3.1.1 DE Amino-acid N-acetyltransferase. CA Acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate. CC -!- Also acts with L-aspartate and, more slowly, with some other amino CC acids. DR O66143, ARGA_BUCAI; P59099, ARGA_BUCAP; P08205, ARGA_ECOLI; DR Q9JW21, ARGA_NEIMA; Q9JXU9, ARGA_NEIMB; Q9CMJ6, ARGA_PASMU; DR P22567, ARGA_PSEAE; P32042, ARGA_PSEPK; Q8XZZ5, ARGA_RALSO; DR Q8Z421, ARGA_SALTI; Q8ZMB8, ARGA_SALTY; P59292, ARGA_SHEON; DR P59293, ARGA_SHIFL; Q9KPQ0, ARGA_VIBCH; P59294, ARGA_VIBVU; DR Q8ZH86, ARGA_YERPE; Q8UA56, ARGJ_AGRT5; O67100, ARGJ_AQUAE; DR O29118, ARGJ_ARCFU; Q9ZJ14, ARGJ_BACAM; Q9K8V3, ARGJ_BACHD; DR Q07908, ARGJ_BACST; P36843, ARGJ_BACSU; Q8G5F0, ARGJ_BIFLO; DR P59610, ARGJ_BRAJA; Q8YJF9, ARGJ_BRUME; Q8FYE2, ARGJ_BRUSU; DR Q9A3Y4, ARGJ_CAUCR; P59611, ARGJ_CHLTE; Q9RTQ2, ARGJ_DEIRA; DR Q93EJ3, ARGJ_HELHP; Q9CHD4, ARGJ_LACLA; O08319, ARGJ_LACPL; DR Q8EYV8, ARGJ_LEPIN; Q92BB8, ARGJ_LISIN; Q8Y6U2, ARGJ_LISMO; DR Q8TK55, ARGJ_METAC; Q8TX15, ARGJ_METKA; Q8PZL8, ARGJ_METMA; DR O26284, ARGJ_METTH; Q9CC14, ARGJ_MYCLE; P94988, ARGJ_MYCTU; DR P38434, ARGJ_NEIGO; Q9JRJ2, ARGJ_NEIMA; Q8CUN1, ARGJ_OCEIH; DR Q8XVJ7, ARGJ_RALSO; Q98G72, ARGJ_RHILO; Q92MJ1, ARGJ_RHIME; DR P96426, ARGJ_RHOFA; Q99X38, ARGJ_STAAM; Q8NYM7, ARGJ_STAAW; DR Q8CSF9, ARGJ_STAEP; Q9LCS7, ARGJ_STRCL; Q8DV45, ARGJ_STRMU; DR Q8DHN4, ARGJ_SYNEL; P74122, ARGJ_SYNY3; Q9X2A3, ARGJ_THEMA; DR Q9Z4S1, ARGJ_THENE; Q8R7B9, ARGJ_THETN; Q04728, ARGJ_YEAST; DR Q9K3D6, ARHA_MORS3; Q9K3D7, ARHA_MORS4; Q8YVA8, ARJ1_ANASP; DR Q97GH6, ARJ1_CLOAB; Q8YPF9, ARJ2_ANASP; Q97ET6, ARJ2_CLOAB; // ID 2.3.1.2 DE Imidazole N-acetyltransferase. AN Imidazole acetylase. CA Acetyl-CoA + imidazole = CoA + N-acetylimidazole. CC -!- Also acts with propanoyl-CoA. // ID 2.3.1.3 DE Glucosamine N-acetyltransferase. AN Glucosamine acetylase. CA Acetyl-CoA + D-glucosamine = CoA + N-acetyl-D-glucosamine. // ID 2.3.1.4 DE Glucosamine 6-phosphate N-acetyltransferase. AN Phosphoglucosamine transacetylase. AN Phosphoglucosamine acetylase. AN Glucosamine-6-phosphate acetylase. AN D-glucosamine-6-P N-acetyltransferase. AN Aminodeoxyglucosephosphate acetyltransferase. AN Glucosamine 6-phosphate acetylase. AN Glucosamine 6-phosphate N-acetyltransferase. AN N-acetylglucosamine-6-phosphate synthase. AN Phosphoglucosamine N-acetylase. AN Glucosamine-phosphate N-acetyltransferase. CA Acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine CA 6-phosphate. DR Q17427, GNA1_CAEEL; O93806, GNA1_CANAL; Q9VAI0, GNA1_DROME; DR P43577, GNA1_YEAST; // ID 2.3.1.5 DE Arylamine N-acetyltransferase. AN Arylamine acetylase. CA Acetyl-CoA + an arylamine = CoA + an N-acetylarylamine. CC -!- Wide specificity for aromatic amines, including serotonin. CC -!- Also catalyzes acetyl-transfer between arylamines without CoA. DR P13913, ARY1_CHICK; P18440, ARY1_HUMAN; P50292, ARY1_MESAU; DR P50294, ARY1_MOUSE; P18605, ARY1_RABIT; P50297, ARY1_RAT ; DR P13914, ARY2_CHICK; P11245, ARY2_HUMAN; P50293, ARY2_MESAU; DR P50295, ARY2_MOUSE; P11246, ARY2_RABIT; P50298, ARY2_RAT ; DR P50296, ARY3_MOUSE; P12275, ARYL_CHICK; O62696, ARYL_FELCA; DR O86309, NAT_MYCSM ; P96848, NAT_MYCTU ; // ID 2.3.1.6 DE Choline O-acetyltransferase. AN Choline acetylase. AN CHOACTase. CA Acetyl-CoA + choline = CoA + O-acetylcholine. CC -!- Propanoyl-CoA can act, more slowly, in place of acetyl-CoA. PR PROSITE; PDOC00402; DR P32756, CLAT_CAEEL; P07668, CLAT_DROME; P28329, CLAT_HUMAN; DR Q03059, CLAT_MOUSE; P13222, CLAT_PIG ; P32738, CLAT_RAT ; // ID 2.3.1.7 DE Carnitine O-acetyltransferase. AN Carnitine acetylase. CA Acetyl-CoA + carnitine = CoA + O-acetylcarnitine. CC -!- Also acts on propanoyl-CoA and butanoyl-CoA (cf. EC 2.3.1.21 and CC EC 2.3.1.137). PR PROSITE; PDOC00402; DR P80235, CACM_YEAST; Q00614, CACP_CANTR; P52826, CACP_COLLI; DR P43155, CACP_HUMAN; P47934, CACP_MOUSE; P32796, CACP_YEAST; // ID 2.3.1.8 DE Phosphate acetyltransferase. AN Phosphotransacetylase. AN Phosphoacylase. CA Acetyl-CoA + phosphate = CoA + acetyl phosphate. CC -!- Also acts with other short-chain acyl-CoA's. DR P39646, PTA_BACSU ; O51535, PTA_BORBU ; P57273, PTA_BUCAI ; DR Q8K9W5, PTA_BUCAP ; P71103, PTA_CLOAB ; O52593, PTA_CLOTM ; DR Q59330, PTA_CLOTS ; P77844, PTA_CORGL ; P39184, PTA_ECOLI ; DR P45107, PTA_HAEIN ; Q9ZKU4, PTA_HELPJ ; P38503, PTA_METTE ; DR Q49112, PTA_MYCCA ; P47541, PTA_MYCGE ; P75359, PTA_MYCPN ; DR P96254, PTA_MYCTU ; P39197, PTA_PARDE ; Q9X448, PTA_RHIME ; DR Q9ZE39, PTA_RICPR ; P73662, PTA_SYNY3 ; Q9X0L4, PTA_THEMA ; DR O83132, PTA_TREPA ; // ID 2.3.1.9 DE Acetyl-CoA C-acetyltransferase. AN Acetoacetyl-CoA thiolase. CA 2 acetyl-CoA = CoA + acetoacetyl-CoA. DI Alpha-methylacetoaceticaciduria; MIM:203750. PR PROSITE; PDOC00092; DR P76461, ATOB_ECOLI; P44873, ATOB_HAEIN; Q04677, THIB_CANTR; DR P14611, THIL_ALCEU; P45369, THIL_CHRVI; Q9ZHI1, THIL_CHRVO; DR P24752, THIL_HUMAN; P46707, THIL_MYCLE; Q10629, THIL_MYCTU; DR P54810, THIL_PARDE; P14610, THIL_PIG ; P17764, THIL_RAT ; DR P50174, THIL_RHIME; P10551, THIL_SACBA; P45363, THIL_THIVI; DR P41338, THIL_YEAST; P07097, THIL_ZOORA; P45359, THLA_CLOAB; DR P45855, THL_BACSU ; P45362, THL_CLODI ; P81347, THL_CLOPA ; DR Q46939, YQEF_ECOLI; // ID 2.3.1.10 DE Hydrogen-sulfide S-acetyltransferase. CA Acetyl-CoA + H(2)S = CoA + thioacetate. // ID 2.3.1.11 DE Thioethanolamine S-acetyltransferase. AN Thioltransacetylase B. CA Acetyl-CoA + thioethanolamine = CoA + S-acetylthioethanolamine. // ID 2.3.1.12 DE Dihydrolipoamide S-acetyltransferase. AN Lipoate acetyltransferase. AN Thioltransacetylase A. CA Acetyl-CoA + dihydrolipoamide = CoA + S-acetyldihydrolipoamide. CF Lipoyl group. CC -!- Component of multienzyme pyruvate dehydrogenase complex. DR P27747, ACOC_ALCEU; O31550, ACOC_BACSU; Q59695, ACOC_PSEPU; DR P35489, ODP2_ACHLA; Q59098, ODP2_ALCEU; P10802, ODP2_AZOVI; DR P11961, ODP2_BACST; P21883, ODP2_BACSU; P11180, ODP2_BOVIN; DR P57302, ODP2_BUCAI; Q8K9T8, ODP2_BUCAP; Q89AQ9, ODP2_BUCBP; DR P36413, ODP2_DICDI; P06959, ODP2_ECOLI; P45118, ODP2_HAEIN; DR P10515, ODP2_HUMAN; Q49110, ODP2_MYCCA; P47514, ODP2_MYCGE; DR P75392, ODP2_MYCPN; P20285, ODP2_NEUCR; Q59638, ODP2_PSEAE; DR P08461, ODP2_RAT ; Q9R9N3, ODP2_RHIME; Q92HK7, ODP2_RICCN; DR Q9ZD20, ODP2_RICPR; O59816, ODP2_SCHPO; P81421, ODP2_SOLTU; DR Q59821, ODP2_STAAU; P12695, ODP2_YEAST; O66119, ODP2_ZYMMO; DR P81420, ODP3_SOLTU; // ID 2.3.1.13 DE Glycine N-acyltransferase. CA Acyl-CoA + glycine = CoA + N-acylglycine. CC -!- The CoA derivatives of a number of aliphatic and aromatic acids, but CC not phenylacetyl-CoA or indole-3-acetyl-CoA, can act as donor. // ID 2.3.1.14 DE Glutamine N-phenylacetyltransferase. CA Phenylacetyl-CoA + L-glutamine = CoA + alpha-N-phenylacetyl-L-glutamine. // ID 2.3.1.15 DE Glycerol-3-phosphate O-acyltransferase. CA Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol CA 3-phosphate. CC -!- Acyl-[acyl-carrier protein] can also act as acyl donor. CC -!- Acts only with derivatives of fatty acids of chain length above CC C(10). DR Q43307, PLSB_ARATH; Q22949, PLSB_CAEEL; Q42713, PLSB_CARTI; DR P10349, PLSB_CUCMO; Q39639, PLSB_CUCSA; P58130, PLSB_ECO57; DR P00482, PLSB_ECOLI; P44857, PLSB_HAEIN; Q9HCL2, PLSB_HUMAN; DR Q61586, PLSB_MOUSE; Q9X7B0, PLSB_MYCLE; O53207, PLSB_MYCTU; DR Q9CLN7, PLSB_PASMU; P30706, PLSB_PEA ; Q43822, PLSB_PHAVU; DR Q9HXW7, PLSB_PSEAE; P97564, PLSB_RAT ; Q8Z1T6, PLSB_SALTI; DR Q8ZKH9, PLSB_SALTY; Q43869, PLSB_SPIOL; Q9KVP8, PLSB_VIBCH; DR Q87KN0, PLSB_VIBPA; Q8DD48, PLSB_VIBVU; Q8PES0, PLSB_XANAC; DR Q8P3E3, PLSB_XANCP; Q9PEJ7, PLSB_XYLFA; Q87EJ1, PLSB_XYLFT; DR Q8ZJ18, PLSB_YERPE; // ID 2.3.1.16 DE Acetyl-CoA C-acyltransferase. AN Beta-ketothiolase. AN 3-ketoacyl-CoA thiolase. CA Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA. DI Pseudo-Zellweger syndrome; MIM:261510. PR PROSITE; PDOC00092; DR O46629, ECHB_BOVIN; P55084, ECHB_HUMAN; Q60587, ECHB_RAT ; DR P21775, THIJ_RAT ; P33290, THIK_CANTR; Q8X8J4, THIK_ECO57; DR P21151, THIK_ECOLI; P09110, THIK_HUMAN; P28790, THIK_PSEFR; DR P07871, THIK_RAT ; Q9L6L6, THIK_SALTY; Q05493, THIK_YARLI; DR P27796, THIK_YEAST; Q8ZAM9, THIK_YERPE; P33291, THIL_CANTR; DR P42765, THIM_HUMAN; P13437, THIM_RAT ; P76503, YFCY_ECOLI; // ID 2.3.1.17 DE Aspartate N-acetyltransferase. CA Acetyl-CoA + L-aspartate = CoA + N-acetyl-L-aspartate. // ID 2.3.1.18 DE Galactoside O-acetyltransferase. AN Thiogalactoside acetyltransferase. CA Acetyl-CoA + a beta-D-galactoside = CoA + a 6-acetyl-beta-D- CA galactoside. CC -!- Acts on thiogalactosides and phenylgalactoside. PR PROSITE; PDOC00094; DR P07464, THGA_ECOLI; P52984, THGA_LACLA; // ID 2.3.1.19 DE Phosphate butyryltransferase. AN Phosphotransbutyrylase. CA Butanoyl-CoA + phosphate = CoA + butanoyl phosphate. DR P54530, PTB_BACSU ; P58255, PTB_CLOAB ; Q05624, PTB_CLOBE ; // ID 2.3.1.20 DE Diacylglycerol O-acyltransferase. AN Diglyceride acyltransferase. CA Acyl-CoA + 1,2-diacylglycerol = CoA + triacylglycerol. CC -!- Palmitoyl-CoA and other long-chain acyl-CoA's can act as donors. DR Q9GMF1, DGT1_CERAE; O75907, DGT1_HUMAN; Q9Z2A7, DGT1_MOUSE; DR Q9ERM3, DGT1_RAT ; // ID 2.3.1.21 DE Carnitine O-palmitoyltransferase. CA Palmitoyl-CoA + L-carnitine = CoA + L-palmitoylcarnitine. CC -!- Broad specificity to acyl group, over the range C(8) to C(18); CC optimal activity with palmitoyl-CoA (cf. EC 2.3.1.7 and CC EC 2.3.1.137). DI Lipid myopathy due to deficiency of CPT I; MIM:255120. DI Lipid myopathy due to deficiency of CPT II; MIM:255110. PR PROSITE; PDOC00402; DR P50416, CPT1_HUMAN; P97742, CPT1_MOUSE; P32198, CPT1_RAT ; DR P23786, CPT2_HUMAN; P52825, CPT2_MOUSE; P18886, CPT2_RAT ; DR Q92523, CPTM_HUMAN; Q63704, CPTM_RAT ; // ID 2.3.1.22 DE 2-acylglycerol O-acyltransferase. AN Acylglycerol palmitoyltransferase. AN Monoglyceride acyltransferase. CA Acyl-CoA + 2-acylglycerol = CoA + diacylglycerol. CC -!- Various 2-acylglycerols can act as acceptor. CC -!- Palmitoyl-CoA and other long-chain acyl-CoA's can act as donors. CC -!- The sn-1 position and the sn-3 position are both acylated, at about CC the same rate. // ID 2.3.1.23 DE 1-acylglycerophosphocholine O-acyltransferase. AN Lysolecithin acyltransferase. CA Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn- CA glycero-3-phosphocholine. CC -!- Acts preferentially with unsaturated acyl-CoA derivatives. CC -!- 1-acyl-sn-glycero-3-phosphoinositol can also act as acceptor. // ID 2.3.1.24 DE Sphingosine N-acyltransferase. CA Acyl-CoA + sphingosine = CoA + N-acylsphingosine. CC -!- Acts on sphingosine or its 2-epimer. // ID 2.3.1.25 DE Plasmalogen synthase. CA Acyl-CoA + 1-O-alk-1-enyl-glycero-3-phosphocholine = CoA + CA plasmenylcholine. // ID 2.3.1.26 DE Sterol O-acyltransferase. AN Cholesterol acyltransferase. AN Sterol-ester synthase. CA Acyl-CoA + cholesterol = CoA + cholesterol ester. CC -!- The animal enzyme is highly specific for transfer of acyl groups CC with a single cis double bond 9 carbon atoms distant from the CC carboxyl group. DR P25628, ARE1_YEAST; P53629, ARE2_YEAST; Q10269, AREH_SCHPO; DR O77760, SOA1_CERAE; Q60457, SOA1_CRIGR; P35610, SOA1_HUMAN; DR O77761, SOA1_MACFA; Q61263, SOA1_MOUSE; O70536, SOA1_RAT ; DR O77759, SOA2_CERAE; O75908, SOA2_HUMAN; O88908, SOA2_MOUSE; // ID 2.3.1.27 DE Cortisol O-acetyltransferase. CA Acetyl-CoA + cortisol = CoA + cortisol 21-acetate. // ID 2.3.1.28 DE Chloramphenicol O-acetyltransferase. CA Acetyl-CoA + chloramphenicol = CoA + chloramphenicol 3-acetate. CC -!- Chloramphenicol is an antibiotic. PR PROSITE; PDOC00093; PR PROSITE; PDOC00094; DR P26825, CAT1_CLOPE; P00485, CAT1_STAAU; P26826, CAT2_CLOPE; DR P22615, CAT2_ECOLI; P22616, CAT2_HAEIN; P00486, CAT2_STAAU; DR P00484, CAT3_ECOLI; P06135, CAT3_STAAU; P23364, CAT4_AGRT5; DR P26838, CAT4_ECOLI; P50868, CAT4_ENTAE; P50869, CAT4_MORMO; DR P26841, CAT4_PSEAE; P36882, CAT4_STAAU; P36883, CAT5_STAAU; DR P00487, CAT_BACPU ; P22782, CAT_CAMCO ; Q02736, CAT_CLOBU ; DR P11504, CAT_CLODI ; P00483, CAT_ECOLI ; P58777, CAT_KLESP ; DR P07641, CAT_PROMI ; P25309, CAT_STAIN ; P20074, CAT_STRAC ; DR Q03058, CAT_STRAG ; P49417, CAT_VIBAN ; // ID 2.3.1.29 DE Glycine C-acetyltransferase. AN 2-amino-3-ketobutyrate coenzyme A ligase. CA Acetyl-CoA + glycine = CoA + 2-amino-3-oxobutanoate. CF Pyridoxal-phosphate. PR PROSITE; PDOC00518; DR O31777, KBL_BACSU ; P07912, KBL_ECOLI ; O75600, KBL_HUMAN ; DR O88986, KBL_MOUSE ; P37419, KBL_SALTY ; // ID 2.3.1.30 DE Serine O-acetyltransferase. CA Acetyl-CoA + L-serine = CoA + O-acetyl-L-serine. PR PROSITE; PDOC00094; DR Q06750, CYSE_BACSU; P57162, CYSE_BUCAI; P32003, CYSE_BUCAP; DR P05796, CYSE_ECOLI; P43886, CYSE_HAEIN; Q9ZK14, CYSE_HELPJ; DR P71405, CYSE_HELPY; P29847, CYSE_SALTY; P77985, CYSE_STAXY; DR Q56002, CYSE_SYNP7; P74089, CYSE_SYNY3; P23145, NIFP_AZOCH; DR Q59967, SRPH_SYNP7; // ID 2.3.1.31 DE Homoserine O-acetyltransferase. AN Homoserine O-trans-acetylase. AN Homoserine transacetylase. CA Acetyl-CoA + L-homoserine = CoA + O-acetyl-L-homoserine. DR P12917, MET2_ASCIM; Q9Y875, MET2_EMENI; Q06736, MET2_SACPS; DR O60062, MET2_SCHPO; P08465, MET2_YEAST; Q9AAS1, METX_CAUCR; DR Q8KES7, METX_CHLTE; Q8FRT0, METX_COREF; O68640, METX_CORGL; DR Q9RVZ8, METX_DEIRA; P45131, METX_HAEIN; P57715, METX_HALN1; DR Q8F4I0, METX_LEPIN; P94891, METX_LEPME; Q92E58, METX_LISIN; DR Q8Y9D6, METX_LISMO; O27848, METX_METTH; O32874, METX_MYCLE; DR O53391, METX_MYCTU; Q9JUT9, METX_NEIMA; Q9JZQ5, METX_NEIMB; DR P57884, METX_PASMU; P57714, METX_PSEAE; Q8Y3F3, METX_RALSO; DR Q98G09, METX_RHILO; Q9RA51, METX_THETH; Q8PK44, METX_XANAC; DR Q8P8L2, METX_XANCP; Q9PAN0, METX_XYLFA; Q87BG9, METX_XYLFT; // ID 2.3.1.32 DE Lysine N-acetyltransferase. AN Lysine N(6)-acetyltransferase. AN LAT. CA Acetyl phosphate + L-lysine = phosphate + N(6)-acetyl-L-lysine. DR P41929, LYC1_YARLI; // ID 2.3.1.33 DE Histidine N-acetyltransferase. CA Acetyl-CoA + L-histidine = CoA + N-acetyl-L-histidine. // ID 2.3.1.34 DE D-tryptophan N-acetyltransferase. CA Acetyl-CoA + D-tryptophan = CoA + N-acetyl-D-tryptophan. // ID 2.3.1.35 DE Glutamate N-acetyltransferase. AN Ornithine acetyltransferase. AN Ornithine transacetylase. CA N(2)-acetyl-L-ornithine + L-glutamate = L-ornithine + N-acetyl-L- CA glutamate. CC -!- Also has some hydrolytic activity on acetyl-L-ornithine, but rate is CC 1% of that of transferase activity. DR Q8UA56, ARGJ_AGRT5; O67100, ARGJ_AQUAE; O29118, ARGJ_ARCFU; DR Q9ZJ14, ARGJ_BACAM; Q9K8V3, ARGJ_BACHD; Q07908, ARGJ_BACST; DR P36843, ARGJ_BACSU; Q8G5F0, ARGJ_BIFLO; P59610, ARGJ_BRAJA; DR Q8YJF9, ARGJ_BRUME; Q8FYE2, ARGJ_BRUSU; Q9A3Y4, ARGJ_CAUCR; DR P59611, ARGJ_CHLTE; Q8FTN4, ARGJ_COREF; Q59280, ARGJ_CORGL; DR Q9RTQ2, ARGJ_DEIRA; Q93EJ3, ARGJ_HELHP; Q9CHD4, ARGJ_LACLA; DR O08319, ARGJ_LACPL; Q8EYV8, ARGJ_LEPIN; Q92BB8, ARGJ_LISIN; DR Q8Y6U2, ARGJ_LISMO; Q8TK55, ARGJ_METAC; Q57645, ARGJ_METJA; DR Q8TX15, ARGJ_METKA; Q8PZL8, ARGJ_METMA; O26284, ARGJ_METTH; DR Q9CC14, ARGJ_MYCLE; P94988, ARGJ_MYCTU; P38434, ARGJ_NEIGO; DR Q9JRJ2, ARGJ_NEIMA; Q8CUN1, ARGJ_OCEIH; Q9HW04, ARGJ_PSEAE; DR P59612, ARGJ_PSEPK; Q8XVJ7, ARGJ_RALSO; Q98G72, ARGJ_RHILO; DR Q92MJ1, ARGJ_RHIME; P96426, ARGJ_RHOFA; Q99X38, ARGJ_STAAM; DR Q8NYM7, ARGJ_STAAW; Q8CSF9, ARGJ_STAEP; Q9LCS7, ARGJ_STRCL; DR Q8CK24, ARGJ_STRCO; Q8DV45, ARGJ_STRMU; Q8DHN4, ARGJ_SYNEL; DR P74122, ARGJ_SYNY3; Q9X2A3, ARGJ_THEMA; Q9Z4S1, ARGJ_THENE; DR P96137, ARGJ_THETH; Q8R7B9, ARGJ_THETN; Q04728, ARGJ_YEAST; DR Q8YVA8, ARJ1_ANASP; Q97GH6, ARJ1_CLOAB; Q8YPF9, ARJ2_ANASP; DR Q97ET6, ARJ2_CLOAB; // ID 2.3.1.36 DE D-amino-acid N-acetyltransferase. CA Acetyl-CoA + a D-amino acid = CoA + an N-acetyl-D-amino acid. // ID 2.3.1.37 DE 5-aminolevulinic acid synthase. AN Delta-aminolevulinate synthase. AN Delta-Ala synthetase. AN ALAS. CA Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2). CF Pyridoxal-phosphate. CC -!- The enzyme in erythrocytes is genetically distinct from that in CC other tissues. PR PROSITE; PDOC00518; DR Q9YHT4, HEM0_BRARE; P18080, HEM0_CHICK; Q9XT75, HEM0_DELLE; DR P22557, HEM0_HUMAN; P08680, HEM0_MOUSE; P43090, HEM0_OPSTA; DR Q63147, HEM0_RAT ; Q06965, HEM0_RHOSH; Q92403, HEM1_AGABI; DR P26505, HEM1_AGRRD; P08262, HEM1_BRAJA; O94069, HEM1_CANAL; DR P07997, HEM1_CHICK; Q9XS79, HEM1_DELLE; P38092, HEM1_EMENI; DR P13196, HEM1_HUMAN; P78698, HEM1_KLULA; P43091, HEM1_OPSTA; DR P43089, HEM1_PARDE; P13195, HEM1_RAT ; P08080, HEM1_RHIME; DR P18079, HEM1_RHOCA; Q04512, HEM1_RHOSH; Q9ZCB8, HEM1_RICPR; DR P09950, HEM1_YEAST; // ID 2.3.1.38 DE [Acyl-carrier protein] S-acetyltransferase. CA Acetyl-CoA + [acyl-carrier protein] = CoA + acetyl-[acyl-carrier CA protein]. DR P34731, FAS1_CANAL; Q9UUG0, FAS1_SCHPO; P34229, FAS1_YARLI; DR P07149, FAS1_YEAST; P12276, FAS_CHICK ; P49327, FAS_HUMAN ; DR P19096, FAS_MOUSE ; P12785, FAS_RAT ; Q92215, TOXC_COCCA; // ID 2.3.1.39 DE [Acyl-carrier protein] S-malonyltransferase. CA Malonyl-CoA + [acyl-carrier protein] = CoA + malonyl-[acyl-carrier CA protein]. DR P71019, FABD_BACSU; Q8K9J6, FABD_BUCAP; Q89AH0, FABD_BUCBP; DR P25715, FABD_ECOLI; P43712, FABD_HAEIN; Q10501, FABD_MYCTU; DR O85140, FABD_SALTY; P73242, FABD_SYNY3; P34731, FAS1_CANAL; DR Q9UUG0, FAS1_SCHPO; P34229, FAS1_YARLI; P07149, FAS1_YEAST; DR P12276, FAS_CHICK ; P49327, FAS_HUMAN ; P19096, FAS_MOUSE ; DR P12785, FAS_RAT ; Q92215, TOXC_COCCA; // ID 2.3.1.40 DE Acyl-[acyl-carrier protein]--phospholipid O-acyltransferase. CA Acyl-[acyl-carrier protein] + O-(2-acyl-sn-glycero-3- CA phospho)ethanolamine = [acyl-carrier protein] + O-(1-beta-acyl-2-acyl- CA sn-glycero-3-phospho)ethanolamine. // ID 2.3.1.41 DE 3-oxoacyl-[acyl-carrier protein] synthase. AN Beta-ketoacyl-ACP synthase. CA Acyl-[acyl-carrier protein] + malonyl-[acyl-carrier protein] = CA 3-oxoacyl-[acyl-carrier protein] + CO(2) + [acyl-carrier protein]. PR PROSITE; PDOC00529; DR P39525, CEM1_YEAST; Q9CBS7, FAB1_MYCLE; Q10524, FAB1_MYCTU; DR O69473, FAB2_MYCLE; Q10525, FAB2_MYCTU; P52410, FABB_ARATH; DR P57193, FABB_BUCAI; Q8KA28, FABB_BUCAP; Q89AY4, FABB_BUCBP; DR P14926, FABB_ECOLI; P43710, FABB_HAEIN; P23902, FABB_HORVU; DR P39435, FABF_ECOLI; P56902, FABF_RHIME; P73283, FABF_SYNY3; DR Q9KQH9, FABF_VIBCH; P55338, FABF_VIBHA; O67185, FABH_AQUAE; DR P49243, FABH_ARATH; O34746, FABH_BACSU; Q9PIH1, FABH_CAMJE; DR Q9PKF5, FABH_CHLMU; Q9Z8P0, FABH_CHLPN; O84242, FABH_CHLTR; DR P24249, FABH_ECOLI; P43711, FABH_HAEIN; Q9ZMN0, FABH_HELPJ; DR O24994, FABH_HELPY; O06399, FABH_MYCTU; P51196, FABH_PORPU; DR P31176, FABH_PORUM; P20582, FABH_PSEAE; P30790, FABH_RHOCA; DR Q9ZCH1, FABH_RICPR; O85139, FABH_SALTY; Q07510, FABH_SPIOL; DR P43098, FAS2_CANAL; P15368, FAS2_PENPA; Q10289, FAS2_SCHPO; DR P19097, FAS2_YEAST; P12276, FAS_CHICK ; P49327, FAS_HUMAN ; DR P19096, FAS_MOUSE ; P12785, FAS_RAT ; P49244, FBH1_CUPWR; DR P49245, FBH2_CUPWR; // ID 2.3.1.42 DE Glycerone-phosphate O-acyltransferase. AN Dihydroxyacetone phosphate acyltransferase. CA Acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate. CC -!- Uses CoA derivatives of palmitate, stearate, and oleate, with CC highest activity on palmitoyl-CoA. DR O15228, DAPT_HUMAN; P98192, DAPT_MOUSE; Q9ES71, DAPT_RAT ; // ID 2.3.1.43 DE Phosphatidylcholine--sterol O-acyltransferase. AN Lecithin--cholesterol acyltransferase. AN LCAT. AN Phospholipid--cholesterol acyltransferase. CA Phosphatidylcholine + a sterol = a sterol ester + CA 1-acylglycerophosphocholine. CC -!- Palmitoyl, oleoyl, and linoleoyl can be transferred; a number of CC sterols, including cholesterol, can act as acceptor. CC -!- The bacterial enzyme also catalyzes the reactions of EC 3.1.1.4 and CC EC 3.1.1.5. DI Norum disease; MIM:245900. DI Fish-eye disease; MIM:136120. PR PROSITE; PDOC00110; DR P10480, GCAT_AERHY; P53760, LCAT_CHICK; O35502, LCAT_CLEGL; DR O35573, LCAT_ELIQU; P04180, LCAT_HUMAN; O35724, LCAT_MICMN; DR P16301, LCAT_MOUSE; Q08758, LCAT_PAPAN; P30930, LCAT_PIG ; DR P53761, LCAT_RABIT; P18424, LCAT_RAT ; O35840, LCAT_TATKG; // ID 2.3.1.44 DE N-acetylneuraminate 4-O-acetyltransferase. CA Acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-4-O-acetylneuraminate. CC -!- Both free and glycosidically bound N-acetyl-and N-glycolyl- CC neuraminates can act as O-acetyl acceptor. // ID 2.3.1.45 DE N-acetylneuraminate 7-O(or 9-O)-acetyltransferase. CA Acetyl-CoA + N-acetylneuraminate = CoA + N-acetyl-7-O(or 9-O)- CA acetylneuraminate. CC -!- Both free and glycosidically bound N-acetyl and N-glycolyl- CC neuraminates can act as O-acetyl acceptor. // ID 2.3.1.46 DE Homoserine O-succinyltransferase. AN Homoserine O-transsuccinylase. CA Succinyl-CoA + L-homoserine = CoA + O-succinyl-L-homoserine. DR Q9KAK7, META_BACHD; P54167, META_BACSU; Q8YBV5, META_BRUME; DR Q9PLV2, META_CAMJE; Q97I29, META_CLOAB; Q8X610, META_ECO57; DR P07623, META_ECOLI; Q9CEC5, META_LACLA; Q92L99, META_RHIME; DR Q8Z1W1, META_SALTI; P37413, META_SALTY; Q97PM9, META_STRPN; DR Q9WZY3, META_THEMA; Q9KRM5, META_VIBCH; Q87NW7, META_VIBPA; DR Q8D937, META_VIBVU; Q8ZAR4, META_YERPE; // ID 2.3.1.47 DE 8-amino-7-oxononanoate synthase. AN AONS. AN 8-amino-7-ketopelargonate synthase. AN 7-keto-8-amino-pelargonic acid synthetase. AN 7-KAP synthetase. CA 6-carboxyhexanoyl-CoA + L-alanine = 8-amino-7-oxononanoate + CoA + CO(2). CF Pyridoxal-phosphate. PR PROSITE; PDOC00518; DR O66875, BIOF_AQUAE; P22806, BIOF_BACSH; P53556, BIOF_BACSU; DR P12998, BIOF_ECOLI; Q47829, BIOF_ERWHE; P44422, BIOF_HAEIN; DR Q9ZLN3, BIOF_HELPJ; O25320, BIOF_HELPY; Q58694, BIOF_METJA; DR P45487, BIOF_MYCLE; O06621, BIOF_MYCTU; P36570, BIOF_SERMA; // ID 2.3.1.48 DE Histone acetyltransferase. CA Acetyl-CoA + histone = CoA + acetyl-histone. CC -!- A group of enzymes with differing specificity towards histone CC acceptors. DR Q92793, CBP_HUMAN ; P45481, CBP_MOUSE ; O14929, HAT1_HUMAN; DR Q12341, HAT1_YEAST; Q9Y6Q9, NCO3_HUMAN; O09000, NCO3_MOUSE; DR Q9EPU2, NCO3_RAT ; O57539, NCO3_XENLA; Q09472, P300_HUMAN; // ID 2.3.1.49 DE Deacetyl-[citrate-(pro-3S)-lyase] S-acetyltransferase. CA S-acetylphosphopantetheine + deacetyl-[citrate-oxaloacetate-lyase CA ((pro-3S)-CH(2)COO(-)-acetate)] = phosphopantetheine + CA [citrate oxaloacetate-lyase ((pro-3S)-CH(2)COO(-)-acetate)]. CC -!- Acetylates and activates EC 4.1.3.6. // ID 2.3.1.50 DE Serine C-palmitoyltransferase. CA Palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO(2). CF Pyridoxal-phosphate. PR PROSITE; PDOC00518; DR O54695, LCB1_CRIGR; O15269, LCB1_HUMAN; O35704, LCB1_MOUSE; DR P25045, LCB1_YEAST; O54694, LCB2_CRIGR; O15270, LCB2_HUMAN; DR P48241, LCB2_KLULA; P97363, LCB2_MOUSE; Q09925, LCB2_SCHPO; DR P40970, LCB2_YEAST; // ID 2.3.1.51 DE 1-acylglycerol-3-phosphate O-acyltransferase. CA Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol CA 3-phosphate. CC -!- Acyl-[acyl-carrier protein] can also acts as acyl donor. CC -!- The animal enzyme is specific for the transfer of unsaturated fatty CC acyl groups. DR Q93841, PLC1_CAEEL; Q22267, PLC2_CAEEL; Q99943, PLCA_HUMAN; DR O35083, PLCA_MOUSE; O15120, PLCB_HUMAN; Q9NRZ7, PLCC_HUMAN; DR Q9NRZ5, PLCD_HUMAN; Q924S1, PLCD_RAT ; Q9NUQ2, PLCE_HUMAN; DR Q9D1E8, PLCE_MOUSE; Q59188, PLSC_BORBU; Q42670, PLSC_COCNU; DR P26647, PLSC_ECOLI; P44848, PLSC_HAEIN; Q9ZJN8, PLSC_HELPJ; DR O25903, PLSC_HELPY; Q42868, PLSC_LIMAL; Q42870, PLSC_LIMDO; DR Q49402, PLSC_MYCGE; P75479, PLSC_MYCPN; Q59601, PLSC_NEIGO; DR Q9JU41, PLSC_NEIMA; Q9JZ47, PLSC_NEIMB; P26974, PLSC_SALTY; DR P33333, PLSC_YEAST; // ID 2.3.1.52 DE 2-acylglycerol-3-phosphate O-acyltransferase. CA Acyl-CoA + 2-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol CA 3-phosphate. CC -!- Saturated acyl-CoA thioesters are the most effective acyl donors. // ID 2.3.1.53 DE Phenylalanine N-acetyltransferase. CA Acetyl-CoA + L-phenylalanine = CoA + N-acetyl-L-phenylalanine. CC -!- Also acts, more slowly, on L-histidine and L-alanine. // ID 2.3.1.54 DE Formate C-acetyltransferase. AN Pyruvate formate-lyase. CA Acetyl-CoA + formate = CoA + pyruvate. PR PROSITE; PDOC00665; DR P09373, PFLB_ECOLI; P43753, PFLB_HAEIN; P32674, PFLD_ECOLI; DR P75793, PFLF_ECOLI; P37836, PFL_CHLRE ; Q46266, PFL_CLOPA ; DR O32797, PFL_LACLA ; O32799, PFL_LACLC ; Q59934, PFL_STRMU ; // ID 2.3.1.55 DE Transferred entry: 2.3.1.82. // ID 2.3.1.56 DE Aromatic-hydroxylamine O-acetyltransferase. CA N-hydroxy-4-acetylaminobiphenyl + N-hydroxy-4-aminobiphenyl = CA N-hydroxy-4-aminobiphenyl + N-acetoxy-4-aminobiphenyl. CC -!- Transfers the N-acetyl group of some aromatic acethydroxamates to CC the O-position of some aromatic hydroxylamines. // ID 2.3.1.57 DE Diamine N-acetyltransferase. AN Spermidine acetyltransferase. AN Putrescine acetyltransferase. CA Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine. CC -!- Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, CC spermidine (forming N(1)- and N(8)-acetylspermidine), spermine, CC N(1)-acetylspermidine and N(8)-acetylspermidine. DR P37354, ATDA_ECOLI; P21673, ATDA_HUMAN; Q01612, ATDA_MESAU; DR P48026, ATDA_MOUSE; P49431, ATDA_MUSSA; Q28999, ATDA_PIG ; DR P39909, BLTD_BACSU; P57139, GLMU_BUCAI; Q8KA74, GLMU_BUCAP; DR P17114, GLMU_ECOLI; P43889, GLMU_HAEIN; Q50986, GLMU_NEIGO; // ID 2.3.1.58 DE 2,3-diaminopropionate N-oxalyltransferase. AN Oxalyldiaminopropionate synthase. CA Oxalyl-CoA + L-2,3-diaminopropanoate = CoA + N(3)-oxalyl-L-2,3- CA diaminopropanoate. // ID 2.3.1.59 DE Gentamicin 2'-N-acetyltransferase. AN Gentamicin acetyltransferase II. CA Acetyl-CoA + gentamicin C(1A) = CoA + N(2')-acetylgentamicin C(1A). CC -!- The antibiotics gentamicin A, sisomicin, tobramycin, paromomycin, CC neomycin B, kanamycin B and kanamycin C can also act as acceptors. // ID 2.3.1.60 DE Gentamicin 3'-N-acetyltransferase. AN Gentamicin acetyltransferase I. AN Aminoglycoside acetyltransferase AAC(3)-I. CA Acetyl-CoA + gentamicin C = CoA + N(3')-acetylgentamicin C. CC -!- Also acetylates sisomicin. DR P23181, AAC1_PSEAE; // ID 2.3.1.61 DE Dihydrolipoamide S-succinyltransferase. CA Succinyl-CoA + dihydrolipoamide = CoA + S-succinyldihydrolipoamide. CF Lipoyl group. CC -!- Component of the multienzyme 2-oxoglutarate dehydrogenase complex. DI Maple syrup urine disease type II; MIM:248610. DR P52993, ODO2_ALCEU; P20708, ODO2_AZOVI; P16263, ODO2_BACSU; DR P11179, ODO2_BOVIN; P57389, ODO2_BUCAI; Q8K9N2, ODO2_BUCAP; DR Q89AJ6, ODO2_BUCBP; P07016, ODO2_ECOLI; Q90512, ODO2_FUGRU; DR P45302, ODO2_HAEIN; P36957, ODO2_HUMAN; Q10381, ODO2_MYCTU; DR Q9N0F1, ODO2_PIG ; P31051, ODO2_PSEPU; Q01205, ODO2_RAT ; DR Q92J43, ODO2_RICCN; Q9ZDY4, ODO2_RICPR; O94681, ODO2_SCHPO; DR P19262, ODO2_YEAST; // ID 2.3.1.62 DE 2-acylglycerophosphocholine O-acyltransferase. CA Acyl-CoA + 2-acyl-sn-glycero-3-phosphocholine = CoA + CA phosphatidylcholine. // ID 2.3.1.63 DE 1-alkylglycerophosphocholine O-acyltransferase. CA Acyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 1-alkyl-2-acyl- CA sn-glycero-3-phosphocholine. CC -!- May be identical with EC 2.3.1.23. // ID 2.3.1.64 DE Agmatine N(4)-coumaroyltransferase. AN p-coumaroyl-CoA-agmatine N-P-coumaroyltransferase. CA 4-coumaroyl-CoA + agmatine = CoA + N-(4-guanidinobutyl)-4- CA hydroxycinnamamide. // ID 2.3.1.65 DE Glycine N-choloyltransferase. AN Glycine-taurine N-acyltransferase. CA Choloyl-CoA + glycine = CoA + glycocholate. CC -!- Taurine can act, more slowly, as acceptor. CC -!- Acts on CoA derivatives of other bile acids. // ID 2.3.1.66 DE Leucine N-acetyltransferase. CA Acetyl-CoA + L-leucine = CoA + N-acetyl-L-leucine. CC -!- Propanoyl-CoA can act, more slowly, as donor. CC -!- L-arginine, L-valine, L-phenylalanine and peptides containing CC L-leucine can act as acceptor. // ID 2.3.1.67 DE 1-alkylglycerophosphocholine O-acetyltransferase. CA Acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 1-alkyl-2- CA acetyl-sn-glycero-3-phosphocholine. // ID 2.3.1.68 DE Glutamine N-acyltransferase. CA Acyl-CoA + L-glutamine = CoA + N-acyl-L-glutamine. CC -!- Phenylacetyl-CoA or indole-3-acetyl-CoA, but not benzoyl-CoA, can CC act as acyl donor. CC -!- Not identical with EC 2.3.1.13 or EC 2.3.1.71. // ID 2.3.1.69 DE Monoterpenol O-acetyltransferase. AN Menthol transacetylase. CA Acetyl-CoA + a monoterpenol = CoA + a monoterpenol acetate ester. CC -!- (-)-menthol, (+)-neomenthol, borneol, cyclohexanol and N-decanol can CC be acetylated. // ID 2.3.1.70 DE CDP-acylglycerol O-arachidonyltransferase. CA Arachidonyl-CoA + CDP-acylglycerol = CoA + CDP-diacylglycerol. CC -!- Highly specific for both donor and acceptor. // ID 2.3.1.71 DE Glycine N-benzoyltransferase. CA Benzoyl-CoA + glycine = CoA + N-benzoylglycine. CC -!- Not identical with EC 2.3.1.13 or EC 2.3.1.68. // ID 2.3.1.72 DE Indoleacetylglucose--inositol O-acyltransferase. CA Indole-3-acetyl-beta-1-D-glucose + myo-inositol = D-glucose + CA indole-3-acetyl-myo-inositol. // ID 2.3.1.73 DE Diacylglycerol--sterol O-acyltransferase. CA 1,2-diacyl-sn-glycerol + a sterol = monoacylglycerol + a sterol ester. CC -!- Cholesterol, sitosterol, campesterol and diacylglycerol can act as CC acceptor. CC -!- Transfers a number of long-chain fatty acyl groups. // ID 2.3.1.74 DE Naringenin-chalcone synthase. AN Chalcone synthase. AN Flavonone synthase. AN 6'-deoxychalcone synthase. CA 3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + naringenin-chalcone + 3 CO(2). CC -!- In the presence of NADH and a reductase, 6'-deoxychalcone is CC produced. PR PROSITE; PDOC00403; DR P54157, BCSA_BACSU; P48386, CHS1_CAMSI; Q9ZRR8, CHS1_CASGL; DR Q9SML4, CHS1_CICAR; Q9XJ58, CHS1_CITSI; Q9ZS41, CHS1_DAUCA; DR P48390, CHS1_GERHY; P26018, CHS1_HORVU; Q9MB33, CHS1_IPOBA; DR P23418, CHS1_LYCES; P24824, CHS1_MAIZE; P30073, CHS1_MEDSA; DR Q01286, CHS1_PEA ; Q9FSB9, CHS1_RUTGR; P53414, CHS1_SECCE; DR P13416, CHS1_SINAL; Q9XGX2, CHS1_SORBI; P24826, CHS1_SOYBN; DR P51083, CHS1_TRISU; P48387, CHS2_CAMSI; Q9XJ57, CHS2_CITSI; DR Q9ZS40, CHS2_DAUCA; P48391, CHS2_GERHY; Q96562, CHS2_HORVU; DR Q9MB41, CHS2_IPOBA; P23419, CHS2_LYCES; P24825, CHS2_MAIZE; DR P30074, CHS2_MEDSA; Q01287, CHS2_PEA ; Q9FSB8, CHS2_RUTGR; DR P53415, CHS2_SECCE; Q43188, CHS2_SOLTU; Q9SBL7, CHS2_SORBI; DR P17957, CHS2_SOYBN; P51084, CHS2_TRISU; O23729, CHS3_BROFI; DR P48388, CHS3_CAMSI; P48392, CHS3_GERHY; Q9MB40, CHS3_IPOBA; DR P51077, CHS3_MEDSA; O23883, CHS3_PEA ; Q9FSB7, CHS3_RUTGR; DR P13417, CHS3_SINAL; Q9SBL6, CHS3_SORBI; P19168, CHS3_SOYBN; DR P51085, CHS3_TRISU; O23730, CHS4_BROFI; Q9MB39, CHS4_IPOBA; DR P30075, CHS4_MEDSA; O23882, CHS4_PEA ; Q9SBL5, CHS4_SORBI; DR P51086, CHS4_TRISU; P51078, CHS5_MEDSA; O23884, CHS5_PEA ; DR Q9SBL4, CHS5_SORBI; P48406, CHS5_SOYBN; P51087, CHS5_TRISU; DR Q9MB38, CHS6_IPOBA; P51079, CHS6_MEDSA; Q01288, CHS6_PEA ; DR Q9SBL3, CHS6_SORBI; P30080, CHS6_SOYBN; P51088, CHS6_TRISU; DR Q9MB37, CHS7_IPOBA; P51080, CHS7_MEDSA; Q9M5M0, CHS7_PICMA; DR Q9XGX1, CHS7_SORBI; P30081, CHS7_SOYBN; O23731, CHS8_BROFI; DR Q9MB36, CHS8_IPOBA; P30076, CHS8_MEDSA; P30077, CHS9_MEDSA; DR P48393, CHSA_IPOCO; P48400, CHSA_IPOPL; P48397, CHSA_IPOPU; DR P48401, CHSA_IPOTF; P48403, CHSA_IPOTR; P51081, CHSA_PEA ; DR P08894, CHSA_PETHY; P48395, CHSA_PHANI; Q41436, CHSA_SOLTU; DR P48394, CHSB_IPOCO; P48398, CHSB_IPOPU; P48402, CHSB_IPOTF; DR P48404, CHSB_IPOTR; P51082, CHSB_PEA ; P22924, CHSB_PETHY; DR P48396, CHSB_PHANI; Q43163, CHSB_SOLTU; P48399, CHSC_IPOPU; DR P22925, CHSD_PETHY; O22045, CHSD_PHANI; O22047, CHSE_IPOPU; DR O22046, CHSE_PHANI; P22926, CHSF_PETHY; P22927, CHSG_PETHY; DR P22928, CHSJ_PETHY; P06515, CHSY_ANTMA; Q9SEP4, CHSY_ARAAL; DR P13114, CHSY_ARATH; P51075, CHSY_BETVE; P48385, CHSY_CALCH; DR Q9SEP2, CHSY_CARAN; Q9ZRS4, CHSY_CATRO; O04220, CHSY_CHRAE; DR P48389, CHSY_DIACA; Q9LKP7, CHSY_DIAMO; Q9MBB1, CHSY_EQUAR; DR P51076, CHSY_FRAAN; O82144, CHSY_HYDMC; P30078, CHSY_MALDO; DR P17818, CHSY_MATIN; O22586, CHSY_ONOVI; P48405, CHSY_ORYSA; DR Q9ZU06, CHSY_PERAE; O04111, CHSY_PERFR; P16107, CHSY_PETCR; DR P49440, CHSY_PHAVU; O65872, CHSY_PINST; P30079, CHSY_PINSY; DR P23569, CHSY_PUELO; O22652, CHSY_RAPSA; P51089, CHS_VIGUN ; DR P51090, CHS_VITVI ; // ID 2.3.1.75 DE Long-chain-alcohol O-fatty-acyltransferase. AN Wax synthase. CA Acyl-CoA + a long-chain alcohol = CoA + a long-chain ester. CC -!- Transfers saturated or unsaturated acyl residues of chain length CC C(18) to C(20) to long-chain alcohols, forming waxes. CC -!- The best acceptor is cis-icos-11-en-1-ol. // ID 2.3.1.76 DE Retinol O-fatty-acyltransferase. CA Acyl-CoA + retinol = CoA + retinyl ester. CC -!- Acts on palmitoyl-CoA and other long-chain fatty-acyl derivatives of CC CoA. // ID 2.3.1.77 DE Triacylglycerol--sterol O-acyltransferase. CA Triacylglycerol + a 3-beta-hydroxysterol = diacylglycerol + a CA 3-beta-hydroxysterol ester. CC -!- Tripalmitoylglycerol can act as donor, and, more slowly, other CC triacylglycerols containing C(6) to C(22) fatty acids. CC -!- The best acceptors are 3-beta-hydroxysterols with a planar ring CC system. // ID 2.3.1.78 DE Heparan-alpha-glucosaminide N-acetyltransferase. CA Acetyl-CoA + heparan alpha-D-glucosaminide = CoA + heparan CA N-acetyl-alpha-D-glucosaminide. CC -!- Brings about the acetylation of glucosamine groups of heparan CC sulfate and heparin from which the sulfate has been removed. CC -!- Also acts on heparin. CC -!- Not identical with EC 2.3.1.3 or EC 2.3.1.4. // ID 2.3.1.79 DE Maltose O-acetyltransferase. CA Acetyl-CoA + maltose = CoA + acetyl-maltose. CC -!- Not identical with EC 2.3.1.18. PR PROSITE; PDOC00094; DR P37515, MAA_BACSU ; P77791, MAA_ECOLI ; // ID 2.3.1.80 DE Cysteine-S-conjugate N-acetyltransferase. CA Acetyl-CoA + an S-substituted L-cysteine = CoA + an S-substituted CA N-acetyl-L-cysteine. CC -!- S-benzyl-L-cysteine can act as acceptor, and, in decreasing order of CC activity, S-butyl-L-cysteine, S-propyl-L-cysteine, O-benzyl-L-serine CC and S-ethyl-L-cysteine. // ID 2.3.1.81 DE Aminoglycoside N(3')-acetyltransferase. AN Gentamicin-(3)-N-acetyltransferase. CA Acetyl-CoA + a 2-deoxystreptamine antibiotic = CoA + N(3')-acetyl-2- CA deoxystreptamine antibiotic. CC -!- A wide range of antibiotics containing the 2-deoxystreptamine ring CC can act as acceptor, including gentamicin, kanamycin, tobramycin, CC neomycin and apramycin. CC -!- Different from EC 2.3.1.60. DR P29807, AAC2_ACIBA; P13246, AAC2_SALSP; P29808, AAC3_PSEAE; DR P13245, AAC3_SALSP; Q01515, AAC3_SERMA; P08988, AAC4_SALSP; DR P30180, AAC7_STRRM; P29809, AAC8_STRFR; P29810, AAC9_MICCH; // ID 2.3.1.82 DE Kanamycin 6'-N-acetyltransferase. AN Aminoglycoside N(6')-acetyltransferase. AN 6'-aminoglycoside-N-acetyltransferase. AN AAC(6'). CA Acetyl-CoA + kanamycin = CoA + N(6')-acetylkanamycin. CC -!- The antibiotics kanamycin A, kanamycin B, neomycin, gentamicin C1a, CC gentamicin C2, sisomicin and tobramycin are substrates. CC -!- The antibiotic paromomycin is not a substrate. CC -!- The 6-amino group of the purpurosamine ring is acetylated. CC -!- Formerly EC 2.3.1.55. DR P10051, AAC6_CITDI; P50858, AAC6_ENTAE; P19650, AAC6_KLEPN; DR P20092, AAC6_SERMA; // ID 2.3.1.83 DE Phosphatidylcholine--dolichol O-acyltransferase. CA 3-sn-phosphatidylcholine + dolichol = 1-acyl-sn-glycero-3-phosphocholine CA + acyldolichol. // ID 2.3.1.84 DE Alcohol O-acetyltransferase. AN AATASE. CA Acetyl-CoA + an alcohol = CoA + an acetyl ester. CC -!- Acts on a range of short-chain aliphatic alcohols, including methanol CC and ethanol. DR P40353, ATF1_YEAST; P53296, ATF2_YEAST; // ID 2.3.1.85 DE Fatty-acid synthase. CA Acetyl-CoA + N malonyl-CoA + 2N NADPH = a long-chain fatty acid + (N+1) CA CoA + N CO(2) + 2N NADP(+). CC -!- The animal enzyme is a multifunctional protein catalyzing the CC reactions of EC 2.3.1.38, EC 2.3.1.39, EC 2.3.1.41, EC 1.1.1.100, CC EC 4.2.1.61, EC 1.3.1.10 and EC 3.1.2.14. DR P36189, FAS_ANSAN ; P08757, FAS_CAPHI ; P12276, FAS_CHICK ; DR P49327, FAS_HUMAN ; P19096, FAS_MOUSE ; P07855, FAS_RABIT ; DR P12785, FAS_RAT ; // ID 2.3.1.86 DE Fatty-acyl-CoA synthase. AN Yeast fatty acid synthase. CA Acetyl-CoA + N malonyl-CoA + 2N NADH + 2N NADPH = a long-chain CA acyl-CoA + N CoA + N CO(2) + 2N NAD(+) + 2N NADP(+). CC -!- The yeast enzyme is a multifunctional protein catalyzing the CC reactions of EC 2.3.1.38, EC 2.3.1.39, EC 2.3.1.41, EC 1.1.1.100, CC EC 4.2.1.61 and EC 1.3.1.9. DR P34731, FAS1_CANAL; Q9UUG0, FAS1_SCHPO; P34229, FAS1_YARLI; DR P07149, FAS1_YEAST; P43098, FAS2_CANAL; P15368, FAS2_PENPA; DR Q10289, FAS2_SCHPO; P19097, FAS2_YEAST; // ID 2.3.1.87 DE Aralkylamine N-acetyltransferase. AN Serotonin N-acetyltransferase. AN Serotonin acetyltransferase. AN Serotonin acetylase. CA Acetyl-CoA + an aralkylamine = CoA + an N-acetylaralkylamine. CC -!- Narrow specificity towards aralkylamines, including serotonin. CC -!- Not identical with EC 2.3.1.5. DR O02785, SNAT_BOVIN; P79774, SNAT_CHICK; Q16613, SNAT_HUMAN; DR O97756, SNAT_MACMU; Q9R0A9, SNAT_MESAU; O88816, SNAT_MOUSE; DR Q64666, SNAT_RAT ; Q29495, SNAT_SHEEP; // ID 2.3.1.88 DE Peptide alpha-N-acetyltransferase. AN Beta-endorphin acetyltransferase. CA Acetyl-CoA + peptide = CoA + N-acetylpeptide. CC -!- Acetylates N-terminal alanine, serine, methionine and glutamate CC residues in a number of peptides and proteins, including beta- CC endorphin, corticotropins and melanotropin (cf. EC 2.3.1.108). DR P12945, NAT1_YEAST; P37293, NAT2_YEAST; // ID 2.3.1.89 DE Tetrahydrodipicolinate N-acetyltransferase. AN Tetrahydrodipicolinate acetylase. CA Acetyl-CoA + L-2,3,4,5-tetrahydrodipicolinate = CoA + L-2-acetamido- CA 6-oxoheptanedioate. // ID 2.3.1.90 DE Beta-glucogallin O-galloyltransferase. CA 2 1-O-galloyl-beta-D-glucose = D-glucose + 1-O,6-O-digalloyl-beta- CA D-glucose. CC -!- Beta-glucogallin can act as donor and as acceptor. CC -!- Digalloylglucose can also act as acceptor, with the formation of CC 1-O,2-O,6-O-trigalloylglucose. // ID 2.3.1.91 DE Sinapoylglucose--choline O-sinapoyltransferase. CA 1-O-sinapoyl-beta-D-glucose + choline = D-glucose + O-sinapoylcholine. // ID 2.3.1.92 DE Sinapoylglucose--malate O-sinapoyltransferase. CA 1-O-sinapoyl-beta-D-glucose + (S)-malate = D-glucose + sinapoyl-(S)- CA malate. // ID 2.3.1.93 DE 13-hydroxylupinine O-tigloyltransferase. CA (E)-2-methylcrotonoyl-CoA + 13-hydroxylupinine = CoA + 13- CA (2-methylcrotonoyl)oxylupinine. CC -!- Benzoyl-CoA and, more slowly, pentanoyl-CoA, 3-methylbutanoyl-CoA CC and butanoyl-CoA can act as acyl donors. CC -!- Involved in the synthesis of lupinine alkaloids. // ID 2.3.1.94 DE Erythronolide synthase. AN Erythronolide condensing enzyme. CA 6 malonyl-CoA + propionyl-CoA = 7 CoA + 6-deoxyerythronolide B. CC -!- The product, which contains a 14-membered lactone ring, is an CC intermediate in the biosynthesis of erythromycin antibiotics (cf. CC EC 2.3.1.74). DR Q03131, ERY1_SACER; Q03132, ERY2_SACER; Q03133, ERY3_SACER; // ID 2.3.1.95 DE Trihydroxystilbene synthase. AN Resveratrol synthase. AN Stilbene synthase. CA 3 malonyl-CoA + 4-coumaroyl-CoA = 4 CoA + 3,4',5-trihydroxystilbene. CC -!- Not identical with EC 2.3.1.74 or EC 2.3.1.146. PR PROSITE; PDOC00403; DR P20178, THS1_ARAHY; P28343, THS1_VITVI; P20077, THS2_ARAHY; DR P51070, THS2_VITVI; P51069, THS3_ARAHY; P51071, THS3_VITVI; // ID 2.3.1.96 DE Glycoprotein N-palmitoyltransferase. CA Palmitoyl-CoA + glycoprotein = CoA + N-palmitoylglycoprotein. CC -!- Acts on glycoprotein from mucus. Activated by 1,4-dithiothreitol. // ID 2.3.1.97 DE Glycylpeptide N-tetradecanoyltransferase. AN Peptide N-myristoyltransferase. AN Peptide N-tetradecanoyltransferase. CA Tetradecanoyl-CoA + glycyl-peptide = CoA + N-tetradecanoylglycyl- CA peptide. CC -!- The enzyme from yeast is highly specific for tetradecanoyl-CoA, and CC for N-terminal glycine in oligopeptides containing serine in the CC 5-position. Tthe enzyme from mammalian heart transfers acyl groups CC to a specific acceptor protein of 51 Kd. PR PROSITE; PDOC00752; DR P31717, NMT1_BOVIN; P30419, NMT1_HUMAN; O70310, NMT1_MOUSE; DR Q9N181, NMT2_BOVIN; O60551, NMT2_HUMAN; O70311, NMT2_MOUSE; DR P34763, NMT_AJECA ; Q9UVX3, NMT_ASPFU ; P46548, NMT_CAEEL ; DR P30418, NMT_CANAL ; O74234, NMT_CANGA ; P34809, NMT_CRYNE ; DR O61613, NMT_DROME ; O43010, NMT_SCHPO ; P14743, NMT_YEAST ; // ID 2.3.1.98 DE Chlorogenate--glucarate O-hydroxycinnamoyltransferase. CA Chlorogenate + glucarate = quinate + 2-O-caffeoylglucarate. CC -!- Galactarate can act as acceptor, more slowly. CC -!- Involved with EC 2.3.1.99 in the formation of caffeoylglucarate in CC tomato. // ID 2.3.1.99 DE Quinate O-hydroxycinnamoyltransferase. AN Hydroxycinnamoyl coenzyme A-quinate transferase. CA Feruloyl-CoA + quinate = CoA + O-feruloylquinate. CC -!- Caffeoyl-CoA and 4-coumaroyl-CoA can also act as donors, more CC slowly. CC -!- Involved in the biosynthesis of chlorogenic acid in sweet potato and, CC with EC 2.3.1.98 in the formation of caffeoyl-CoA in tomato. // ID 2.3.1.100 DE Myelin-proteolipid O-palmitoyltransferase. AN Myelin PLP acyltransferase. AN Acyl-protein synthase. CA Palmitoyl-CoA + [myelin proteolipid] = CoA + [myelin proteolipid] CA O-palmitoylprotein. CC -!- The enzyme in brain transfers long-chain acyl residues to the CC endogenous myelin proteolipid. // ID 2.3.1.101 DE Formylmethanofuran--tetrahydromethanopterin N-formyltransferase. CA N-formylmethanofuran + 5,6,7,8-tetrahydromethanopterin = methanofuran + CA 5-formyl-5,6,7,8-tetrahydromethanopterin. CC -!- Methanofuran is a complex 4-substituted furfurylamine. CC -!- Involved in the formation of methane from CO(2) in Methanobacterium CC thermoautotrophicum. DR O28076, FTR_ARCFU ; Q8TUQ5, FTR_METAC ; P55301, FTR_METBA ; DR Q9ADT1, FTR_METCA ; Q49118, FTR_METEX ; Q49168, FTR_METFE ; DR Q57766, FTR_METJA ; Q49610, FTR_METKA ; Q8PXA1, FTR_METMA ; DR P21348, FTR_METTH ; // ID 2.3.1.102 DE N(6)-hydroxylysine O-acetyltransferase. CA Acetyl-CoA + N(6)-hydroxy-L-lysine = CoA + N(6)-acetyl-N(6)-hydroxy-L- CA lysine. CC -!- Involved in the synthesis of aerobactin from lysine in a strain of CC E.coli. // ID 2.3.1.103 DE Sinapoylglucose--sinapoylglucose O-sinapoyltransferase. CA 2 1-O-sinapoyl beta-D-glucoside = D-glucose + 1,2-bis-O-sinapoyl CA beta-D-glucoside. // ID 2.3.1.104 DE 1-alkenylglycerophosphocholine O-acyltransferase. CA Acyl-CoA + 1-alkenylglycerophosphocholine = CoA + 1-alkenyl-2- CA acylglycerophosphocholine. CC -!- Not identical with EC 2.3.1.121. // ID 2.3.1.105 DE Alkylglycerophosphate 2-O-acetyltransferase. CA Acetyl-CoA + 1-alkyl-sn-glycerol 3-phosphate = CoA + 1-alkyl-2-acetyl- CA sn-glycerol 3-phosphate. CC -!- Involved in the biosynthesis of thrombocyte activating factor in CC animal tissues. // ID 2.3.1.106 DE Tartronate O-hydroxycinnamoyltransferase. AN Tartronate sinapoyltransferase. AN Hydroxycinnamoyl-coenzyme-A:tartronate hydroxycinnamoyltransferase. CA Sinapoyl-CoA + 2-hydroxymalonate = CoA + sinapoyltartronate. CC -!- 4-Coumaroyl-CoA (4-hydroxycinnamoyl-CoA), caffeoyl-CoA (3,4- CC dihydroxycinnamoyl-CoA) and feruloyl-CoA (4-hydroxy-3- CC methoxycinnamoyl-CoA) can also act as donors for the enzyme from CC the mung bean (Vigna radiata). // ID 2.3.1.107 DE 17-O-deacetylvindoline O-acetyltransferase. CA Acetyl-CoA + 17-O-deacetylvindoline = CoA + vindoline. CC -!- Catalyzes the final step in the biosynthesis of vindoline from CC tabersonine in Catharanthus roseus. // ID 2.3.1.108 DE Tubulin N-acetyltransferase. AN Alpha-tubulin acetylase. CA Acetyl-CoA + [alpha-tubulin] L-lysine = CoA + [alpha-tubulin] N(6)- CA acetyl-L-lysine. CC -!- The enzyme from Chlamydomonas flagella also acetylates mammalian CC brain alpha-tubulin. // ID 2.3.1.109 DE Arginine N-succinyltransferase. CA Succinyl-CoA + L-arginine = CoA + N(2)-succinyl-L-arginine. CC -!- Also acts on L-ornithine. DR P76218, ASTA_ECOLI; P80357, ASTA_PSEAE; P80358, ASTG_PSEAE; // ID 2.3.1.110 DE Tyramine N-feruloyltransferase. CA Feruloyl-CoA + tyramine = CoA + N-feruloyltyramine. CC -!- Cinnamoyl-CoA, 4-coumaroyl-CoA and sinapoyl-CoA can also act as CC donors. CC -!- Some aromatic amines can act as acceptors. DR P80969, THTA_TOBAC; Q9SMB8, THTB_TOBAC; // ID 2.3.1.111 DE Mycocerosate synthase. CA Acyl-CoA + N methylmalonyl-CoA + 2N NADPH = multi-methyl-branched CA acyl-CoA + N CoA + N CO(2) + 2N NADP(+). CC -!- Elongates CoA esters of fatty acids from C(6) to C(20) by CC incorporation of methylmalonyl, but not malonyl, residues, to form CC multimethyl-branched fatty-acyl-CoA such as 2,4,6,8-tetramethyl- CC octosanoyl-CoA. // ID 2.3.1.112 DE D-tryptophan N-malonyltransferase. CA Malonyl-CoA + D-tryptophan = CoA + N(2)-malonyl-D-tryptophan. CC -!- 1-aminocyclopropane-1-carboxylate can act instead of malonyl-CoA. // ID 2.3.1.113 DE Anthranilate N-malonyltransferase. CA Malonyl-CoA + anthranilate = CoA + N-malonylanthranilate. // ID 2.3.1.114 DE 3,4-dichloroaniline N-malonyltransferase. CA Malonyl-CoA + 3,4-dichloroaniline = CoA + N-(3,4-dichlorophenyl)malonate. // ID 2.3.1.115 DE Isoflavone-7-O-beta-glucoside 6''-O-malonyltransferase. AN Flavone/flavonol 7-O-beta-D-glucoside malonyltransferase. CA Malonyl-CoA + biochanin A = CoA + 6''-malonyl-biochanin A. CC -!- The 6-position of the glucose residue of formononetin can also act CC as acceptor. CC -!- Some other 7-O-glucosides of isoflavones, flavones and flavonols can CC also act, more slowly. // ID 2.3.1.116 DE Flavonol-3-O-beta-glucoside O-malonyltransferase. CA Malonyl-CoA + flavonol 3-O-beta-D-glucoside = CoA + malonyl-flavonol CA 3-O-beta-D-glucoside. // ID 2.3.1.117 DE 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase. AN Tetrahydrodipicolinate succinylase. AN Tetrahydrodipicolinate N-succinyltransferase. AN Tetrahydrodipicolinate succinyltransferase. AN Succinyl-CoA:tetrahydrodipicolinate N-succinyltransferase. CA Succinyl-CoA + (R)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + CA H(2)O = CoA + (R)-2-(succinylamino)-6-oxoheptanedioate. CC -!- Involved in the biosynthesis of lysine in bacteria, blue-green algae CC and higher plants. CC -!- Earlier erroneously called 2,3,4,5-tetrahydropyridine-2- CC carboxylate N-succinyltransferase. PR PROSITE; PDOC00094; DR P41396, DAPD_ACTPL; Q9ZEX2, DAPD_BORPE; P57323, DAPD_BUCAI; DR O85290, DAPD_BUCAP; P03948, DAPD_ECOLI; P45284, DAPD_HAEIN; DR P41397, DAPD_KLEPN; P56220, DAPD_MYCBO; Q9ZDX0, DAPD_RICPR; // ID 2.3.1.118 DE N-hydroxyarylamine O-acetyltransferase. AN Arylhydroxamate N,O-acetyltransferase. AN Arylamine N-acetyltransferase. CA Acetyl-CoA + an N-hydroxyarylamine = CoA + an N-acetoxyarylamine. CC -!- The enzyme from liver, but not that from bacteria, can also catalyze CC N-acetylation of arylamines and N,O-acetylation of arylhydroxamates. DR P77567, NHOA_ECOLI; Q00267, NHOA_SALTY; // ID 2.3.1.119 DE Icosanoyl-CoA synthase. AN Acyl-CoA elongase. CA Stearoyl-CoA + malonyl-CoA + 2 NAD(P)H = icosanoyl-CoA + CO(2) + 2 CA NAD(P)(+). CC -!- Icosanoyl-CoA can act in place of stearoyl-CoA. CC -!- The membrane enzyme brings about the elongation of these long-chain CC fatty-acyl-CoA's. // ID 2.3.1.120 DE Deleted entry. // ID 2.3.1.121 DE 1-alkenylglycerophosphoethanolamine O-acyltransferase. CA Acyl-CoA + 1-alkenylglycerophosphoethanolamine = CoA + 1-alkenyl-2- CA acyl-glycerophosphoethanolamine. CC -!- Long-chain unsaturated acyl-CoA's are the best substrates. CC -!- Not identical with EC 2.3.1.104. // ID 2.3.1.122 DE Trehalose O-mycolyltransferase. CA 2 alpha,alpha'-trehalose 6-mycolate = alpha,alpha'-trehalose + CA alpha,alpha'-trehalose 6,6'-bismycolate. CC -!- Catalyzes the exchange of mycolic acid between trehalose, trehalose CC mycolate and trehalose bismycolate. CC -!- Trehalose 6-palmitate can also act as a donor. // ID 2.3.1.123 DE Dolichol O-acyltransferase. CA Palmitoyl-CoA + dolichol = CoA + dolichyl palmitate. CC -!- Other acyl-CoA's can act, more slowly. CC -!- Alpha-saturated dolichols are acylated more rapidly than the CC alpha-unsaturated analogs. // ID 2.3.1.124 DE Deleted entry. // ID 2.3.1.125 DE 1-alkyl-2-acetylglycerol O-acyltransferase. AN 1-hexadecyl-2-acetylglycerol acyltransferase. CA Acyl-CoA + 1-O-alkyl-2-acetyl-sn-glycerol = CoA + 1-O-alkyl-2-acetyl- CA 3-acyl-sn-glycerol. CC -!- A number of acyl-CoA's can act as acyl donor; maximum activity is CC obtained with linoleoyl-CoA. CC -!- Not identical with EC 2.3.1.20. // ID 2.3.1.126 DE Isocitrate O-dihydroxycinnamoyltransferase. CA Caffeoyl-CoA + isocitrate = CoA + 2-caffeoylisocitrate. CC -!- Feruloyl-CoA and 4-coumaroyl-CoA can act as donors. // ID 2.3.1.127 DE Ornithine N-benzoyltransferase. CA 2 benzoyl-CoA + L-ornithine = 2 CoA + N(2),N(5)-dibenzoyl-L-ornithine. // ID 2.3.1.128 DE Ribosomal-protein-alanine N-acetyltransferase. CA Acetyl-CoA + ribosomal-protein L-alanine = CoA + ribosomal-protein CA N-acetyl-L-alanine. CC -!- A groups of enzymes in E.coli which acetylate the N-terminal alanine CC residues of specific ribosomal proteins (cf. EC 2.3.1.88). DR P09453, RIMI_ECOLI; P44305, RIMI_HAEIN; P09454, RIMJ_ECOLI; // ID 2.3.1.129 DE Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase. AN UDP-N-acetylglucosamine acyltransferase. CA (R)-3-hydroxytetradecanoyl-[acyl-carrier protein] + UDP-N- CA acetylglucosamine = [acyl-carrier protein] + UDP-3-O-(3- CA hydroxytetradecanoyl)-N-acetylglucosamine. CC -!- Involved with EC 2.4.1.182 and EC 2.7.1.130 in the biosynthesis of CC the phosphorylated glycolipid, lipid A, in the outer membrane of CC E.coli. PR PROSITE; PDOC00094; DR Q8UFL3, LPXA_AGRT5; O66862, LPXA_AQUAE; P54080, LPXA_BRUAB; DR Q8YHG8, LPXA_BRUME; Q9PIM1, LPXA_CAMJE; Q9A715, LPXA_CAUCR; DR Q9PJL1, LPXA_CHLMU; Q9Z7Q4, LPXA_CHLPN; Q8KAZ0, LPXA_CHLTE; DR O84536, LPXA_CHLTR; Q46481, LPXA_CHRVI; Q9TLX4, LPXA_CYACA; DR Q8X8X8, LPXA_ECO57; P10440, LPXA_ECOLI; Q8RFU2, LPXA_FUSNN; DR P43887, LPXA_HAEIN; Q9ZJL7, LPXA_HELPJ; O25927, LPXA_HELPY; DR Q9JX26, LPXA_NEIMA; P95379, LPXA_NEIMB; Q9CJK8, LPXA_PASMU; DR P72215, LPXA_PROMI; Q9X6P4, LPXA_PSEAE; Q8XZH9, LPXA_RALSO; DR Q98MC6, LPXA_RHILO; Q92Q45, LPXA_RHIME; Q92JQ9, LPXA_RICCN; DR Q9ZED5, LPXA_RICPR; P32199, LPXA_RICRI; Q8Z9A2, LPXA_SALTI; DR P32200, LPXA_SALTY; Q55746, LPXA_SYNY3; Q9KPW4, LPXA_VIBCH; DR Q87ME9, LPXA_VIBPA; Q8DBE9, LPXA_VIBVU; Q8D2H3, LPXA_WIGBR; DR Q8PML7, LPXA_XANAC; Q8PAW5, LPXA_XANCP; Q9PEI5, LPXA_XYLFA; DR Q87EI4, LPXA_XYLFT; P32201, LPXA_YEREN; Q8ZH56, LPXA_YERPE; // ID 2.3.1.130 DE Galactarate O-hydroxycinnamoyltransferase. CA Feruloyl-CoA + galactarate = CoA + O-feruloylgalactarate. CC -!- Sinapoyl-CoA and 4-coumaroyl-CoA can also act as donors. // ID 2.3.1.131 DE Glucarate O-hydroxycinnamoyltransferase. CA Sinapoyl-CoA + glucarate = CoA + O-sinapoylglucarate. CC -!- 4-coumaroyl-CoA, feruloyl-CoA and caffeoyl-CoA can also act as CC donors, more slowly. // ID 2.3.1.132 DE Glucarolactone O-hydroxycinnamoyltransferase. CA Sinapoyl-CoA + glucarolactone = CoA + O-sinapoylglucarolactone. CC -!- 4-coumaroyl-CoA, feruloyl-CoA and caffeoyl-CoA can also act as CC donors, more slowly. // ID 2.3.1.133 DE Shikimate O-hydroxycinnamoyltransferase. CA 4-coumaroyl-CoA + shikimate = CoA + 4-coumaroylshikimate. CC -!- Caffeoyl-CoA, feruloyl-CoA and sinapoyl-CoA can also act as donors, CC more slowly. // ID 2.3.1.134 DE Galactolipid O-acyltransferase. AN Galactolipid:galactolipid acyltransferase. CA 2 mono-beta-D-galactosyldiacylglycerol = acylmono-beta-D- CA galactosyldiacylglycerol + mono-beta-D-galactosylacylglycerol. CC -!- Di-D-galactosyldiacylglycerol can also act as acceptor. // ID 2.3.1.135 DE Phosphatidylcholine--retinol O-acyltransferase. AN Lecithin-retinol acyltransferase. CA Phosphatidylcholine + retinol-[cellular-retinol-binding-protein] = CA 2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding- CA protein]. CC -!- Specific for transfer of the sn-1-acyl residue of phosphatidyl- CC choline. // ID 2.3.1.136 DE Polysialic-acid O-acetyltransferase. CA Acetyl-CoA + an alpha-2,8-linked polymer of sialic acid = CoA + CA polysialic acid acetylated at O-7 or O-9. CC -!- Acts only on substrates containing more than 14 sialosyl residues. CC -!- Catalyzes the modification of capsular polysaccharides in some CC strains of E.coli. // ID 2.3.1.137 DE Carnitine O-octanoyltransferase. CA Octanoyl-CoA + L-carnitine = CoA + L-octanoylcarnitine. CC -!- Acts on a range of acyl-CoA's, with optimal activity with C(6) or CC C(8) acyl groups. CC -!- Cf. EC 2.3.1.7 and EC 2.3.1.21. // ID 2.3.1.138 DE Putrescine N-hydroxycinnamoyltransferase. CA Caffeoyl-CoA + putrescine = CoA + N-caffeoylputrescine. CC -!- Feruloyl-CoA, cinnamoyl-CoA and sinapoyl-CoA can also act as donors, CC more slowly. // ID 2.3.1.139 DE Ecdysone O-acyltransferase. CA Palmitoyl-CoA + ecdysone = CoA + ecdysone palmitate. // ID 2.3.1.140 DE Rosmarinate synthase. CA Caffeoyl-CoA + 3-(3,4-dihydroxyphenyl)lactate = CoA + rosmarinate. CC -!- Involved with EC 1.1.1.237 in the biosynthesis of rosmarinic acid. // ID 2.3.1.141 DE Galactosylacylglycerol O-acyltransferase. CA Acyl-[acyl-carrier protein] + sn-3-D-galactosyl-sn-2-acylglycerol = CA [acyl-carrier protein] + D-galactosyldiacylglycerol. CC -!- Transfers long-chain acyl groups to the sn-1 position of the CC glycerol residues. // ID 2.3.1.142 DE Glycoprotein O-fatty-acyltransferase. CA Palmitoyl-CoA + mucus glycoprotein = CoA + O-palmitoylglycoprotein. // ID 2.3.1.143 DE Beta-glucogallin--tetrakisgalloylglucose O-galloyltransferase. CA 1-O-galloyl-beta-D-glucose + 1,2,3,6-tetrakis-O-galloyl-beta-D-glucose = CA D-glucose + 1,2,3,4,6-pentakis-O-galloyl-beta-D-glucose. // ID 2.3.1.144 DE Anthranilate N-benzoyltransferase. CA Benzoyl-CoA + anthranilate = CoA + N-benzoylanthranilate. CC -!- Cinnamoyl-CoA, 4-coumaroyl-CoA and salicyloyl-CoA can act as donors, CC more slowly. CC -!- Involved in the biosynthesis of phytoalexins. // ID 2.3.1.145 DE Piperidine N-piperoyltransferase. CA (E,E)-piperoyl-CoA + piperidine = CoA + N-[(E,E)-piperoyl]-piperidine. CC -!- Pyrrolidine and 3-pyrroline can also act as acceptors, more slowly. // ID 2.3.1.146 DE Pinosylvin synthase. AN Stilbene synthase. CA 3 malonyl-CoA + cinnamoyl-CoA = 4 CoA + pinosylvin + 3 CO(2). CC -!- Not identical with EC 2.3.1.74 or EC 2.3.1.95. // ID 2.3.1.147 DE Glycerophospholipid arachidonoyl-transferase (CoA-independent). CA 1-organyl-2-arachidonoyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso- CA sn-glycero-3-phosphoethanolamine = 1-organyl-2-arachidonyl-sn-glycero-3- CA phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine. CC -!- Catalyzes the transfer of arachidonate and other polyenoic fatty CC acids from intact choline or ethanolamine-containing CC glycerophospholipids to the sn-2 position of a lyso- CC glycerophospholipid. CC -!- The organyl group on sn-1 of the donor or acceptor molecule can be CC alkyl, acyl or alk-1-enyl. The term 'radyl' has sometimes been used CC to refer to such substituting groups. CC -!- Differs from EC 2.3.1.148 in not requiring CoA and in its specificity CC for poly-unsaturated acyl groups. // ID 2.3.1.148 DE Glycerophospholipid acyltransferase (CoA-dependent). CA 1-organyl-2-acyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn- CA glycero-3-phosphoethanolamine = 1-organyl-2-acyl-sn-glycero-3- CA phosphoethanolamine + 1-organyl-2-lyso-sn-glycero-3-phosphocholine. CF Coenzyme-A. CC -!- Catalyzes the transfer of fatty acids from intact choline- or CC ethanolamine-containing glycerophospholipids to the sn-2 position of CC a lyso-glycerophospholipid. CC -!- The organyl group on sn-1 of the donor or acceptor molecule can be CC alkyl, acyl or alk-1-enyl. The term 'radyl' has sometimes been used CC to refer to such substituting groups. CC -!- Differs from EC 2.3.1.147 in requiring CoA and not favoring the CC transfer of polyunsaturated acyl groups. // ID 2.3.1.149 DE Platelet-activating factor acetyltransferase. AN PAF acetyltransferase. CA 1-alkyl-2-acetyl-sn-glycero-3-phosphocholine + 1-organyl-2-lyso-sn- CA glycero-3-phospholipid = 1-organyl-2-lyso-sn-glycero-3-phosphocholine + CA 1-alkyl'-2-acetyl-sn-glycero-3-phospholipid. CC -!- Catalyzes the transfer of the acetyl group from 1-alkyl-2-acyl-sn- CC glycero-3-phosphocholine (platelet-activating factor) to the sn-2 CC position of lyso-glycerophospholipids containing ethanolamine, CC choline, serine, inositol or phosphate groups at the sn-3 position CC as well as to sphingosine and long-chain fatty alcohols. CC -!- The organyl group can be alkyl, acyl or alk-1-enyl (sometimes also CC collectively referred to as 'radyl'). // ID 2.3.1.150 DE Salutaridinol 7-O-acetyltransferase. CA Acetyl-CoA + salutaridinol = CoA + 7-O-acetylsalutaridinol. CC -!- At higher pH values the product, 7-O-acetylsalutaridinol, CC spontaneously closes the 4->5 oxide bridge by allylic elimination to CC form the morphine precursor thebaine. CC -!- From the opium poppy plant, Papaver somniferum. // ID 2.3.1.151 DE Benzophenone synthase. CA 3 malonyl-CoA + 3-hydroxybenzoyl-CoA = 4 CoA + 2,3',4,6- CA tetrahydroxybenzophenone + 3 CO(2). CC -!- Involved in the biosynthesis of plant xanthomes. CC -!- Benzoyl-CoA can replace 3-hydroxybenzoyl-CoA. // ID 2.3.1.152 DE Alcohol O-cinnamoyltransferase. CA 1-O-trans-cinnamoyl-beta-D-glucopyranose + ROH = alkyl cinnamate + CA glucose. CC -!- Acceptor alcohols (ROH) include methanol, ethanol and propanol. CC -!- No cofactors are required as 1-O-trans-cinnamoyl-beta-D-glucopyranose CC itself is an 'energy-rich' (activated) acyl-donor, comparable to CoA- CC thioesters. CC -!- 1-O-trans-Cinnamoyl-beta-D-gentobiose can also act as the acyl donor, CC but with much less affinity. // ID 2.3.1.153 DE Anthocyanin 5-aromatic acyltransferase. CA Hydroxycinnamoyl-CoA + anthocyanidin-3,5-diglucoside = CoA + CA anthocyanidin 3-glucoside-5-hydroxycinnamoylglucoside. CC -!- Transfers hydroxycinnamoyl group only to the C-5 glucoside of CC anthocyanin. CC -!- Malonyl-CoA cannot act as a donor. // ID 2.3.1.154 DE Propionyl-CoA C(2)-trimethyltridecanoyltransferase. AN 3-oxopristanoyl-CoA hydrolase. AN 3-oxopristanoyl-CoA thiolase. CA 4,8,12-trimethyltridecanoyl-CoA + propanoyl-CoA = 3-oxopristanoyl-CoA + CA CoA. CC -!- The peroxisomal protein sterol carrier protein X (SCPx) combines CC this thiolase activity with its carrier function, and is involved in CC branched chain fatty acid beta-oxidation in peroxisomes. CC -!- It also acts on 3-oxopalmitoyl-CoA as a substrate but differs from CC EC 2.3.1.16 which has little activity towards the 3-oxoacyl-CoA CC esters of 2-methyl-branched chain fatty acids such as CC 3-oxopristanoyl-CoA. // ID 2.3.1.155 DE Acetyl-CoA C-myristoyltransferase. AN Myristoyl-CoA C-acetyltransferase. AN 3-oxopalmitoyl-CoA hydrolase. AN 3-oxopalmitoyl-CoA-CoA acetyltransferase. CA Myristoyl-CoA + acetyl-CoA = 3-oxopalmitoyl-CoA + CoA. CC -!- A peroxisomal enzyme involved in branched chain fatty acid CC beta-oxidation in peroxisomes. CC -!- It differs from EC 2.3.1.154 in not being active towards CC 3-oxopristanoyl-CoA. // ID 2.3.1.156 DE Phloroisovalerophenone synthase. AN Valerophenone synthase. AN 3-methyl-1-(trihydroxyphenyl)butan-1-one synthase. CA Isovaleryl-CoA + 3 malonyl-CoA = 4 CoASH + 3 CO(2) + 3-methyl-1- CA (2,4,6-trihydroxyphenyl)butan-1-one. CC -!- Closely related to EC 2.3.1.74. CC -!- The product, 3-methyl-1-(2,4,6-trihydroxyphenyl)butan-1-one, is CC phloroisovalerophenone. CC -!- Also acts on isobutyryl-CoA as substrate to give CC phlorisobutyrophenone. CC -!- The products are intermediates in the biosynthesis of the bitter CC (alpha) acids in hops (Humulus lupulus). PR PROSITE; PDOC00403; DR O80400, VPS_HUMLU ; Q9SLX9, VPS_PSINU ; // ID 2.3.1.157 DE Glucosamine-1-phosphate N-acetyltransferase. CA Acetyl-CoA + D-glucosamine 1-phosphate = CoA + N-acetyl-D-glucosamine CA 1-phosphate. CC -!- The enzyme from several bacteria has been shown to be bifunctional CC and also to possess the activity of EC 2.7.7.23. // ID 2.3.1.158 DE Phospholipid:diacylglycerol acyltransferase. AN PDAT. CA Phospholipid + 1,2-diacylglycerol = lysophospholipid + CA triacylglycerol. CC -!- This enzyme differs from EC 2.3.1.20 by synthesising CC triacylglycerol using an acyl-CoA-independent mechanism. CC -!- The specificity of the enzyme for the acyl group in the CC phospholipid varies with species, e.g., the enzyme from castor CC bean (Ricinus communis) preferentially incorporates vernoloyl CC (12,13-epoxyoctadec-9-enoyl) groups into triacylglycerol, whereas CC that from the hawk's beard (Crepis palaestina) incorporates both CC ricinoleoyl (12-hydroxyoctadec-9-enoyl) and vernoloyl groups. CC -!- The enzyme from the yeast Saccharomyces cerevisiae specifically CC transfers acyl groups from the sn-2 position of the phospholipid CC to diacylglycerol, thus forming an sn-1-lysophospholipid. DR O94680, PDAT_SCHPO; P40345, PDAT_YEAST; // ID 2.3.1.159 DE Acridone synthase. CA 3 malonyl-CoA + N-methylanthraniloyl-CoA = 4 CoA + 1,3-dihydroxy-N- CA methylacridone + 3 CO(2). PR PROSITE; PDOC00403; DR Q9FSC0, ACS2_RUTGR; Q9FSC2, ACS3_RUTGR; Q9FSC1, ACS4_RUTGR; // ID 2.3.1.160 DE Vinorine synthase. CA Acetyl-CoA + 16-epivellosimine = CoA + vinorine. CC -!- The reaction proceeds in two stages. CC -!- The indole nitrogen of 16-epivellosimine interacts with its CC aldehyde group giving an hydroxy-substituted new ring. CC -!- This alcohol is then acetylated. CC -!- Also acts on gardneral (11-methoxy-16-epivellosimine). CC -!- Generates the ajmalan skeleton, which forms part of the route to CC ajmaline. // ID 2.3.1.161 DE Lovastatin nonaketide synthase. CA Acetyl-CoA + 8 malonyl-CoA + 11 NADP(H) + S-adenosyl-L-methionine = CA dihydromonacolin L + 9 CoA + 8 CO(2) + 11 NADP(+) + S-adenosyl-L- CA homocysteine + 6 H(2)O. CC -!- The microbial enzyme is a multi-functional protein catalyzing many CC of the chain building reactions of EC 2.3.1.85 as well as a CC reductive methylation and a Diels-Alder reaction. // ID 2.3.1.162 DE Taxadien-5-alpha-ol O-acetyltransferase. AN Taxa-4(20),11(12)-dien-5alpha-ol-O-acetyltransferase. AN Acetyl coenzyme A:taxa-4(20),11(12)-dien-5-alpha-ol O-acetyl transferase. AN Taxadienol acetyltransferase. CA Acetyl-CoA + taxa-4(20),11-dien-5-alpha-ol = CoA + taxa-4(20),11-dien- CA 5-alpha-yl acetate. DR Q8S9G6, T5AT_TAXCH; Q9M6F0, T5AT_TAXCU; // ID 2.3.1.163 DE 10-hydroxytaxane O-acetyltransferase. AN Acetyl coenzyme A:10-hydroxytaxane O-acetyltransferase. CA Acetyl-CoA + 10-desacetyltaxuyunnanin C = CoA + taxuyunnanin C. CC -!- Acts on a number of related taxane diterpenoids with a free 10- CC beta-hydroxy group. CC -!- May be identical to EC 2.3.1.167. // ID 2.3.1.164 DE Isopenicillin N N-acyltransferase. AN Acyl-coenzyme A:isopenicillin N acyltransferase. AN Isopenicillin N:acyl-CoA: acyltransferase. AN Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase. CA Phenylacetyl-CoA + isopenicillin N + H(2)O = CoA + penicillin G + L-2- CA aminohexanedioate. CC -!- Proceeds by a two stage mechanism via 6-aminopenicillanic acid. CC -!- Different from EC 3.5.1.11. DR P15802, AAAA_PENCH; // ID 2.3.1.165 DE 6-methylsalicylic acid synthase. AN 6-MSAS. CA Acetyl-CoA + 3 malonyl-CoA + NADPH = 6-methylsalicylate + 4 CoA + CA 3 CO(2) + NADP(+). CC -!- A multienzyme complex with a 4'-phosphopantetheine prosthetic group CC on the acyl carrier protein. CC -!- It has a similar sequence to vertebrate type I fatty acid synthase. CC -!- Acetoacetyl-CoA can also act as a starter molecule. DR P22367, MSAS_PENPA; // ID 2.3.1.166 DE 2-alpha-hydroxytaxane 2-O-benzoyltransferase. AN Benzoyl-CoA:taxane 2-alpha-O-benzoyltransferase. AN 2-debenzoyl-7,13-diacetylbaccatin III-2-O-benzoyl transferase. CA Benzoyl-CoA + 10-deacetyl-2-debenzoylbaccatin III = CoA + 10- CA deacetylbaccatin III. CC -!- The enzyme was studied using the semisynthetic substrate 2- CC debenzoyl-7,13-diacetylbaccatin III. CC -!- It will not acylate the hydroxy group at 1-beta, 7-beta, 10-beta CC or 13-alpha of 10-deacetyl baccatin III, or at 2-alpha or 5-alpha CC of taxa-4(20),11-diene-2-alpha,5-alpha-diol. DR Q9FPW3, DBBT_TAXCU; // ID 2.3.1.167 DE 10-deacetylbaccatin III 10-O-acetyltransferase. CA Acetyl-CoA + 10-deacetylbaccatin III = CoA + baccatin III. CC -!- The enzyme will not acylate the hydroxy group at 1-beta, 7-beta, CC 13-alpha of 10-deacetyl baccatin III, or at 5-alpha of taxa-4(20), CC 11-dien-5-alpha-ol. CC -!- May be identical to EC 2.3.1.163. DR Q9M6E2, DBAT_TAXCU; // ID 2.3.2.1 DE D-glutamyltransferase. AN D-glutamyl transpeptidase. CA L(or D)-glutamine + D-glutamyl-peptide = NH(3) + 5-glutamyl-D-glutamyl- CA peptide. // ID 2.3.2.2 DE Gamma-glutamyltransferase. AN Gamma-glutamyltranspeptidase. AN Glutamyl transpeptidase. CA (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl-amino CA acid. DI Glutathionuria; MIM:231950. PR PROSITE; PDOC00404; DR P19440, GGT1_HUMAN; Q60928, GGT1_MOUSE; P20735, GGT1_PIG ; DR P07314, GGT1_RAT ; P36268, GGT2_HUMAN; P36269, GGT5_HUMAN; DR P54422, GGT_BACSU ; P18956, GGT_ECOLI ; P36267, GGT_PSESP ; DR P74181, GGT_SYNY3 ; P15557, PAC1_PSES3; Q05053, PAC1_PSESV; // ID 2.3.2.3 DE Lysyltransferase. CA L-lysyl-tRNA + phosphatidylglycerol = tRNA + 3-phosphatidyl-1'-(3'-O-L- CA lysyl)glycerol. // ID 2.3.2.4 DE Gamma-glutamylcyclotransferase. CA (5-L-glutamyl)-L-amino acid = 5-oxoproline + L-amino acid. CC -!- Acts on derivatives of L-glutamate, L-2-aminobutanoate, L-alanine CC and glycine. // ID 2.3.2.5 DE Glutaminyl-peptide cyclotransferase. AN Glutaminyl-tRNA cyclotransferase. AN Glutaminyl cyclase. CA L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH(3). CC -!- Involved in the formation of thyrotropin-releasing hormone and other CC biologically active peptides containing N-terminal pyroglutamyl CC residues. CC -!- The enzyme from papaya also acts on glutaminyl-tRNA. DR Q28120, QPCT_BOVIN; Q16769, QPCT_HUMAN; // ID 2.3.2.6 DE Leucyltransferase. CA L-leucyl-tRNA + protein = tRNA + L-leucyl-protein. CF Monovalent cation. CC -!- Also transfers phenylalanyl groups. CC -!- Peptides and proteins containing an N-terminal arginine, lysine or CC histidine residue can act as acceptors. // ID 2.3.2.7 DE Aspartyltransferase. CA L-asparagine + hydroxylamine = L-aspartylhydroxamate + NH(3). // ID 2.3.2.8 DE Arginyltransferase. AN Arginyl-tRNA--protein transferase. CA L-arginyl-tRNA + protein = tRNA + L-arginyl-protein. CC -!- Requires mercaptoethanol and a univalent cation. CC -!- Peptides and proteins containing an N-terminal glutamate, aspartate CC or cystine residue can act as acceptors. DR Q9ZT48, ATE1_ARATH; O96539, ATE1_DROME; O95260, ATE1_HUMAN; DR Q9Z2A5, ATE1_MOUSE; P16639, ATE1_YEAST; // ID 2.3.2.9 DE Agaritine gamma-glutamyltransferase. CA Agaritine + acceptor = 4-hydroxymethylphenylhydrazine + gamma-L- CA glutamyl-acceptor. CC -!- 4-hydroxyaniline, cyclohexylamine, 1-naphthylhydrazine and similar CC compounds can act as acceptors. CC -!- Also catalyzes the hydrolysis of agaritine. // ID 2.3.2.10 DE UDP-N-acetylmuramoylpentapeptide-lysine N(6)-alanyltransferase. CA L-alanyl-tRNA + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-D- CA alanyl-D-alanine = tRNA + UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl- CA N(6)-(L-alanyl)-L-lysyl-D-alanyl-D-alanine. CC -!- Also acts on L-seryl-tRNA. // ID 2.3.2.11 DE Alanylphosphatidylglycerol synthase. CA L-alanyl-tRNA + phosphatidylglycerol = tRNA + 3-O-L-alanyl-1-O- CA phosphatidylglycerol. // ID 2.3.2.12 DE Peptidyltransferase. CA Peptidyl-tRNA(1) + aminoacyl-tRNA(2) = tRNA(1) + peptidylaminoacyl- CA tRNA(2). CC -!- An enzyme in ribosomes. // ID 2.3.2.13 DE Protein-glutamine gamma-glutamyltransferase. AN Transglutaminase. AN Fibrinoligase. AN TGase. CA Protein glutamine + alkylamine = protein N(5)-alkylglutamine + NH(3). CF Calcium. CC -!- The gamma-carboxymide groups of peptide-bound glutamine residues act CC as acyl donors, and the 6-amino-groups of protein- and peptide-bound CC lysine residues act as acceptors, to give intra- and inter-molecular CC N(6)-(5-glutamyl)lysine crosslinks. PR PROSITE; PDOC00473; DR P52183, ANNU_SCHAM; P12260, F13A_BOVIN; P00488, F13A_HUMAN; DR P81453, TGL_STRSS ; P22735, TGM1_HUMAN; P22758, TGM1_RABIT; DR P23606, TGM1_RAT ; P51176, TGM2_BOVIN; P08587, TGM2_CAVCU; DR Q01841, TGM2_CHICK; P21980, TGM2_HUMAN; P21981, TGM2_MOUSE; DR P52181, TGM2_PAGMA; Q08188, TGM3_HUMAN; Q08189, TGM3_MOUSE; DR P49221, TGM4_HUMAN; Q99041, TGM4_RAT ; O43548, TGM5_HUMAN; DR Q96PF1, TGM7_HUMAN; Q05187, TGMH_TACTR; O95932, TGML_HUMAN; // ID 2.3.2.14 DE D-alanine gamma-glutamyltransferase. CA L-glutamine + D-alanine = gamma-L-glutamyl-D-alanine + NH(3). CC -!- D-phenylalanine and D-2-aminobutyrate can also act as acceptors, CC more slowly. CC -!- Also catalyzes some of the reactions of EC 2.3.2.2. // ID 2.3.2.15 DE Glutathione gamma-glutamylcysteinyltransferase. AN Phytochelatin synthase. CA Glutathione + {Glu(-Cys)}(N)-Gly = Gly + {Glu(-Cys)}(N+1)-Gly. // ID 2.3.3.1 DE Citrate (Si)-synthase. AN (R)-citric synthase. AN Condensing enzyme. AN Citrogenase. AN Oxaloacetate transacetase. AN Oxalacetic transacetase. AN Citrate condensing enzyme. AN Citrate oxaloacetate-lyase [(pro-3S)-CH(2)COO(-)->acetyl-CoA]. AN Citrate oxaloacetate-lyase, CoA-acetylating. AN Citrate synthase. AN Citrate synthetase. AN Citric synthase. AN Citric-condensing enzyme. CA Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA. CC -!- The stereospecificity of this enzyme is opposite to that of CC EC 2.3.3.4, which is found in some anaerobes. CC -!- Formerly EC 4.1.3.7. PR PROSITE; PDOC00422; DR P45858, CISW_BACSU; P43635, CISX_YEAST; O34002, CISY_ABDS2; DR P20901, CISY_ACEAC; P20902, CISY_ACIAN; P20115, CISY_ARATH; DR P51044, CISY_ASPNG; Q59136, CISY_ASTRI; P27660, CISY_BACCO; DR P39119, CISY_BACSU; P51031, CISY_BARBA; Q59198, CISY_BARDO; DR P51032, CISY_BAREL; P51033, CISY_BARHE; P51034, CISY_BARQU; DR Q59258, CISY_BARTA; P51035, CISY_BARVB; P51036, CISY_BARVI; DR P94325, CISY_BRAJA; P34575, CISY_CAEEL; P79024, CISY_CANTR; DR P23007, CISY_CHICK; P49298, CISY_CITMA; P42457, CISY_CORGL; DR P18789, CISY_COXBU; O80433, CISY_DAUCA; P00891, CISY_ECOLI; DR O00098, CISY_EMENI; P83372, CISY_FRAAN; Q9ZN37, CISY_HELPJ; DR P56062, CISY_HELPY; O75390, CISY_HUMAN; P26491, CISY_MYCSM; DR Q10530, CISY_MYCTU; P34085, CISY_NEUCR; P00889, CISY_PIG ; DR P14165, CISY_PSEAE; Q53554, CISY_PYRFU; O33915, CISY_RHIME; DR P51037, CISY_RHITR; Q59732, CISY_RICAF; Q59730, CISY_RICAK; DR P51039, CISY_RICAU; Q59734, CISY_RICBE; P51041, CISY_RICCA; DR P51042, CISY_RICCN; P51040, CISY_RICFE; Q59741, CISY_RICHE; DR Q59742, CISY_RICJA; Q59748, CISY_RICMA; Q59759, CISY_RICPA; DR P09948, CISY_RICPR; Q59768, CISY_RICRH; Q59778, CISY_RICSI; DR Q59776, CISY_RICSL; P51043, CISY_RICTY; O68883, CISY_SALTY; DR Q10306, CISY_SCHPO; Q43175, CISY_SOLTU; P20903, CISY_STRHY; DR P80148, CISY_SULSO; Q59977, CISY_SYNY3; P24118, CISY_TETTH; DR P21553, CISY_THEAC; P51045, CISY_THIFE; P00890, CISY_YEAST; DR P39120, CISZ_BACSU; Q10529, CISZ_MYCTU; P51038, CISZ_RHITR; DR Q59939, CISZ_STRMU; P08679, CISZ_YEAST; P49299, CYSZ_CUCMA; // ID 2.3.3.2 DE Decylcitrate synthase. AN 2-decylcitrate synthase. AN (2S,3S)-2-hydroxytridecane-1,2,3-tricarboxylate oxaloacetate-lyase (CoA- AN acylating). CA Lauroyl-CoA + H(2)O + oxaloacetate = (2S,3S)-2-hydroxytridecane-1,2,3- CA tricarboxylate + CoA. CC -!- Formerly EC 4.1.3.23. // ID 2.3.3.3 DE Citrate (Re)-synthase. AN (R)-citrate synthase. AN Re-citrate-synthase. AN Citrate oxaloacetate-lyase [(pro-3R)-CH(2)COO(-)->acetyl-CoA]. CA Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA. CC -!- This enzyme is inactivated by oxygen and is found in some anaerobes. CC -!- Its stereospecificity is opposite to that of EC 2.3.3.1. CC -!- Formerly EC 4.1.3.28. // ID 2.3.3.4 DE Decylhomocitrate synthase. AN 2-decylhomocitrate synthase. AN 3-hydroxytetradecane-1,3,4-tricarboxylate 2-oxoglutarate-lyase (CoA- AN acylating). CA Dodecanoyl-CoA + H(2)O + 2-oxoglutarate = (3S,4S)-3- CA hydroxytetradecane-1,3,4-tricarboxylate + CoA. CC -!- Decanoyl-CoA can act instead of dodecanoyl-CoA, but 2-oxoglutarate CC cannot be replaced by oxaloacetate or pyruvate. CC -!- Formerly EC 4.1.3.29. // ID 2.3.3.5 DE 2-methylcitrate synthase. AN 2-methylcitrate oxaloacetate-lyase. AN MCS. AN Methylcitrate synthase. AN Methylcitrate synthetase. CA Propanoyl-CoA + H(2)O + oxaloacetate = (2R,3S)-2-hydroxybutane-1,2,3- CA tricarboxylate + CoA. CC -!- The enzyme acts on acetyl-CoA, propanoyl-CoA, butanoyl-CoA and CC pentanoyl-CoA. CC -!- The relative rate of condensation of acetyl-CoA and oxaloacetate is CC 140% of that of propanoyl-CoA and oxaloacetate, but the enzyme has CC been separated from EC 2.3.3.1. CC -!- Oxaloacetate cannot be replaced by glyoxylate, pyruvate or 2- CC oxoglutarate. CC -!- Formerly EC 4.1.3.31. PR PROSITE; PDOC00422; DR Q8NSH7, PRC1_CORGL; Q8NSL1, PRC2_CORGL; P31660, PRPC_ECOLI; DR Q56063, PRPC_SALTY; // ID 2.3.3.6 DE 2-ethylmalate synthase. AN (R)-2-ethylmalate 2-oxobutanoyl-lyase (CoA-acetylating). AN 2-ethylmalate-3-hydroxybutanedioate synthase. AN Propylmalate synthase; propylmalic synthase. CA Acetyl-CoA + H(2)O + 2-oxobutanoate = (R)-2-ethylmalate + CoA. CC -!- Also acts on (R)-2-(n-propyl)-malate. CC -!- Formerly EC 4.1.3.33. // ID 2.3.3.7 DE 3-ethylmalate synthase. AN 2-ethyl-3-hydroxybutanedioate synthase. AN 3-ethylmalate glyoxylate-lyase (CoA-butanoylating). CA Butanoyl-CoA + H(2)O + glyoxylate = 3-ethylmalate + CoA. CC -!- Formerly EC 4.1.3.10. // ID 2.3.3.8 DE ATP citrate synthase. AN ATP-citrate (pro-S-)-lyase. AN ATP-citric lyase. AN ATP:citrate oxaloacetate-lyase [(pro-S)-CH(2)COO(-)->acetyl-CoA] (ATP- AN dephosphorylating). AN Acetyl-CoA:oxaloacetate acetyltransferase (isomerizing; ADP- AN phosphorylating). AN Adenosine triphosphate citrate lyase. AN Citrate cleavage enzyme. AN Citrate-ATP lyase. AN Citric cleavage enzyme. AN ATP citrate (pro-S)-lyase. CA ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA. CC -!- The enzyme can be dissociated into components, two of which are CC identical with EC 4.1.3.34 and EC 6.2.1.18. CC -!- Formerly EC 4.1.3.8. PR PROSITE; PDOC00335; DR Q8X097, ACL1_NEUCR; Q9P7W3, ACL1_SCHPO; O93988, ACL1_SORMA; DR P53585, ACLY_CAEEL; P53396, ACLY_HUMAN; Q91V92, ACLY_MOUSE; DR P16638, ACLY_RAT ; // ID 2.3.3.9 DE Malate synthase. AN Malate synthetase. AN Malate condensing enzyme. AN Malic synthetase. AN Malic-condensing enzyme. AN L-malate glyoxylate-lyase (CoA-acetylating). AN Glyoxylate transacetylase. AN Glyoxylate transacetase. AN Glyoxylic transacetase. CA Acetyl-CoA + H(2)O + glyoxylate = S-malate + CoA. CC -!- Formerly EC 4.1.3.2. PR PROSITE; PDOC00441; DR Q10663, GCP_CAEEL ; P13244, MASY_BRANA; Q02216, MASY_CANTR; DR P24571, MASY_CUCMA; P08216, MASY_CUCSA; P08997, MASY_ECOLI; DR P28344, MASY_EMENI; P17432, MASY_GOSHI; P49081, MASY_MAIZE; DR P95329, MASY_MYXXA; P28345, MASY_NEUCR; P21360, MASY_PICAN; DR Q43827, MASY_RAPSA; P17815, MASY_RICCO; P45458, MASY_SOYBN; DR P77947, MASY_STRAE; Q9ZH77, MASY_STRCL; P30952, MASY_YEAST; DR Q8UJ85, MASZ_AGRT5; Q9KB03, MASZ_BACHD; Q89UE3, MASZ_BRAJA; DR Q8YIR3, MASZ_BRUME; Q8FZ50, MASZ_BRUSU; Q8FNB3, MASZ_COREF; DR P42450, MASZ_CORGL; Q8FDN6, MASZ_ECOL6; P37330, MASZ_ECOLI; DR O32913, MASZ_MYCLE; Q50596, MASZ_MYCTU; Q9I636, MASZ_PSEAE; DR O05137, MASZ_PSEFL; Q88QX8, MASZ_PSEPK; Q98DK4, MASZ_RHILO; DR Q937W7, MASZ_RHILV; Q92TA4, MASZ_RHIME; Q9AE55, MASZ_RHOFA; DR P59663, MASZ_SHIFL; P21826, MASZ_YEAST; Q88AB2, MAZ1_PSESM; DR Q87Z72, MAZ2_PSESM; // ID 2.3.3.10 DE Hydroxymethylglutaryl-CoA synthase. AN HMG-CoA synthase. AN (S)-3-hydroxy-3-methylglutaryl-CoA acetoacetyl-CoA-lyase (CoA- AN acetylating). AN 3-hydroxy-3-methylglutaryl CoA synthetase. AN 3-hydroxy-3-methylglutaryl coenzyme A synthase. AN 3-hydroxy-3-methylglutaryl coenzyme A synthetase. AN 3-hydroxy-3-methylglutaryl-CoA synthase. AN 3-hydroxy-3-methylglutaryl-coenzyme A synthase. AN Beta-hydroxy-beta-methylglutaryl-CoA synthase. AN Acetoacetyl coenzyme A transacetase. AN Hydroxymethylglutaryl coenzyme A synthase. AN Hydroxymethylglutaryl coenzyme alpha-condensing enzyme. CA Acetyl-CoA + H(2)O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl- CA CoA + CoA. CC -!- Formerly EC 4.1.3.5. PR PROSITE; PDOC00942; DR P54961, HMC1_BLAGE; P54870, HMC2_BLAGE; P54868, HMCM_HUMAN; DR P54869, HMCM_MOUSE; O02734, HMCM_PIG ; P22791, HMCM_RAT ; DR P54873, HMCS_ARATH; P54871, HMCS_CAEEL; P23228, HMCS_CHICK; DR P13704, HMCS_CRIGR; P54872, HMCS_DICDI; Q01581, HMCS_HUMAN; DR P17425, HMCS_RAT ; P54874, HMCS_SCHPO; P54839, HMCS_YEAST; // ID 2.3.3.11 DE 2-hydroxyglutarate synthase. AN 2-hydroxyglutaratic synthetase. AN 2-hydroxyglutaric synthetase. AN Alpha-hydroxyglutarate synthase. AN Hydroxyglutarate synthase. AN 2-hydroxyglutarate glyoxylate-lyase (CoA-propanoylating). CA Propanoyl-CoA + H(2)O + glyoxylate = 2-hydroxyglutarate + CoA. CC -!- Formerly EC 4.1.3.9. // ID 2.3.3.12 DE 3-propylmalate synthase. AN 3-(n-propyl)-malate synthase. AN 3-propylmalate glyoxylate-lyase (CoA-pentanoylating). AN Beta-n-propylmalate synthase. AN N-propylmalate synthase. CA Pentanoyl-CoA + H(2)O + glyoxylate = 3-propylmalate + CoA. CC -!- Formerly EC 4.1.3.11. // ID 2.3.3.13 DE 2-isopropylmalate synthase. AN Alpha-isopropylmalate synthetase. AN Alpha-isopropylmalate synthase. AN Alpha-isopropylmalic synthetase. AN Alpha-IPM synthetase. AN 3-carboxy-3-hydroxy-4-methylpentanoate 3-methyl-2-oxobutanoate-lyase AN (CoA-acetylating). AN Isopropylmalate synthase. AN Isopropylmalate synthetase. CA Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = 2-hydroxy-2- CA isopropylsuccinate + CoA. CF Potassium. CC -!- Formerly EC 4.1.3.12. PR PROSITE; PDOC00643; DR O29305, LE11_ARCFU; Q8TKQ6, LE11_METAC; Q57926, LE11_METJA; DR Q8TW28, LE11_METKA; P58967, LE11_METMA; O27667, LE11_METTH; DR Q9UZ08, LE11_PYRAB; Q8XXP1, LE11_RALSO; Q97ZE0, LE11_SULSO; DR Q974X3, LE11_SULTO; Q8RDK3, LE11_THETN; O30020, LE12_ARCFU; DR Q8THA5, LE12_METAC; Q58595, LE12_METJA; Q8TYM1, LE12_METKA; DR P58968, LE12_METMA; O27525, LE12_METTH; Q9V1J1, LE12_PYRAB; DR Q8XSZ5, LE12_RALSO; Q97W36, LE12_SULSO; Q971S5, LE12_SULTO; DR Q8RCF9, LE12_THETN; Q8UD63, LEU1_AGRT5; P48575, LEU1_ANASP; DR O67862, LEU1_AQUAE; Q9K8E8, LEU1_BACHD; Q8RL85, LEU1_BACST; DR P94565, LEU1_BACSU; Q8YIJ3, LEU1_BRUME; Q9ZEY8, LEU1_BUCAI; DR O85063, LEU1_BUCAP; O85070, LEU1_BUCDN; Q9EVG4, LEU1_BUCML; DR P58898, LEU1_BUCPS; P48571, LEU1_BUCRP; O31287, LEU1_BUCTS; DR Q9EVH6, LEU1_BUCUE; Q9EVE3, LEU1_BUCUL; Q9EVH0, LEU1_BUCUM; DR Q9EVI8, LEU1_BUCUN; Q9PLV9, LEU1_CAMJE; Q9A823, LEU1_CAUCR; DR Q97MC5, LEU1_CLOAB; P42455, LEU1_CORGL; Q9RUA9, LEU1_DEIRA; DR Q8X9Z8, LEU1_ECO57; P09151, LEU1_ECOLI; P43861, LEU1_HAEIN; DR Q02141, LEU1_LACLA; Q92A28, LEU1_LISIN; Q8Y5R9, LEU1_LISMO; DR P94907, LEU1_MICAE; Q9CB76, LEU1_MYCLE; P96420, LEU1_MYCTU; DR Q9JUK6, LEU1_NEIMA; Q9JZG1, LEU1_NEIMB; Q9CJN5, LEU1_PASMU; DR Q9HXK5, LEU1_PSEAE; Q8ZW35, LEU1_PYRAE; Q8U2A2, LEU1_PYRFU; DR O59390, LEU1_PYRHO; Q98HN3, LEU1_RHILO; Q9X7L2, LEU1_RHIME; DR Q8Z9I0, LEU1_SALTI; P15875, LEU1_SALTY; O59736, LEU1_SCHPO; DR Q39891, LEU1_SOYBN; Q99SJ5, LEU1_STAAM; P58899, LEU1_STAAW; DR O31046, LEU1_STRCO; P48576, LEU1_SYNY3; Q9WZ23, LEU1_THEMA; DR Q56216, LEU1_THETH; Q9KP83, LEU1_VIBCH; P58900, LEU1_XANAC; DR P58901, LEU1_XANCP; Q9PCG3, LEU1_XYLFA; Q87CL8, LEU1_XYLFT; DR P06208, LEU1_YEAST; Q8ZIG8, LEU1_YERPE; O04973, LU1A_LYCPN; DR O04974, LU1B_LYCPN; // ID 2.3.3.14 DE Homocitrate synthase. AN 2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase (CoA- AN acetylating). AN Acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase. AN Homocitrate synthetase. CA Acetyl-CoA + H(2)O + 2-oxoglutarate = 2-hydroxybutane-1,2,4- CA tricarboxylate + CoA. CC -!- Formerly EC 4.1.3.21. PR PROSITE; PDOC00643; DR O87198, HOSC_THETH; P48570, HOSC_YEAST; O94225, HOSM_PENCH; DR Q12726, HOSM_YARLI; Q12122, HOSM_YEAST; P70728, NIFV_AZOBR; DR P23122, NIFV_AZOCH; P05342, NIFV_AZOVI; Q52070, NIFV_ENTAG; DR Q47884, NIFV_FRAAL; P54610, NIFV_FRASP; P05345, NIFV_KLEPN; DR Q07179, NIFV_RHOCA; Q01181, NIFV_RHOSH; Q44290, NIV1_ANASP; DR P58637, NIV2_ANASP; Q00853, NIVA_CLOPA; Q00852, NIVO_CLOPA; // ID 2.4.1.1 DE Phosphorylase. AN Muscle phosphorylase A and B. AN Amylophosphorylase. AN Polyphosphorylase. CA {(1,4)-alpha-D-glucosyl}(N) + phosphate = {(1,4)-alpha-D-glucosyl}(N-1) CA + alpha-D-glucose 1-phosphate. CC -!- The recommended name should be qualified in each instance by adding CC the name of the natural substance, e.g. maltodextrin phosphorylase, CC starch phosphorylase, glycogen phosphorylase. DI Glycogen storage disease V; MIM:232600. DI Glycogen storage disease VI; MIM:232700. PR PROSITE; PDOC00095; DR Q00766, PHS1_DICDI; P06737, PHS1_HUMAN; Q9ET01, PHS1_MOUSE; DR P09811, PHS1_RAT ; P04045, PHS1_SOLTU; P79334, PHS2_BOVIN; DR P34114, PHS2_DICDI; P11217, PHS2_HUMAN; Q9WUB3, PHS2_MOUSE; DR P00489, PHS2_RABIT; P09812, PHS2_RAT ; O18751, PHS2_SHEEP; DR P53535, PHS2_SOLTU; P11216, PHS3_HUMAN; P53534, PHS3_RAT ; DR O66932, PHSG_AQUAE; P39123, PHSG_BACSU; Q9PKE6, PHSG_CHLMU; DR Q9Z8N1, PHSG_CHLPN; O84250, PHSG_CHLTR; Q9XTL9, PHSG_DROME; DR P13031, PHSG_ECOLI; P45180, PHSG_HAEIN; Q10639, PHSG_MYCTU; DR P73511, PHSG_SYNY3; P06738, PHSG_YEAST; Q9SD76, PHSH_ARATH; DR P32811, PHSH_SOLTU; P53537, PHSH_VICFA; Q9LKJ3, PHSH_WHEAT; DR P27598, PHSL_IPOBA; P53536, PHSL_VICFA; P00490, PHSM_ECOLI; DR P07094, PHSM_KLEPN; P29849, PHSM_STRPN; // ID 2.4.1.2 DE Dextrin dextranase. AN Dextrin 6-glucosyltransferase. CA {(1,4)-alpha-D-glucosyl}(N) + {(1,6)-alpha-D-glucosyl}(M) = CA {(1,4)-alpha-D-glucosyl}(N-1) + {(1,6)-alpha-D-glucosyl}(M+1). // ID 2.4.1.3 DE Transferred entry: 2.4.1.25. // ID 2.4.1.4 DE Amylosucrase. AN Sucrose-glucan glucosyltransferase. CA Sucrose + {(1,4)-alpha-D-glucosyl}(N) = D-fructose + {(1,4)-alpha-D- CA glucosyl}(N+1). // ID 2.4.1.5 DE Dextransucrase. AN Sucrose 6-glucosyltransferase. CA Sucrose + {(1,6)-alpha-D-glucosyl}(N) = D-fructose + {(1,6)-alpha-D- CA glucosyl}(N+1). DR P11001, GTF1_STRDO; P27470, GTF2_STRDO; P08987, GTFB_STRMU; DR P13470, GTFC_STRMU; P49331, GTFD_STRMU; P29336, GTFS_STRDO; // ID 2.4.1.6 DE Deleted entry. // ID 2.4.1.7 DE Sucrose phosphorylase. AN Sucrose glucosyltransferase. AN Disaccharide glucosyltransferase. CA Sucrose + phosphate = D-fructose + alpha-D-glucose 1-phosphate. CC -!- In the forward reaction, arsenate may replace phosphate. CC -!- In the reverse reaction various ketoses and L-arabinose may replace CC D-fructose. DR P33910, SUCP_AGRVI; P76041, SUCP_ECOLI; Q59495, SUCP_LEUME; DR P10249, SUCP_STRMU; // ID 2.4.1.8 DE Maltose phosphorylase. CA Maltose + phosphate = D-glucose + beta-D-glucose 1-phosphate. // ID 2.4.1.9 DE Inulosucrase. AN Sucrose 1-fructosyl transferase. CA Sucrose + {(2,1)-beta-D-fructosyl}(N) = glucose + {(2,1)-beta-D- CA fructosyl}(N+1). CC -!- Converts sucrose into inulin and D-glucose. CC -!- Some other sugars can act as D-fructosyl acceptors. // ID 2.4.1.10 DE Levansucrase. AN Sucrose 6-fructosyl transferase. CA Sucrose + {(2,6)-beta-D-fructosyl}(N) = glucose + {(2,6)-beta-D- CA fructosyl}(N+1). CC -!- Some other sugars can act as D-fructosyl acceptors. DR Q43998, SACB_ACEDI; P21130, SACB_BACAM; P94468, SACB_BACST; DR P05655, SACB_BACSU; Q46654, SACB_ERWAM; O52408, SACB_PSESG; DR O68609, SACB_PSESH; O54435, SACB_RAHAQ; P11701, SACB_STRMU; DR Q55242, SACB_STRSL; Q60114, SACB_ZYMMO; // ID 2.4.1.11 DE Glycogen (starch) synthase. AN UDP-glucose-glycogen glucosyltransferase. CA UDP-glucose + {(1,4)-alpha-D-glucosyl}(N) = UDP + {(1,4)-alpha-D- CA glucosyl}(N+1). CC -!- The recommended name varies according to the source of the enzyme CC and the nature of its synthetic product. CC -!- Glycogen synthase from animal tissues is a complex of a catalytic CC subunit and the protein glycogenin. CC -!- The enzyme requires glucosylated glycogenin as a primer; this is CC the reaction product of EC 2.4.1.186. CC -!- A similar enzyme utilizes ADP-glucose (cf. EC 2.4.1.21). DI Glycogen storage disease 0; MIM:240600. DR P13807, GYS1_HUMAN; Q8MJ26, GYS1_MACMU; Q9Z1E4, GYS1_MOUSE; DR P13834, GYS1_RABIT; P23337, GYS1_YEAST; P54840, GYS2_HUMAN; DR P17625, GYS2_RAT ; P27472, GYS2_YEAST; P54859, GYS3_MOUSE; DR Q9U2D9, GYS_CAEEL ; Q9VFC8, GYS_DROME ; O93869, GYS_NEUCR ; DR Q9FNF2, UGS2_ARATH; Q40739, UGS2_ORYSA; P93568, UGS2_SOLTU; DR Q43654, UGS2_WHEAT; Q43093, UGS3_PEA ; Q43847, UGS3_SOLTU; DR Q43846, UGS4_SOLTU; O82627, UGST_ANTMA; Q9MAQ0, UGST_ARATH; DR P09842, UGST_HORVU; Q42857, UGST_IPOBA; P04713, UGST_MAIZE; DR Q43784, UGST_MANES; Q42968, UGST_ORYGL; P19395, UGST_ORYSA; DR Q43092, UGST_PEA ; Q00775, UGST_SOLTU; Q43134, UGST_SORBI; DR P27736, UGST_WHEAT; // ID 2.4.1.12 DE Cellulose synthase (UDP-forming). AN UDP-glucose-beta-D-glucan glucosyltransferase. AN UDP-glucose-cellulose glucosyltransferase. CA UDP-glucose + {(1,4)-beta-D-glucosyl}(N) = UDP + {(1,4)-beta-D- CA glucosyl}(N+1). CC -!- Involved in the synthesis of cellulose. CC -!- A similar enzyme utilizes GDP-glucose (cf. EC 2.4.1.29). DR P21877, ACS1_ACEXY; Q59167, ACS2_ACEXY; P19449, BCA1_ACEXY; DR O82859, BCA2_ACEXY; Q9WX61, BCA3_ACEXY; Q9RBJ2, BCA4_ACEXY; DR Q9WX75, BCA5_ACEXY; Q8X5L7, BCSA_ECO57; P37653, BCSA_ECOLI; DR P58931, BCSA_PSEFL; Q8Z291, BCSA_SALTI; Q93IN2, BCSA_SALTY; DR P58932, BCSA_XANAC; // ID 2.4.1.13 DE Sucrose synthase. AN UDP-glucose-fructose glucosyltransferase. AN Sucrose-UDP glucosyltransferase. CA UDP-glucose + D-fructose = UDP + sucrose. DR P49040, SUS1_ARATH; P49035, SUS1_DAUCA; P31922, SUS1_HORVU; DR P04712, SUS1_MAIZE; P30298, SUS1_ORYSA; P10691, SUS1_SOLTU; DR Q41608, SUS1_TULGE; Q00917, SUS2_ARATH; O49845, SUS2_DAUCA; DR P31923, SUS2_HORVU; P49036, SUS2_MAIZE; P31924, SUS2_ORYSA; DR O24301, SUS2_PEA ; P49039, SUS2_SOLTU; Q41607, SUS2_TULGE; DR Q43009, SUS3_ORYSA; P49034, SUSY_ALNGL; Q42652, SUSY_BETVU; DR P49037, SUSY_LYCES; O65026, SUSY_MEDSA; Q01390, SUSY_PHAAU; DR P31925, SUSY_SACOF; P13708, SUSY_SOYBN; P31926, SUSY_VICFA; // ID 2.4.1.14 DE Sucrose-phosphate synthase. AN UDP-glucose-fructose-phosphate glucosyltransferase. AN Sucrosephosphate-UDP glucosyltransferase. CA UDP-glucose + D-fructose 6-phosphate = UDP + sucrose 6-phosphate. DR O22060, SPS1_CITUN; O04932, SPS1_CRAPL; O04933, SPS2_CRAPL; DR P49031, SPS_BETVU ; P31927, SPS_MAIZE ; Q43802, SPS_ORYSA ; DR Q43845, SPS_SOLTU ; P31928, SPS_SPIOL ; Q43876, SPS_VICFA ; // ID 2.4.1.15 DE Alpha,alpha-trehalose-phosphate synthase (UDP-forming). AN UDP-glucose-glucosephosphate glucosyltransferase. AN Trehalosephosphate-UDP glucosyltransferase. AN Trehalose-6-phosphate synthase. AN Trehalose-6-phosphate synthetase. AN Trehalose-phosphate synthase. AN Trehalose-phosphate synthetase. AN Transglucosylase. AN Trehalosephosphate-UDP glucosyl transferase. CA UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose CA 6-phosphate. CC -!- See also EC 2.4.1.36. DR Q8XCE7, OTSA_ECO57; P31677, OTSA_ECOLI; P55612, OTSA_RHISN; DR Q9L893, OTSA_SALTY; Q92410, TPS1_CANAL; O59921, TPS1_EMENI; DR Q07158, TPS1_KLULA; O94213, TPS1_PICAN; P40387, TPS1_SCHPO; DR O74932, TPS1_YARLI; Q00764, TPS1_YEAST; Q96WK6, TPS1_ZYGRO; DR P38426, TPS3_YEAST; Q00075, TPSA_ASPNG; Q00217, TPSB_ASPNG; DR O14081, TPSX_SCHPO; Q9UUI7, TPSY_SCHPO; P38427, TSL1_YEAST; // ID 2.4.1.16 DE Chitin synthase. AN Chitin-UDP acetyl-glucosaminyl transferase. CA UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N) = CA UDP + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N+1). CC -!- Converts UDP-N-acetyl-D-glucosamine into chitin and UDP. DR P30576, CHS1_AJECA; P30579, CHS1_AJEDE; P30581, CHS1_ASPNG; DR P49603, CHS1_BOTCI; P23316, CHS1_CANAL; O13356, CHS1_CRYNE; DR P30583, CHS1_EMENI; P30600, CHS1_EXODE; P30585, CHS1_EXOJE; DR P30588, CHS1_NEUCR; P30590, CHS1_PHAEX; P87073, CHS1_PHYBL; DR P30592, CHS1_RHIAT; P30594, CHS1_RHIOL; Q12632, CHS1_RHIRA; DR P30596, CHS1_SCHCO; P30597, CHS1_SCHPO; P55003, CHS1_TUBUN; DR P30598, CHS1_USTMA; P30603, CHS1_XYLBA; P08004, CHS1_YEAST; DR P30577, CHS2_AJECA; P30580, CHS2_AJEDE; P30582, CHS2_ASPNG; DR P30572, CHS2_CANAL; P30601, CHS2_EXODE; P30586, CHS2_EXOJE; DR P30589, CHS2_NEUCR; Q92444, CHS2_PARBR; P30591, CHS2_PHAEX; DR P30593, CHS2_RHIAT; P30595, CHS2_RHIOL; O74756, CHS2_SCHPO; DR P30599, CHS2_USTMA; P30604, CHS2_XYLBA; P14180, CHS2_YEAST; DR P30578, CHS3_AJECA; P30573, CHS3_CANAL; P30602, CHS3_EXODE; DR P30587, CHS3_EXOJE; P29070, CHS3_NEUCR; P29465, CHS3_YEAST; DR O13353, CHS4_MAGGR; Q01285, CHS4_NEUCR; O13394, CHS5_USTMA; DR O13395, CHS6_USTMA; Q12564, CHSA_AMPQU; P30584, CHSA_EMENI; DR Q00757, CHSB_EMENI; Q92197, CHSC_ASPFU; P78746, CHSD_ASPFU; DR P78611, CHSD_EMENI; P54267, CHSG_ASPFU; Q99126, CHSX_USTMA; DR Q99127, CHSY_USTMA; P48017, CHS_SAPMO ; // ID 2.4.1.17 DE UDP-glucuronosyltransferase. AN UDPGT. CA UDP-glucuronate + acceptor = UDP + acceptor beta-D-glucuronoside. CC -!- Family of enzymes accepting a wide range of substrates, including CC phenols, alcohols, amines and fatty acids. CC -!- Some of the activities catalyzed were previously listed separately CC as EC 2.4.1.42, EC 2.4.1.59, EC 2.4.1.61, EC 2.4.1.76, EC 2.4.1.77, CC EC 2.4.1.84, EC 2.4.1.107 and EC 2.4.1.108. CC -!- A temporary nomenclature for the various forms whose delineation CC is in a state of flux. DI Hyperbilirubinemia I (Gilbert syndrome); MIM:143500. PR PROSITE; PDOC00359; DR P22309, UD11_HUMAN; Q63886, UD11_MOUSE; Q64550, UD11_RAT ; DR P36509, UD12_HUMAN; P70691, UD12_MOUSE; P20720, UD12_RAT ; DR P35503, UD13_HUMAN; Q64637, UD13_RAT ; P22310, UD14_HUMAN; DR Q28612, UD14_RABIT; P35504, UD15_HUMAN; Q64638, UD15_RAT ; DR P19224, UD16_HUMAN; Q64435, UD16_MOUSE; Q28611, UD16_RABIT; DR P08430, UD16_RAT ; Q9HAW7, UD17_HUMAN; Q62452, UD17_MOUSE; DR Q64633, UD17_RAT ; Q9HAW9, UD18_HUMAN; Q64634, UD18_RAT ; DR O60656, UD19_HUMAN; Q9HAW8, UD1A_HUMAN; P19489, UD21_RAT ; DR P36510, UDA1_RAT ; P09875, UDB1_RAT ; P08541, UDB2_RAT ; DR P08542, UDB3_RAT ; P06133, UDB4_HUMAN; P17717, UDB5_MOUSE; DR P19488, UDB6_RAT ; P16662, UDB7_HUMAN; Q62789, UDB8_RAT ; DR O02663, UDB9_MACFA; P36537, UDBA_HUMAN; O75310, UDBB_HUMAN; DR P36511, UDBC_RAT ; P36512, UDBD_RABIT; P36513, UDBE_RABIT; DR P54855, UDBF_HUMAN; O19103, UDBG_RABIT; O75795, UDBH_HUMAN; DR Q9XT55, UDBJ_MACFA; O77649, UDBK_MACFA; Q9BY64, UDBS_HUMAN; DR P36514, UDC1_RABIT; Q91280, UGT3_PLEPL; Q20086, UGT5_CAEEL; DR Q22180, UGTB_CAEEL; Q22181, UGTC_CAEEL; Q10941, UGTE_CAEEL; DR Q18081, UGTF_CAEEL; Q22295, UGTG_CAEEL; // ID 2.4.1.18 DE 1,4-alpha-glucan branching enzyme. AN Glycogen branching enzyme. AN Amylo-(1,4 to 1,6)transglucosidase. AN Branching enzyme. AN Amylo-(1,4-1,6)-transglycosylase. CA Formation of 1,6-glucosidic linkages of glycogen. CC -!- Converts amylose into amylopectin. CC -!- The recommended name requires a qualification depending on the CC product, glycogen or amylopectin, e.g. glycogen branching enzyme, CC amylopectin branching enzyme. The latter has frequently been CC termed Q-enzyme. DI Glycogen storage disease IV; MIM:232500. DR P52979, GLGB_AGRTU; P30537, GLGB_BACCL; P30538, GLGB_BACST; DR P39118, GLGB_BACSU; P30539, GLGB_BUTFI; P07762, GLGB_ECOLI; DR P45177, GLGB_HAEIN; Q04446, GLGB_HUMAN; Q08047, GLGB_MAIZE; DR Q10625, GLGB_MYCTU; Q01401, GLGB_ORYSA; P30924, GLGB_SOLTU; DR P52980, GLGB_STRAU; P16954, GLGB_SYNP7; P52981, GLGB_SYNY3; DR P32775, GLGB_YEAST; // ID 2.4.1.19 DE Cyclomaltodextrin glucanotransferase. AN Cyclodextrin-glycosyltransferase. AN Bacillus macerans amylase. AN Cyclodextrin glucanotransferase. CA Degrades starch to cyclodextrins by formation of a 1,4-alpha-D- CA glucosidic bond. CC -!- Cyclomaltodextrins (Schardinger dextrins) of various sizes (6, 7, 8, CC etc. glucose units) are formed reversibly from starch and similar CC substrates. CC -!- Also disproportionate linear maltodextrins without cyclizing CC (cf. EC 2.4.1.25). DR P04830, CDG1_PAEMA; P31835, CDG2_PAEMA; P30920, CDGT_BACCI; DR P14014, CDGT_BACLI; P27036, CDGT_BACOH; P05618, CDGT_BACS0; DR P31746, CDGT_BACS2; P09121, CDGT_BACS3; P30921, CDGT_BACSP; DR P31747, CDGT_BACSS; P31797, CDGT_BACST; P08704, CDGT_KLEPN; DR P26827, CDGT_THETU; P43379, CDGU_BACCI; // ID 2.4.1.20 DE Cellobiose phosphorylase. CA Cellobiose + phosphate = alpha-D-glucose 1-phosphate + D-glucose. // ID 2.4.1.21 DE Starch (bacterial glycogen) synthase. AN Glycogen synthase. AN ADP-glucose-starch glucosyltransferase. CA ADP-glucose + {(1,4)-alpha-D-glucosyl}(N) = ADP + {(1,4)-alpha-D- CA glucosyl}(N+1). CC -!- The recommended name various according to the source of the enzyme CC and the nature of its synthetic product, e.g. starch synthase, CC bacterial glycogen synthase. CC -!- A similar enzyme utilizes UDP-glucose (cf. EC 2.4.1.11). DR P39670, GLG1_AGRT5; P58393, GLG1_RHIME; Q8UK38, GLG2_AGRT5; DR Q8Z0Q9, GLG2_ANASP; P58394, GLG2_RHIME; P72623, GLG2_SYNY3; DR Q8YVU5, GLGA_ANASP; O66935, GLGA_AQUAE; Q9KDX6, GLGA_BACHD; DR O08328, GLGA_BACST; P39125, GLGA_BACSU; Q9PLC3, GLGA_CHLMU; DR Q9Z6V8, GLGA_CHLPN; Q8KAY6, GLGA_CHLTE; O84804, GLGA_CHLTR; DR Q97GX6, GLGA_CLOAB; Q8XPA1, GLGA_CLOPE; Q9RWS1, GLGA_DEIRA; DR P08323, GLGA_ECOLI; Q8RF65, GLGA_FUSNN; P45179, GLGA_HAEIN; DR Q9CHM9, GLGA_LACLA; Q59001, GLGA_METJA; Q9CN91, GLGA_PASMU; DR Q9I1V0, GLGA_PSEAE; Q8XT73, GLGA_RALSO; Q985P2, GLGA_RHILO; DR Q9EUT5, GLGA_RHITR; Q9RNH6, GLGA_RHOSH; Q8Z232, GLGA_SALTI; DR P05416, GLGA_SALTY; Q97QS5, GLGA_STRPN; Q935Y7, GLGA_SYNP7; DR P74521, GLGA_SYNY3; P58395, GLGA_THECA; Q9WZZ7, GLGA_THEMA; DR Q9KRB6, GLGA_VIBCH; Q8PQA3, GLGA_XANAC; Q8PDD2, GLGA_XANCP; DR Q8ZA78, GLGA_YERPE; // ID 2.4.1.22 DE Lactose synthase. AN UDP-galactose-glucose galactosyltransferase. AN N-acetyllactosamine synthase. CA UDP-galactose + D-glucose = UDP + lactose. CC -!- The enzyme is a complex of 2 proteins A and B. In the absence of the CC B protein (alpha-lactalbumin) the enzyme catalyzes the transfer of CC galactose from UDP-galactose to N-acetylglucosamine (cf. CC EC 2.4.1.90). DR P08037, B4G1_BOVIN; P15291, B4G1_HUMAN; P15535, B4G1_MOUSE; DR P80225, B4G1_RAT ; O60909, B4G2_HUMAN; // ID 2.4.1.23 DE Sphingosine beta-galactosyltransferase. AN Psychosine-UDP galactosyltransferase. CA UDP-galactose + sphingosine = UDP + psychosine. // ID 2.4.1.24 DE 1,4-alpha-glucan 6-alpha-glucosyltransferase. AN Oligoglucan-branching glycosyltransferase. CA Transfers an alpha-D-glucosyl residue in a (1,4)-alpha-D-glucan to the CA primary hydroxyl group of glucose, free or combined in a 1,4-alpha-D- CA glucan. // ID 2.4.1.25 DE 4-alpha-glucanotransferase. AN Disproportionating enzyme. AN D-enzyme. AN Dextrin glycosyltransferase. AN Oligo-1,4-1,4-glucantransferase. CA Transfers a segment of a (1,4)-alpha-D-glucan to a new 4-position in an CA acceptor, which may be glucose or (1,4)-alpha-D-glucan. CC -!- An enzymic activity of this nature forms part of the mammalian and CC Yeast glycogen branching system (see EC 3.2.1.33). CC -!- Formerly EC 2.4.1.3. DR Q06801, DPEP_SOLTU; P35573, GDE_HUMAN ; P35574, GDE_RABIT ; DR O66937, MALQ_AQUAE; O34022, MALQ_CHLCV; Q9PKU9, MALQ_CHLMU; DR Q9Z8L2, MALQ_CHLPN; O84089, MALQ_CHLTR; Q59266, MALQ_CLOBU; DR P15977, MALQ_ECOLI; P45176, MALQ_HAEIN; O53932, MALQ_MYCTU; DR O32450, MALQ_PYRKO; P29851, MALQ_STRPN; P72785, MALQ_SYNY3; DR O32462, MALQ_THELI; O87172, MALQ_THETH; P80099, MGTA_THEMA; DR O86956, MGTA_THENE; // ID 2.4.1.26 DE DNA alpha-glucosyltransferase. CA Transfers an alpha-D-glucosyl residue from UDP-glucose to an CA hydroxymethyl-cytosine residue in DNA. DR P04519, GSTA_BPT4 ; // ID 2.4.1.27 DE DNA beta-glucosyltransferase. CA Transfers a beta-D-glucosyl residue from UDP-glucose to an CA hydroxymethylcytosine residue in DNA. DR P04547, GSTB_BPT4 ; // ID 2.4.1.28 DE Glucosyl-DNA beta-glucosyltransferase. CA Transfers a beta-D-glucosyl residue from UDP-glucose to a CA glucosylhydroxymethylcytosine residue in DNA. // ID 2.4.1.29 DE Cellulose synthase (GDP-forming). AN GDP-glucose-beta-D-glucan glucosyltransferase. AN GDP-glucose-cellulose glucosyltransferase. CA GDP-glucose + {(1,4)-beta-D-glucosyl}(N) = GDP + {(1,4)-beta-D- CA glucosyl}(N+1). CC -!- Involved in the synthesis of cellulose. CC -!- A similar enzyme utilizes UDP-glucose (cf. EC 2.4.1.12). // ID 2.4.1.30 DE 1,3-beta-oligoglucan phosphorylase. AN Beta-1,3-oligoglucan:orthophosphate glucosyltransferase II. CA {(1,3)-beta-D-glucosyl}(N) + phosphate = {(1,3)-beta-D-glucosyl}(N-1) + CA alpha-D-glucose 1-phosphate. CC -!- Does not act on laminarin. CC -!- Differs in specificity from EC 2.4.1.31 and EC 2.4.1.97. // ID 2.4.1.31 DE Laminaribiose phosphorylase. CA 3-beta-D-glucosylglucose + phosphate = D-glucose + alpha-D-glucose CA 1-phosphate. CC -!- Also acts on 1,3-beta-D-oligoglucans. CC -!- Differs in specificity from EC 2.4.1.30 and EC 2.4.1.97. // ID 2.4.1.32 DE Glucomannan 4-beta-mannosyltransferase. AN Glucomannan-synthase. CA GDP-mannose + {glucomannan}(N) = GDP + {glucomannan}(N+1). // ID 2.4.1.33 DE Alginate synthase. AN Mannuronosyl transferase. CA GDP-mannuronate + {alginate}(N) = GDP + {alginate}(N+1). // ID 2.4.1.34 DE 1,3-beta-glucan synthase. AN 1,3-beta-D-glucan-UDP glucosyltransferase. AN UDP-glucose-1,3-beta-D-glucan glucosyltransferase. AN Callose synthetase. AN Callose synthase. CA UDP-glucose + {(1,3)-beta-D-glucosyl}(N) = UDP + {(1,3)-beta-D- CA glucosyl}(N+1). DR Q10287, BGS1_SCHPO; O13967, BGS2_SCHPO; Q9P377, BGS3_SCHPO; DR O74475, BGS4_SCHPO; P38631, GLS1_YEAST; P40989, GLS2_YEAST; DR Q04952, GLS3_YEAST; P38678, GS1_NEUCR ; // ID 2.4.1.35 DE Phenol beta-glucosyltransferase. AN UDP-glucosyltransferase. CA UDP-glucose + a phenol = UDP + aryl beta-D-glucoside. CC -!- Acts on a wide range of phenols. // ID 2.4.1.36 DE Alpha,alpha-trehalose-phosphate synthase (GDP-forming). AN GDP-glucose-glucosephosphate glucosyltransferase. AN Trehalose phosphate synthase (GDP-forming). CA GDP-glucose + glucose 6-phosphate = GDP + alpha,alpha-trehalose CA 6-phosphate. CC -!- See also EC 2.4.1.15. // ID 2.4.1.37 DE Fucosylgalactoside 3-alpha-galactosyltransferase. AN Fucosylglycoprotein 3-alpha-galactosyltransferase. AN Histo-blood group B transferase. AN B transferase. AN Blood-group substance B-dependent galactosyltransferase. AN Histo-blood substance beta-dependent galactosyltransferase. AN UDP-galactose:O-alpha-L-fucosyl(1->2)D-galactose alpha-D- AN galactosyltransferase. AN UDPgalactose:glycoprotein-alpha-L-fucosyl-(1,2)-D-galactose 3-alpha-D- AN galactosyltransferase. AN [Blood group substance] alpha-galactosyltransferase. AN Blood-group substance beta-dependent galactosyltransferase. AN Glycoprotein-fucosylgalactoside alpha-galactosyltransferase. CA UDP-galactose + alpha-L-fucosyl-(1->2)-D-galactosyl-R = UDP + alpha-D- CA galactosyl-(1->3)-[alpha-L-fucosyl(1->2)]-D-galactosyl-R. CC -!- Acts on blood group substance, and can use a number of 2-fucosyl- CC galactosides as acceptors. DR P16442, BGAT_HUMAN; P38649, BGAT_MOUSE; // ID 2.4.1.38 DE Beta-N-acetylglucosaminyl-glycopeptide beta-1,4-galactosyltransferase. AN Glycoprotein 4-beta-galactosyltransferase. AN Thyroid galactosyltransferase. AN UDP-galactose-glycoprotein galactosyltransferase. CA UDP-galactose + N-acetyl-beta-D-glucosaminylglycopeptide = UDP + CA beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminylglycopeptide. CC -!- Terminal N-acetyl-beta-D-glucosaminyl residues in polysaccharides, CC glycoproteins and glycopeptides can act as acceptor. High activity CC is shown towards such residues in branched-chain polysaccharides CC when these are linked by beta-1,6 links to galactose residues; lower CC activity towards residues linked to galactose by beta-1,3 links. CC -!- A component of EC 2.4.1.22. DR P08037, B4G1_BOVIN; P15291, B4G1_HUMAN; P15535, B4G1_MOUSE; DR P80225, B4G1_RAT ; O60909, B4G2_HUMAN; O60512, B4G3_HUMAN; // ID 2.4.1.39 DE Steroid N-acetylglucosaminyltransferase. AN Sucrose-glucan glucosyltransferase. CA UDP-N-acetyl-D-glucosamine + estradiol-17-alpha 3-D-glucuronoside = CA UDP + 17-alpha-(N-acetyl-D-glucosaminyl)estradiol 3-D-glucuronoside. // ID 2.4.1.40 DE Glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase. AN Fucosylglycoprotein alpha-N-acetylgalactosaminyltransferase. AN Fucosylgalactose alpha-N-acetylgalactosaminyltransferase. AN Histo-blood group A transferase. AN A transferase. AN Histo-blood group A acetylgalactosaminyltransferase. CA UDP-N-acetyl-D-galactosamine + glycoprotein-alpha-L-fucosyl-(1,2)-D- CA galactose = UDP + glycoprotein-N-acetyl-alpha-D-galactosaminyl-(1,3)- CA [alpha-L-fucosyl-(1,2)]-D-galactose. CC -!- Acts on blood group substance H. CC -!- Can use a number of 2-fucosyl-galactosides as acceptors. DR P16442, BGAT_HUMAN; P38649, BGAT_MOUSE; // ID 2.4.1.41 DE Polypeptide N-acetylgalactosaminyltransferase. AN Protein-UDP acetylgalactosaminyltransferase. CA UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D- CA galactosaminyl-polypeptide. CF Manganese; Calcium. CC -!- The glycosyl residue is transferred to threonine or serine hydroxyl CC groups on the polypeptide core of submaxillary mucin, kappa-casein, CC apofetuin and some other acceptors of high molecular mass. DR P34678, PAG3_CAEEL; Q07537, PAGT_BOVIN; Q10472, PAGT_HUMAN; DR O08912, PAGT_MOUSE; Q29121, PAGT_PIG ; Q10473, PAGT_RAT ; // ID 2.4.1.42 DE Transferred entry: 2.4.1.17. // ID 2.4.1.43 DE Polygalacturonate 4-alpha-galacturonosyltransferase. CA UDP-galacturonate + (1,4-alpha-D-galacturonosyl)(N) = UDP + CA (1,4-alpha-D-galacturonosyl)(N+1). // ID 2.4.1.44 DE Lipopolysaccharide 3-alpha-galactosyltransferase. AN Lipopolysaccharide galactosyltransferase. AN Lipopolysaccharide 1,3-galactosyltransferase. AN UDP-galactose:lipopolysaccharide alpha,3-galactosyltransferase. AN UDP-galactose:polysaccharide galactosyltransferase. AN Uridine diphosphate galactose:lipopolysaccharide alpha-3- AN galactosyltransferase. AN Uridine diphosphogalactose-lipopolysaccharide alpha,3- AN galactosyltransferase. CA UDP-galactose + lipopolysaccharide = UDP + 3-alpha-D-galactosyl- CA [lipopolysaccharide glucose]. CC -!- Transfers D-galactosyl residues to D-glucose in the partially CC completed core of lipopolysaccharide (cf. EC 2.4.1.56, EC 2.4.1.58, CC and EC 2.4.1.73). DR P27128, RFAI_ECOLI; P19816, RFAI_SALTY; // ID 2.4.1.45 DE 2-hydroxyacylsphingosine 1-beta-galactosyltransferase. AN UDP-galactose-ceramide galactosyltransferase. AN Cerebroside synthase. CA UDP-galactose + 2-(2-hydroxyacyl)sphingosine = UDP + 1-(beta-D- CA galactosyl)-2-(2-hydroxyacyl)sphingosine. CC -!- Highly specific. PR PROSITE; PDOC00359; DR Q16880, CGT_HUMAN ; Q64676, CGT_MOUSE ; Q09426, CGT_RAT ; // ID 2.4.1.46 DE 1,2-diacylglycerol 3-beta-galactosyltransferase. CA UDP-galactose + 1,2-diacylglycerol = UDP + 3-beta-D-galactosyl-1,2- CA diacylglycerol. // ID 2.4.1.47 DE N-acylsphingosine galactosyltransferase. CA UDP-galactose + N-acylsphingosine = UDP + D-galactosylceramide. // ID 2.4.1.48 DE Heteroglycan alpha-mannosyltransferase. CA GDP-mannose + heteroglycan = GDP + 1,2(or 1,3)-alpha-D- CA mannosylheteroglycan. CC -!- The acceptor is a heteroglycan primer containing mannose, galactose CC and xylose. 1,2- and 1,3-mannosyl bonds are formed. // ID 2.4.1.49 DE Cellodextrin phosphorylase. CA {(1,4)-beta-D-glucosyl}(N) + phosphate = {(1,4)-beta-D-glucosyl}(N-1) + CA alpha-D-glucose 1-phosphate. DR P50125, CYSD_EMENI; O13326, CYSD_SCHPO; // ID 2.4.1.50 DE Procollagen galactosyltransferase. AN Hydroxylysine galactosyltransferase. CA UDP-galactose + procollagen 5-hydroxy-L-lysine = UDP + procollagen CA 5-(galactosyloxy)-L-lysine. CC -!- Probably involved in the synthesis of carbohydrate units in CC complement (cf. EC 2.4.1.66). // ID 2.4.1.51 DE Transferred entry: 2.4.1.101, 2.4.1.143, 2.4.1.144 and 2.4.1.145. // ID 2.4.1.52 DE Poly(glycerol-phosphate) alpha-glucosyltransferase. CA UDP-glucose + poly(glycerol phosphate) = UDP + alpha-D- CA glucosylpoly(glycerol phosphate). DR P13484, TAGE_BACSU; // ID 2.4.1.53 DE Poly(ribitol-phosphate) beta-glucosyltransferase. CA UDP-glucose + poly(ribitol phosphate) = UDP + beta-D- CA glucosylpoly(ribitol phosphate). // ID 2.4.1.54 DE Undecaprenyl-phosphate mannosyltransferase. CA GDP-mannose + undecaprenyl phosphate = GDP + D-mannosyl-1- CA phosphoundecaprenol. CC -!- Requires phosphatidylglycerol. // ID 2.4.1.55 DE Transferred entry: 2.7.8.14. // ID 2.4.1.56 DE Lipopolysaccharide N-acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + lipopolysaccharide = UDP + N-acetyl-D- CA glucosaminyl-lipopolysaccharide. CC -!- Transfers N-acetylglucosaminyl residues to a D-galactose residue in CC the partially completed lipopolysaccharide core (cf. EC 2.4.1.44, CC EC 2.4.1.58, and EC 2.4.1.73). DR P27242, RFAK_ECOLI; P26470, RFAK_SALTY; // ID 2.4.1.57 DE Phosphatidyl-myo-inositol alpha-mannosyltransferase. CA Transfers one or more alpha-D-mannose units from GDP-mannose to CA positions 2,6- and others in 1-phosphatidyl-myo-inositol. // ID 2.4.1.58 DE Lipopolysaccharide glucosyltransferase I. CA UDP-glucose + lipopolysaccharide = UDP + D-glucosyl-lipopolysaccharide. CC -!- Transfers glucosyl residues to the backbone portion of CC lipopolysaccharide (cf. EC 2.4.1.44, EC 2.4.1.56, and EC 2.4.1.73). DR P27129, RFAJ_ECOLI; P19817, RFAJ_SALTY; // ID 2.4.1.59 DE Transferred entry: 2.4.1.17. // ID 2.4.1.60 DE Abequosyltransferase. CA CDP-abequose + D-mannosyl-rhamnosyl-D-galactose-1-diphospholipid = CDP + CA abequosyl-D-mannosyl-rhamnosyl-D-galactose-1-diphospholipid. // ID 2.4.1.61 DE Transferred entry: 2.4.1.17. // ID 2.4.1.62 DE Ganglioside galactosyltransferase. CA UDP-galactose + N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)- CA D-galactosyl-D-glucosyl-N-acylsphingosine = UDP + D-galactosyl- CA N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)-D-galactosyl-D-glucosyl- CA N-acylsphingosine. CC -!- The substrate is also known as G(M2). DR O96024, B3G4_HUMAN; Q9Z0F0, B3G4_MOUSE; O88178, B3G4_RAT ; // ID 2.4.1.63 DE Linamarin synthase. CA UDP-glucose + 2-hydroxy-2-methylpropanenitrile = UDP + linamarin. CC -!- Glucosylates the cyanohydrins of butanone and pentan-3-one as well CC as that of acetone. // ID 2.4.1.64 DE Alpha,alpha-trehalose phosphorylase. CA Alpha,alpha-trehalose + phosphate = D-glucose + beta-D-glucose CA 1-phosphate. // ID 2.4.1.65 DE 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase. AN Blood group Lewis alpha-4-fucosyltransferase. AN Guanosine diphosphofucose-beta-acetylglucosaminylsaccharide 4-alpha-L- AN fucosyltransferase. AN Alpha(1,3/1,4) fucosyltransferase III. AN Alpha-(1->4)-L-fucosyltransferase. AN Alpha-4-L-fucosyltransferase. AN Beta-acetylglucosaminylsaccharide fucosyltransferase. AN Blood-group substance Le(a)-dependent fucosyltransferase. AN Guanosine diphosphofucose-glycoprotein 4-alpha-fucosyltransferase. AN Guanosine diphosphofucose-glycoprotein 4-alpha-L-fucosyltransferase. AN Lewis blood group alpha-(1->3/4)-fucosyltransferase. AN Lewis alpha-(1->3/4)-fucosyltransferase. AN FucT-II. AN (Le(a))-dependent (alpha-3/4)-fucosyltransferase. AN Lewis alpha-(1->3/4)-fucosyltransferase. AN Lewis(Le) blood group gene-dependent alpha-(1->3/4)-L- AN fucosyltransferase. AN Galactoside 3(4)-L-fucosyltransferase. AN Blood group Lewis alpha-4-fucosyltransferase. AN Lewis FT. CA GDP-beta-L-fucose + beta-D-galactosyl-(1->3)-N-acetyl-D-glucosaminyl-R = CA GDP + beta-D-galactosyl-(1->3)-[alpha-L-fucosyl-(1->4)]-N-acetyl-beta-D- CA glucosaminyl-R. CC -!- This enzyme is the product of the Lewis blood group gene. CC -!- Normally acts on a glycoconjugate where R (see CA line) is a CC glycoprotein or glycolipid. CC -!- Although it is a 4-fucosyltransferase, it has a persistent 3- CC fucosyltransferase activity towards the glucose residue in free CC lactose. CC -!- This enzyme fucosylates on O-4 of an N-acetylglucosamine that CC carries a galactosyl group on O-3, unlike EC 2.4.1.154 which CC fucosylates on O-3 of an N-acetylglucosamine that carries a CC galactosyl group on O-4. CC -!- Enzymes catalyzing the 4-alpha-fucosylation of the GlcNAc in beta-D- CC Gal-(1->3)-beta-GlcNAc sequences (with some activity also as 3- CC alpha-fucosyltransferases) are present in plants, where the function CC in vivo is the modification of N-glycans. CC -!- In addition, the fucTa gene of Helicobacter strain UA948 encodes a CC fucosyltransferase with both 3-alpha- and 4-alpha-fucosyltransferase CC activities. DR Q11126, FUT3_BOVIN; P21217, FUT3_HUMAN; O19058, FUT3_PANTR; DR Q11128, FUT5_HUMAN; P56433, FUT5_PANTR; P51993, FUT6_HUMAN; DR P56434, FUT6_PANTR; // ID 2.4.1.66 DE Procollagen glucosyltransferase. AN Galactosylhydroxylysine-glucosyltransferase. CA UDP-glucose + 5-hydroxyl-L-lysine-procollagen = UDP + O-D-glucosyl- CA 5-hydroxyL-L-lysine-procollagen. CC -!- Probably involved in the synthesis of carbohydrate units in CC complement (cf. EC 2.4.1.50). DI Epidermolysis bullosa simplex; MIM:131880. // ID 2.4.1.67 DE Galactinol-raffinose galactosyltransferase. CA 1-alpha-D-galactosyl-myo-inositol + raffinose = myo-inositol + stachyose. CC -!- Cf. EC 2.4.1.123. // ID 2.4.1.68 DE Glycoprotein 6-alpha-L-fucosyltransferase. AN GDP-fucose--glycoprotein fucosyltransferase. AN GDP-L-Fuc:N-acetyl-beta-D-glucosaminide a16fucosyltransferase. AN GDP-L-fucose-glycoprotein fucosyltransferase. AN Glycoprotein fucosyltransferase. AN Guanosine diphosphofucose-glycoprotein fucosyltransferase. CA GDP-L-fucose + N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D- CA mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl- CA (1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N- CA acetyl-beta-D-glucosaminyl}asparagine = GDP + N(4)-{N-acetyl-beta-D- CA glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D- CA glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N- CA acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->6)]-N-acetyl- CA beta-D-glucosaminyl}asparagine. CC -!- This enzyme catalyzes a reaction similar to that of EC 2.4.1.214, CC but transfers the L-fucosyl group from GDP-beta-L-fucose to form CC an alpha-1,6-linkage rather than an alpha-1,3-linkage. DR Q9N0W2, FUT8_BOVIN; Q9BYC5, FUT8_HUMAN; Q9WTS2, FUT8_MOUSE; DR P79282, FUT8_PIG ; // ID 2.4.1.69 DE Galactoside 2-alpha-L-fucosyltransferase. AN Galactoside 2-L-fucosyltransferase. AN Blood group H alpha-2-fucosyltransferase. AN Guanosine diphosphofucose-galactoside 2-L-fucosyltransferase. AN Alpha-(1->2)-L-fucosyltransferase. AN Alpha-2-fucosyltransferase. AN Alpha-2-L-fucosyltransferase. AN Blood-group substance H-dependent fucosyltransferase. AN Guanosine diphosphofucose-glycoprotein 2-alpha-fucosyltransferase. AN Guanosine diphosphofucose-lactose fucosyltransferase. AN GDP fucose-lactose fucosyltransferase. AN Guanosine diphospho-L-fucose-lactose fucosyltransferase. AN Guanosine diphosphofucose-beta-D-galactosyl-alpha-2-L- AN fucosyltransferase. AN Guanosine diphosphofucose-galactosylacetylglucosaminylgalactosyl- AN glucosylceramide alpha-L-fucosyltransferase. AN Guanosine diphosphofucose-glycoprotein 2-alpha-L-fucosyltransferase. AN H-gene-encoded beta-galactoside alpha-1->2fucosyltransferase. AN Secretor-type beta-galactoside alpha1->2fucosyltransferase. AN beta-galactoside alpha1->2fucosyltransferase. AN GDP-L-fucose:lactose fucosyltransferase. CA GDP-beta-L-fucose + beta-D-galactosyl-R = GDP + alpha-L-fucosyl-1,2- CA beta-D-galactosyl-R. CC -!- Free lactose can act as acceptor. CC -!- The action on glycolipid was previously listed as EC 2.4.1.89. DR Q9SWH5, FUT1_ARATH; P19526, FUT1_HUMAN; O09160, FUT1_MOUSE; DR Q9M5Q1, FUT1_PEA ; Q29043, FUT1_PIG ; Q10979, FUT1_RABIT; DR Q10980, FUT1_RAT ; Q28113, FUT2_BOVIN; Q10981, FUT2_HUMAN; DR Q9JL27, FUT2_MOUSE; Q10982, FUT2_PIG ; Q10983, FUT2_RABIT; DR Q10984, FUT2_RAT ; P97353, SEC1_MOUSE; // ID 2.4.1.70 DE Poly(ribitol-phosphate) N-acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + poly(ribitol phosphate) = UDP + CA N-acetyl-D-glucosaminyl-poly(ribitol phosphate). CC -!- Involved in the synthesis of teichoic acids. // ID 2.4.1.71 DE Arylamine glucosyltransferase. AN UDP glucose-arylamine glucosyltransferase. CA UDP-glucose + an arylamine = UDP + an N-D-glucosylarylamine. // ID 2.4.1.72 DE Transferred entry: 2.4.2.24. // ID 2.4.1.73 DE Lipopolysaccharide glucosyltransferase II. CA UDP-glucose + lipopolysaccharide = UDP + D-glucosyl-lipopolysaccharide. CC -!- Transfers glucosyl residues to the D-galactosyl-D-glucosyl side- CC chains in the partially completed core of lipopolysaccharide (cf. CC EC 2.4.1.44, EC 2.4.1.56, and EC 2.4.1.58). // ID 2.4.1.74 DE Glycosaminoglycan galactosyltransferase. CA UDP-galactose + glycosaminoglycan = UDP + D-galactosylglycosaminoglycan. CC -!- Involved in the biosynthesis of galactose-containing CC glycosaminoglycan of Dictyostelium discoideum. // ID 2.4.1.75 DE UDP-galacturonosyltransferase. AN p-nitrophenol conjugating enzyme. CA UDP-galacturonate + acceptor = UDP + acceptor beta-D-galacturonide. // ID 2.4.1.76 DE Transferred entry: 2.4.1.17. // ID 2.4.1.77 DE Transferred entry: 2.4.1.17. // ID 2.4.1.78 DE Phosphopolyprenol glucosyltransferase. CA UDP-glucose + polyprenyl phosphate = UDP + polyprenylphosphate-glucose. CC -!- Ficaprenyl phosphate is the best substrate; other polyprenols act, CC more slowly. // ID 2.4.1.79 DE Galactosylgalactosylglucosylceramide beta-D-acetyl- DE galactosaminyltransferase. AN Globoside synthetase. CA UDP-N-acetyl-D-galactosamine + D-galactosyl-(1,4)-D-galactosyl-(1,4)-D- CA glucosylceramide = UDP + N-acetyl-D-galactosaminyl-(1,3)-D-galactosyl- CA (1,4)-D-galactosyl-(1,4)-D-glucosylceramide. // ID 2.4.1.80 DE Ceramide glucosyltransferase. AN Glucosylceramide synthase. AN UDP glucose-ceramide glucosyltransferase. CA UDP-glucose + N-acylsphingosine = UDP + D-glucosyl-N-acylsphingosine. CC -!- Sphingosine and dihydrosphingosine can also act as acceptor. CC -!- CDP-glucose can act as donor. DR Q16739, CEGT_HUMAN; // ID 2.4.1.81 DE Flavone 7-O-beta-glucosyltransferase. AN UDP-glucose-apigenin beta-glucosyltransferase. AN UDP-glucose-luteolin beta-D-glucosyltransferase. CA UDP-glucose + 5,7,3',4'-tetrahydroxyflavone = UDP + 7-O-beta-D-glucosyl- CA 5,7,3',4'-tetrahydroxyflavone. CC -!- A number of flavones, flavonones and flavonols can function as CC acceptors. CC -!- Different from EC 2.4.1.91. // ID 2.4.1.82 DE Galactinol--sucrose galactosyltransferase. CA 1-alpha-D-galactosyl-myo-inositol + sucrose = myo-inositol + raffinose. CC -!- 4-nitrophenyl-alpha-D-galactopyranoside can also act as donor. CC -!- Also catalyzes an exchange reaction between raffinose and sucrose CC (cf. EC 2.4.1.123). // ID 2.4.1.83 DE Dolichyl-phosphate beta-D-mannosyltransferase. AN Dolichol-phosphate mannosyltransferase. AN Dolichol-phosphate mannose synthase. AN Mannosylphosphodolichol synthase. AN Mannosylphosphoryldolichol synthase. CA GDP-mannose + dolichyl phosphate = GDP + dolichyl D-mannosyl phosphate. CC -!- Acts only on long-chain polyprenyl phosphates and alpha- CC dihydropolyprenyl phosphates, larger than C(35). DR Q9WU83, DPM1_CRIGR; Q9VIU7, DPM1_DROME; O60762, DPM1_HUMAN; DR O70152, DPM1_MOUSE; O14466, DPM1_SCHPO; P54856, DPM1_USTMA; DR P14020, DPM1_YEAST; // ID 2.4.1.84 DE Transferred entry: 2.4.1.17. // ID 2.4.1.85 DE Cyanohydrin beta-glucosyltransferase. AN UDP-glucose-p-hydroxymandelonitrile glucosyltransferase. CA UDP-glucose + (S)-4-hydroxymandelonitrile = UDP + CA (S)-4-hydroxymandelonitrile beta-D-glucoside. CC -!- Also acts on (S)-mandelonitrile. // ID 2.4.1.86 DE Glucosaminylgalactosylglucosylceramide beta-galactosyltransferase. AN Paragloboside synthase. CA UDP-galactose + N-acetyl-D-glucosaminyl-(1,3)-D-galactosyl-(1,4)-D- CA glucosylceramide = UDP + D-galactosyl-N-acetyl-D-glucosaminyl-(1,3)-D- CA galactosyl-(1,4)-D-glucosylceramide. // ID 2.4.1.87 DE N-acetyllactosaminide 3-alpha-galactosyltransferase. AN N-acetyllactosaminide alpha-1,3-galactosyltransferase. AN Galactosyltransferase. AN Alpha-galactosyltransferase. AN UDP-Gal:beta-D-Gal(1,4)-D-GlcNAc alpha-(1,3)-galactosyltransferase. AN UDP-Gal:N-acetyllactosaminide alpha-(1,3)-galactosyltransferase. AN UDP-Gal:N-acetyllactosaminide alpha-1,3-D-galactosyltransferase. AN UDP-Gal:Gal-beta-1->4GlcNAc-R alpha-1->3-galactosyltransferase. AN UDP-galactose-acetyllactosamine alpha-D-galactosyltransferase. AN UDPgalactose:beta-D-galactosyl-beta-1,4-N-acetyl-D-glucosaminyl- AN glycopeptide alpha-1,3-D-galactosyltransferase. AN Glucosaminylglycopeptide alpha-1,3-galactosyltransferase. AN Uridine diphosphogalactose-acetyllactosamine alpha-1->3- AN galactosyltransferase. AN Uridine diphosphogalactose-acetyllactosamine galactosyltransferase. AN Uridine diphosphogalactose-galactosylacetylglucosaminylgalactosyl- AN glucosylceramide galactosyltransferase. AN Beta-D-galactosyl-N-acetylglucosaminylglycopeptide alpha-1,3- AN galactosyltransferase. CA UDP-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R CA = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N- CA acetylglucosaminyl-R. CC -!- Acts on alpha-galactosyl-1,4-N-acetylglucosaminyl termini on CC asialo-alpha(1)-acid glycoprotein and N-acetyllactosamine (beta-D- CC galactosyl-1,4-N-acetyl-beta-D-glucosamine), but not on 2'- CC fucosylated-N-acetyllactosamine. CC -!- The non-reducing terminal N-acetyllactosamine residues of CC glycoproteins can also act as acceptor. CC -!- Now includes EC 2.4.1.124 and EC 2.4.1.151. DR P14769, GATR_BOVIN; P23336, GATR_MOUSE; P50127, GATR_PIG ; // ID 2.4.1.88 DE Globoside alpha-N-acetylgalactosaminyltransferase. AN Forssman synthase. CA UDP-N-acetyl-D-galactosamine + N-acetyl-D-galactosaminyl-(1,3)-D- CA galactosyl-(1,4)-D-galactosyl-(1,4)-D-glucosylceramide = UDP + N-acetyl- CA D-galactosaminyl-N-acetyl-D-galactosaminyl-(1,3)-D-galactosyl-(1,4)-D- CA galactosyl-(1,4)-D-glucosylceramide. // ID 2.4.1.89 DE Transferred entry: 2.4.1.69. // ID 2.4.1.90 DE N-acetyllactosamine synthase. AN N-acetylglucosamine (beta 1,4)galactosyltransferase. AN Acetyllactosamine synthetase. AN UDP-galactose-N-acetyl-glucosamine beta-D-galactosyltransferase. AN NAL synthetase. CA UDP-galactose + N-acetyl-D-glucosamine = UDP + N-acetyllactosamine. CC -!- The reaction is catalyzed by a component of EC 2.4.1.22, which is CC identical with EC 2.4.1.38, and by an enzyme from the golgi CC apparatus of animal tissues. CC -!- Formerly EC 2.4.1.98. DR P08037, B4G1_BOVIN; P15291, B4G1_HUMAN; P15535, B4G1_MOUSE; DR P80225, B4G1_RAT ; O60909, B4G2_HUMAN; O60512, B4G3_HUMAN; DR O60513, B4G4_HUMAN; // ID 2.4.1.91 DE Flavonol 3-O-glucosyltransferase. AN UDP-glucose flavonol 3,O-glucosyltransferase. CA UDP-glucose + a flavonol = UDP + flavonol 3-O-D-glucoside. CC -!- Acts on a variety of flavonols, including quercetin and quercetin CC 7-O-glucoside. CC -!- Different from EC 2.4.1.81. PR PROSITE; PDOC00359; DR P16166, UFO1_MAIZE; Q40284, UFO1_MANES; P16165, UFO2_MAIZE; DR Q40285, UFO2_MANES; P16167, UFO3_MAIZE; Q40286, UFO4_MANES; DR Q40287, UFO5_MANES; Q40288, UFO6_MANES; Q40289, UFO7_MANES; DR Q96493, UFOG_GENTR; P14726, UFOG_HORVU; Q43716, UFOG_PETHY; DR Q43641, UFOG_SOLME; P51094, UFOG_VITVI; // ID 2.4.1.92 DE (N-acetylneuraminyl)-galactosylglucosylceramide DE N-acetylgalactosaminyltransferase. CA UDP-N-acetyl-D-galactosamine + (N-acetylneuraminyl)-D-galactosyl-D- CA glucosylceramide = UDP + N-acetyl-D-galactosaminyl-(N-acetylneuraminyl)- CA D-galactosyl-D-glucosylceramide. DR Q00973, CAG2_HUMAN; Q09200, CAG2_MOUSE; Q10468, CAG2_RAT ; // ID 2.4.1.93 DE Inulin fructotransferase (depolymerizing). AN Inulase II. AN Inulinase II. CA Transfers a terminal D-fructosyl-D-fructofuranosyl group to the terminal CA 3-position, forming a cyclic anhydride. CC -!- Cf. EC 2.4.1.200. // ID 2.4.1.94 DE Protein N-acetylglucosaminyltransferase. AN N-GlcNAc transferase. CA UDP-N-acetyl-D-glucosamine + protein = UDP + 4-N-(N-acetyl-D- CA glucosaminyl)-protein. CC -!- The acceptor is the asparagine residue in a sequence of the form CC Asn-Xaa-(Ser/Thr). // ID 2.4.1.95 DE Bilirubin-glucuronoside glucuronosyltransferase. AN Bilirubin monoglucuronide transglucuronidase. CA 2 bilirubin-glucuronoside = bilirubin + bilirubin-bisglucuronoside. // ID 2.4.1.96 DE Sn-glycerol-3-phosphate 1-galactosyltransferase. AN Isofloridoside-phosphate synthase. CA UDP-galactose + sn-glycerol 3-phosphate = UDP + alpha-D-galactosyl- CA (1,1')-sn-glycerol 3-phosphate. CC -!- The product is hydrolyzed by a phosphatase to isofloridoside, which CC is involved in osmoregulation (cf. EC 2.4.1.137). // ID 2.4.1.97 DE 1,3-beta-glucan phosphorylase. AN Laminarin phosphorylase. CA {(1,3)-beta-D-glucosyl}(N) + phosphate = {(1,3)-beta-D-glucosyl}(N-1) + CA alpha-D-glucose 1-phosphate. CC -!- Acts on a range of beta-(1,3)-oligoglucans, and on glucans of CC laminarin type. CC -!- Different from EC 2.4.1.30 and EC 2.4.1.31. // ID 2.4.1.98 DE Transferred entry: 2.4.1.90. // ID 2.4.1.99 DE Sucrose 1F-fructosyltransferase. CA Sucrose + sucrose = D-glucose + 1F-beta-D-fructosylsucrose. // ID 2.4.1.100 DE 1,2-beta-fructan 1F-fructosyltransferase. CA {(1,2)-beta-D-fructosyl}(M) + {(1,2)-beta-D-fructosyl}(N) = CA {(1,2)-beta-D-fructosyl}(M-1) + {(1,2)-beta-D-fructosyl}(N+1). // ID 2.4.1.101 DE Alpha-1,3-mannosyl-glycoprotein 2-beta-N- DE acetylglucosaminyltransferase. AN N-acetylglucosaminyltransferase I. AN N-glycosyl-oligosaccharide-glycoprotein N- AN acetylglucosaminyltransferase I. AN Uridine diphosphoacetylglucosamine-alpha-1,3-mannosylglycoprotein AN beta-1,2-N-acetylglucosaminyltransferase. AN UDP-N-acetylglucosaminyl:alpha-1,3-D-mannoside-beta-1,2-N- AN acetylglucosaminyltransferase I. AN UDP-N-acetylglucosaminyl:alpha-3-D-mannoside beta-1,2-N- AN acetylglucosaminyltransferase I. AN Alpha-1,3-mannosyl-glycoprotein beta-1,2-N- AN acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + 3-(alpha-D-mannosyl)-beta-D-mannosyl-R = CA UDP + 3-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D- CA mannosyl-R. CC -!- R represents the remainder of the N-linked oligosaccharide in the CC glycoprotein acceptor. CC -!- Note that this enzyme acts before N-acetylglucosaminyltransferases CC II, III, IV, V and VI. CC -!- Formerly EC 2.4.1.51. DR Q11068, GNT1_CAEEL; P26572, GNT1_HUMAN; P27808, GNT1_MOUSE; DR P27115, GNT1_RABIT; Q09325, GNT1_RAT ; // ID 2.4.1.102 DE Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N- DE acetylglucosaminyltransferase. AN O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase AN I. AN Beta(6)-N-acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,3-N-acetyl-D- CA galactosaminyl-R = UDP + beta-D-galactosyl-1,3-(N-acetyl-beta-D- CA glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R. CC -!- Cf. EC 2.4.1.146, EC 2.4.1.147, and EC 2.4.1.148. DR Q92180, G6NT_BOVIN; Q02742, G6NT_HUMAN; Q09324, G6NT_MOUSE; // ID 2.4.1.103 DE Alizarin 2-beta-glucosyltransferase. CA UDP-glucose + alizarin = UDP + 1-hydroxy-2-(beta-D-glucosyloxy)-9,10- CA anthraquinone. CC -!- Acts on other hydroxy- and dihydroxy-derivatives of 9,10- CC anthraquinone. // ID 2.4.1.104 DE O-dihydroxycoumarin 7-O-glucosyltransferase. CA UDP-glucose + 7,8-dihydroxycoumarin = UDP + daphnin. CC -!- Converts the aglycone daphetin into daphnin and, more slowly, CC esculetin into cichorin, umbelliferone into skimmin, hydrangetin CC into hydrangin and scopoletin into scopolin. // ID 2.4.1.105 DE Vitexin beta-glucosyltransferase. CA UDP-glucose + vitexin = UDP + vitexin 2''-O-beta-D-glucoside. CC -!- Vitexin is a flavonoid from Cannabis sativa and some populations of CC Silex alba. // ID 2.4.1.106 DE Isovitexin beta-glucosyltransferase. CA UDP-glucose + isovitexin = UDP + isovitexin 2''-O-beta-D-glucoside. CC -!- Isovitexin is a flavonoid from petals of Silex alba. // ID 2.4.1.107 DE Transferred entry: 2.4.1.17. // ID 2.4.1.108 DE Transferred entry: 2.4.1.17. // ID 2.4.1.109 DE Dolichyl-phosphate-mannose--protein mannosyltransferase. CA Dolichyl phosphate D-mannose + protein = dolichyl phosphate + CA O-D-mannosyl-protein. CC -!- Transfers mannosyl residues to the hydroxyl of serine or threonine CC residues, producing cell-wall mannoproteins. CC -!- Acts only on long-chain alpha-dihydropolyprenyl derivatives, larger CC than C(35). DR O74189, PMT1_CANAL; P33775, PMT1_YEAST; P31382, PMT2_YEAST; DR P47190, PMT3_YEAST; P46971, PMT4_YEAST; P52867, PMT5_YEAST; DR P42934, PMT6_YEAST; Q06644, PMT7_YEAST; O13898, PMTX_SCHPO; DR O42933, PMTY_SCHPO; Q9Y6A1, POT1_HUMAN; Q8R2R1, POT1_MOUSE; DR Q99PR0, POT1_RAT ; Q9UKY4, POT2_HUMAN; Q8BGQ4, POT2_MOUSE; // ID 2.4.1.110 DE tRNA-queuosine beta-mannosyltransferase. CA GDP-mannose + tRNA(Asp)-queuosine = GDP + tRNA(Asp)-O-5''-beta-D- CA mannosylqueuosine. // ID 2.4.1.111 DE Coniferyl-alcohol glucosyltransferase. CA UDP-glucose + coniferyl alcohol = UDP + coniferin. CC -!- Sinapyl alcohol can also act as acceptor. // ID 2.4.1.112 DE Alpha-1,4-glucan-protein synthase (UDP-forming). CA UDP-glucose + protein = UDP + alpha-D-glucosyl-protein. CC -!- Builds up alpha-1,4-glucan chains covalently bound to protein, thus CC acting as an initiator of glycogen synthesis. // ID 2.4.1.113 DE Alpha-1,4-glucan-protein synthase (ADP-forming). CA ADP-glucose + protein = ADP + alpha-D-glucosyl-protein. CC -!- Builds up alpha-1,4-glucan chains covalently bound to protein, thus CC acting as an initiator of glycogen synthesis. // ID 2.4.1.114 DE 2-coumarate O-beta-glucosyltransferase. CA UDP-glucose + trans-2-hydroxycinnamate = UDP + trans-beta-D-glucosyl- CA 2-hydroxycinnamate. CC -!- Coumarinate (cis-2-hydroxycinnamate) does not act as acceptor. // ID 2.4.1.115 DE Anthocyanidin 3-O-glucosyltransferase. CA UDP-glucose + anthocyanidin = UDP + anthocyanidin-3-O-D-glucoside. CC -!- Pelargonidin and delphinidin can also act as acceptors, more slowly. CC -!- Does not catalyze glucosylation of the 5-position of cyanidin and CC does not act on flavonols such as quercetin and kaempferol (cf. CC EC 2.4.1.91). // ID 2.4.1.116 DE Cyanidin-3-rhamnosylglucoside 5-O-glucosyltransferase. CA UDP-glucose + cyanidin-3-O-D-rhamnosyl-(1,6)-D-glucoside = UDP + CA cyanidin-3-O-[D-rhamnosyl-(1,6)-D-glucoside]-5-O-D-glucoside. CC -!- Pelargonidin-3-O-rhamnosyl glucoside, and, more slowly, cyanidin CC 3-O-glucoside, can also act as acceptors. // ID 2.4.1.117 DE Dolichyl-phosphate beta-glucosyltransferase. CA UDP-glucose + dolichyl phosphate = UDP + dolichyl beta-D-glucosyl CA phosphate. CC -!- Solanesyl phosphate and ficaprenyl phosphate can act as acceptors, CC more slowly. DR Q9Y673, ALG5_HUMAN; Q9DB25, ALG5_MOUSE; P40350, ALG5_YEAST; // ID 2.4.1.118 DE Cytokinin 7-beta-glucosyltransferase. AN UDP-glucose-zeatin 7-glucosyltransferase. CA UDP-glucose + N(6)-alkylaminopurine = UDP + N(6)-alkylaminopurine-7- CA beta-D-glucoside. CC -!- Acts on a range of N(6)-substituted adenines, including zeatin CC (N(6)-(4-hydroxy-3-methylbut-trans-2-enylamino)purine) and N(6)- CC benzylaminopurine, but not N(6)-benzyladenine. CC -!- With some acceptors, 9-beta-D-glucosides are also formed. // ID 2.4.1.119 DE Dolichyl-diphosphooligosaccharide--protein glycosyltransferase. CA Dolichyl diphosphooligosaccharide + protein L-asparagine = dolichyl CA diphosphate + a glycoprotein with the oligosaccharide chain attached CA by glycosylamine linkage to protein L-asparagine. CC -!- Transfers the glucosyl-mannosyl-glucosamine polysaccharide side- CC chains of glycoproteins to an asparagine residue in a sequence CC Asn-Xaa-Ser/Thr in the nascent polypeptide chains of the protein CC moiety. PR PROSITE; PDOC00172; DR P12244, GSBP_CHICK; P80896, OST1_CHICK; P80897, OST2_CHICK; DR P45971, OST4_CAEEL; Q05052, OST4_CANFA; P48440, OST4_CHICK; DR Q24319, OST4_DROME; P39656, OST4_HUMAN; O54734, OST4_MOUSE; DR Q29381, OST4_PIG ; Q10176, OSTA_SCHPO; P41543, OSTA_YEAST; DR P33767, OSTB_YEAST; Q02795, OSTD_YEAST; O14238, OSTE_SCHPO; DR P46964, OSTE_YEAST; P48439, OSTG_YEAST; Q99380, OSTS_YEAST; DR Q03723, OSTY_YEAST; Q92316, OSTZ_YEAST; P04843, RIB1_HUMAN; DR P07153, RIB1_RAT ; P04844, RIB2_HUMAN; P25235, RIB2_RAT ; // ID 2.4.1.120 DE Sinapate 1-glucosyltransferase. CA UDP-glucose + sinapate = UDP + 1-sinapoyl-D-glucose. CC -!- Some other hydroxycinnamates, including 4-coumarate, ferulate and CC caffeate, can also act as acceptors, more slowly. CC -!- Only glucose esters, not glucosides, are formed (cf. EC 2.4.1.126). // ID 2.4.1.121 DE Indole-3-acetate beta-glucosyltransferase. AN IAA-Glu synthetase. CA UDP-glucose + indole-3-acetate = UDP + indole-3-acetyl-beta-1-D-glucose. DR Q41819, IAAG_MAIZE; // ID 2.4.1.122 DE Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase. CA UDP-galactose + glycoprotein N-acetyl-D-galactosamine = UDP + CA glycoprotein D-galactosyl-(1,3)-N-acetyl-D-galactosamine. CC -!- The non-reducing O-serine-linked N-acetylgalactosamine residues in CC mucin glycoproteins can act as acceptors. // ID 2.4.1.123 DE Inositol 1-alpha-galactosyltransferase. AN Galactinol synthase. CA UDP-galactose + myo-inositol = UDP + 1-O-alpha-D-galactosyl-D-myo- CA inositol. CC -!- An enzyme from cucurbits involved in the formation of raffinose and CC stachyose (cf. EC 2.4.1.67 and EC 2.4.1.82). // ID 2.4.1.124 DE Transferred entry: EC 2.4.1.87. // ID 2.4.1.125 DE Sucrose-1,6-alpha-glucan 3(6)-alpha-glucosyltransferase. AN Water-soluble-glucan synthase. CA Sucrose + {(1,6)-alpha-D-glucosyl}(N) = D-fructose + {(1,6)-alpha-D- CA glucosyl}(N+1). CC -!- Also transfers glucosyl residues to the 3-position on glucose CC residues in glucans, producing a highly-branched 1,6-alpha-D-glucan. // ID 2.4.1.126 DE Hydroxycinnamate 4-beta-glucosyltransferase. CA UDP-glucose + trans-4-hydroxycinnamate = UDP + 4-O-beta-D-glucosyl-4- CA hydroxycinnamate. CC -!- Acts on 4-coumarate, ferulate, caffeate and sinapate, forming a CC mixture of 4-glucosides and glucose esters (cf. EC 2.4.1.120). // ID 2.4.1.127 DE Monoterpenol beta-glucosyltransferase. CA UDP-glucose + (-)-menthol = UDP + (-)-menthyl O-beta-D-glucoside. CC -!- (+)-neomenthol can also act as acceptor. // ID 2.4.1.128 DE Scopoletin glucosyltransferase. CA UDP-glucose + scopoletin = UDP + scopolin. // ID 2.4.1.129 DE Peptidoglycan glycosyltransferase. AN PG-II. AN Bactoprenyldiphospho-N-acetylmuramoyl-(N-acetyl-D-glucosaminyl)- AN pentapeptide:peptidoglycan N-acetylmuramoyl-N-acetyl-D- AN glucosaminyltransferase. AN Penicillin binding protein (3 or 1B). AN Peptidoglycan transglycosylase. AN Peptidoglycan TGase. CA [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)- CA diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys- CA D-Ala-D-Ala)-diphosphoundecaprenol = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala- CA gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-diphosphoundecaprenol + undecaprenyl CA diphosphate. CC -!- The enzyme also works when the lysine residue is replaced by meso- CC 2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined CC with adjacent residues through its L-centre, as it is in Gram- CC negative and some Gram-positive organisms. CC -!- The undecaprenol involved is ditrans,octacis-undecaprenol. CC -!- Involved in the synthesis of cell-wall peptidoglycan. DR P57317, FTSI_BUCAI; O85297, FTSI_BUCAP; P04286, FTSI_ECOLI; DR P45059, FTSI_HAEIN; Q9MUV9, FTSI_MESVI; Q9TL36, FTSI_NEPOL; DR P57296, PBPB_BUCAI; P02919, PBPB_ECOLI; P45345, PBPB_HAEIN; DR Q9KUC0, PBPB_VIBCH; // ID 2.4.1.130 DE Dolichyl-phosphate-mannose-glycolipid alpha-mannosyltransferase. CA Transfers an alpha-D-mannosyl residue from dolichyl-phosphate CA D-mannose into membrane lipid-linked oligosaccharide. CC -!- Four of the nine mannosyl residues in the main membrane lipid-linked CC oligosaccharide of the structure Glc(3)Man(9)GlcNAc(2) are produced CC by this enzyme. // ID 2.4.1.131 DE Glycolipid 2-alpha-mannosyltransferase. CA Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked CA oligosaccharide, forming an alpha-1,2-D-mannosyl-D-mannose linkage. CC -!- The two 1,2-linked mannosyl residues in the mammalian lipid-linked CC oligosaccharide of the structure Glc(3)Man(9)GlcNAc(2) are produced CC by this enzyme. DR Q00310, KRE2_CANAL; P27809, KRE2_YEAST; P27810, KTR1_YEAST; DR P33550, KTR2_YEAST; P38130, KTR3_YEAST; P38131, KTR4_YEAST; DR P53966, KTR5_YEAST; P54070, KTR6_YEAST; P40504, KTR7_YEAST; DR P46592, MNT2_CANAL; P87207, MNT3_CANAL; P26725, YUR1_YEAST; // ID 2.4.1.132 DE Glycolipid 3-alpha-mannosyltransferase. AN Mannosyltransferase II. CA Transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked CA oligosaccharide, forming an alpha-1,3-D-mannosyl-D-mannose linkage. CC -!- The 1,3-linked mannosyl residue in the mammalian lipid-linked CC oligosaccharide of the structure Glc(3)Man(9)GlcNAc(2) is produced CC by this enzyme. // ID 2.4.1.133 DE Xylosylprotein 4-beta-galactosyltransferase. AN Galactosyltransferase I. AN UDP-D-galactose:D-xylose galactosyltransferase. AN UDP-D-galactose:xylose galactosyltransferase. AN Uridine diphosphogalactose-xylose galactosyltransferase. CA UDP-galactose + O-beta-D-xylosylprotein = UDP + 4-beta-D-galactosyl-O- CA beta-D-xylosylprotein. CF Manganese. CC -!- Involved in the biosynthesis of the linkage region of CC glycosaminoglycan chains as part of proteoglycan biosynthesis CC (chondroitin, dermatan and heparan sulfates). DR Q9UBV7, B4G7_HUMAN; // ID 2.4.1.134 DE Galactosylxylosylprotein 3-beta-galactosyltransferase. AN Galactosyltransferase II. AN Uridine diphosphogalactose-galactosylxylose galactosyltransferase. CA UDP-galactose + 4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP + CA 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein. CF Manganese. CC -!- Involved in the biosynthesis of the linkage region of CC glycosaminoglycan chains as part of proteoglycan biosynthesis CC (chondroitin, dermatan and heparan sulfates). // ID 2.4.1.135 DE Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase. AN Glucuronosyltransferase I. AN Uridine diphosphate glucuronic acid:acceptor glucuronosyltransferase. CA UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D- CA xylosylprotein = UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4- CA beta-D-galactosyl-O-beta-D-xylosylprotein. CF Manganese. CC -!- Involved in the biosynthesis of the linkage region of CC glycosaminoglycan chains as part of proteoglycan biosynthesis CC (chondroitin, dermatan and heparan sulfates). DR Q9P2W7, B3G1_HUMAN; Q9CW73, B3G1_MOUSE; O35789, B3G1_RAT ; DR Q9NPZ5, B3G2_HUMAN; P59270, B3G2_MOUSE; Q9Z137, B3G2_RAT ; DR Q9WU47, B3G3_CRIGR; O94766, B3G3_HUMAN; P58158, B3G3_MOUSE; DR O97422, B3GT_DROME; Q09363, SQV8_CAEEL; // ID 2.4.1.136 DE Gallate 1-beta-glucosyltransferase. AN UDP-glucose-vanillate 1-glucosyltransferase. CA UDP-glucose + gallate = UDP + 1-galloyl-beta-D-glucose. CC -!- A number of substituted benzoic acids, and, more slowly, cinnamic CC acids, can act as acceptor. Vanillin is the best acceptor CC investigated. // ID 2.4.1.137 DE Sn-glycerol-3-phosphate 2-alpha-galactosyltransferase. AN Floridoside-phosphate synthase. CA UDP-galactose + sn-glycerol 3-phosphate = UDP + 2-(alpha-D-galactosyl)- CA sn-glycerol 3-phosphate. CC -!- The product is hydrolyzed by a phosphatase to floridoside CC (cf. EC 2.4.1.96). // ID 2.4.1.138 DE Mannotetraose 2-alpha-N-acetylglucosaminyltransferase. AN Alpha-N-acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + 1,3-alpha-D-mannosyl-1,2-alpha-D-mannosyl- CA 1,2-alpha-D-mannosyl-D-mannose = UDP + 1,3-alpha-D-mannosyl-1,2-(N- CA acetyl-alpha-D-glucosaminyl-alpha-D-mannosyl)-1,2-alpha-D-mannosyl-D- CA mannose. // ID 2.4.1.139 DE Maltose synthase. CA 2 alpha-D-glucose 1-phosphate = maltose + 2 phosphate. CC -!- Neither free phosphate nor maltose 1-phosphate is an intermediate in CC the reaction. // ID 2.4.1.140 DE Alternansucrase. CA Transfers an alpha-D-glucosyl residue alternately to the 6-position or CA the 3-position of the non-reducing terminal residue of an alpha-D-glucan, CA thus producing a glucan having alternating alpha-1,6 and 1,3 linkages. CC -!- The product, which has quite different properties from other CC dextrans, has been called alternan. // ID 2.4.1.141 DE N-acetylglucosaminyldiphosphodolichol N-acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + N-acetyl-D-glucosaminyl-diphosphodolichol = CA UDP + N,N''-diacetylchitobiosyldiphosphodolichol. // ID 2.4.1.142 DE Chitobiosyldiphosphodolichol beta-mannosyltransferase. AN Guanosine diphosphomannose-dolichol diphosphochitobiose AN mannosyltransferase. AN GDP-mannose-dolichol diphosphochitobiose mannosyltransferase. CA GDP-mannose + chitobiosyldiphosphodolichol = GDP + CA beta-1,4-D-mannosylchitobiosyldiphosphodolichol. DR P16661, ALG1_YEAST; // ID 2.4.1.143 DE Alpha-1,6-mannosyl-glycoprotein 2-beta-N- DE acetylglucosaminyltransferase. AN N-acetylglucosaminyltransferase II. AN N-glycosyl-oligosaccharide-glycoprotein N- AN acetylglucosaminyltransferase II. AN Acetylglucosaminyltransferase II. AN Uridine diphosphoacetylglucosamine-mannoside alpha-1->6- AN acetylglucosaminyltransferase. AN Uridine diphosphoacetylglucosamine-alpha-1,6- AN mannosylglycoprotein beta-1-2-N-acetylglucosaminyltransferase. AN Uridine diphosphoacetylglucosamine-alpha-D-mannoside beta 1-2- AN acetylglucosaminyltransferase. AN UDP-GlcNAc:mannoside alpha-1-6 acetylglucosaminyltransferase. AN Alpha-1,6-mannosyl-glycoprotein beta-1,2-N- AN acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + 6-(alpha-D-mannosyl)-beta-D-mannosyl-R = CA UDP + 6-(2-[N-acetyl-beta-D-glucosaminyl]-alpha-D-mannosyl)-beta-D- CA mannosyl-R. CC -!- R represents the remainder of the N-linked oligosaccharide in the CC glycoprotein acceptor. CC -!- Note that this enzyme acts after N-acetylglucosaminyltransferase CC I but before N-acetylglucosaminyltransferases III, IV, V and VI. CC -!- Formerly EC 2.4.1.51. DR Q10469, GNT2_HUMAN; Q09326, GNT2_RAT ; // ID 2.4.1.144 DE Beta-1,4-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase. AN N-glycosyl-oligosaccharide-glycoprotein N- AN acetylglucosaminyltransferase III. AN N-acetylglucosaminyltransferase III. AN Uridine diphosphoacetylglucosamine-glycopeptide beta-4- AN acetylglucosaminyltransferase III. AN Beta-1,4-mannosyl-glycoprotein beta-1,4-N- AN acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + beta-D-mannosyl-R = UDP + CA 4-(N-acetyl-beta-D-glucosaminyl)-beta-D-mannosyl-R. CC -!- R represents the remainder of the N-linked oligosaccharide in the CC glycoprotein acceptor. CC -!- The action of this enzyme probably prevents further attachment of CC N-acetylglucosamine residues to the growing carbohydrate chain. CC -!- Formerly EC 2.4.1.51. DR Q09327, GNT3_HUMAN; Q10470, GNT3_MOUSE; Q02527, GNT3_RAT ; // ID 2.4.1.145 DE Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase. AN N-acetylglucosaminyltransferase IV. AN N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase AN IV. AN Beta-acetylglucosaminyltransferase IV. AN Uridine diphosphoacetylglucosamine-glycopeptide beta-4- AN acetylglucosaminyltransferase IV. AN Alpha-1,3-mannosylglycoprotein beta-1,4-N-acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + 3-(2-[N-acetyl-beta-D-glucosaminyl]- CA alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 3-(2,4-bis[N-acetyl-beta- CA D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R. CC -!- R represents the remainder of the N-linked oligosaccharide in the CC glycoprotein acceptor. CC -!- The best acceptor for this enzyme is probably the same as that CC favoured by EC 2.4.1.144. CC -!- Formerly EC 2.4.1.51. // ID 2.4.1.146 DE Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,3-N- DE acetylglucosaminyltransferase. AN O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase AN II. AN Elongation 3beta-GalNAc-transferase. CA UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,3-(N-acetyl-D- CA glucosaminyl-1,6)-N-acetyl-D-galactosaminyl-R = UDP + N-acetyl-beta- CA D-glucosaminyl-1,3-beta-D-galactosyl-1,3-(N-acetyl-beta-D-glucosaminyl- CA 1,6)-N-acetyl-D-galactosaminyl-R. CC -!- Cf. EC 2.4.1.102, EC 2.4.1.147, and EC 2.4.1.148. // ID 2.4.1.147 DE Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N- DE acetylglucosaminyltransferase. AN O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase AN III. AN Core 3beta-GlcNAc-transferase. CA UDP-N-acetyl-D-glucosamine + N-acetyl-D-galactosaminyl-R = UDP + CA N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl-D-galactosaminyl-R. CC -!- Cf. EC 2.4.1.102, EC 2.4.1.146, and EC 2.4.1.148. // ID 2.4.1.148 DE Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,6-N- DE acetylglucosaminyltransferase. AN O-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase AN IV. AN Core 6beta-GalNAc-transferase B. CA UDP-N-acetyl-D-glucosamine + N-acetyl-beta-D-glucosaminyl-1,3-N-acetyl- CA D-galactosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-(N-acetyl- CA beta-D-glucosaminyl-1,3)-N-acetyl-D-galactosaminyl-R. CC -!- Cf. EC 2.4.1.102, EC 2.4.1.146, and EC 2.4.1.147. // ID 2.4.1.149 DE N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase. AN Poly-N-acetyllactosamine extension enzyme. CA UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D- CA glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,3-beta-D- CA galactosyl-1,4-N-acetyl-D-glucosaminyl-R. CC -!- Acts on beta-galactosyl-1,4-N-acetylglucosaminyl termini on asialo- CC alpha(1)-acid glycoprotein and other glycoproteins and CC oligosaccharides. DR O43505, B3G6_HUMAN; // ID 2.4.1.150 DE N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase. AN N-acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-D- CA glucosaminyl-R = UDP + N-acetyl-beta-D-glucosaminyl-1,6-beta-D- CA galactosyl-1,4-N-acetyl-D-glucosaminyl-R. CC -!- Acts on beta-galactosyl-1,4-N-acetylglucosaminyl termini on asialo- CC alpha(1)-acid glycoprotein. DR Q06430, BGIB_HUMAN; P97402, BGIB_MOUSE; // ID 2.4.1.151 DE Transferred entry: 2.4.1.87. // ID 2.4.1.152 DE 4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase. AN Lewis-negative alpha-3-fucosyltransferase. AN Plasma alpha-3-fucosyltransferase. AN Guanosine diphosphofucose-glucoside alpha-1->3-fucosyltransferase. AN Galactoside 3-fucosyltransferase. AN GDP-L-fucose:1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-L- AN fucosyltransferase. CA GDP-beta-L-fucose + 1,4-beta-D-galactosyl-N-acetyl-D-glucosaminyl-R CA = GDP + 1,4-beta-D-galactosyl-(alpha-1,3-L-fucosyl)-N-acetyl-D- CA glucosaminyl-R. // ID 2.4.1.153 DE Dolichyl-phosphate alpha-N-acetylglucosaminyltransferase. AN Dolichyl-phosphate acetylglucosaminyltransferase. AN Dolichyl-phosphate N-acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + dolichyl phosphate = UDP + dolichyl CA N-acetyl-alpha-D-glucosaminyl phosphate. // ID 2.4.1.154 DE Globotriosylceramide beta-1,6-N-acetylgalactosaminyltransferase. AN Globoside N-acetylgalactosaminyltransferase. AN GalNAc transferase. CA UDP-N-acetyl-D-galactosamine + globotriosylceramide = UDP + CA globotetraosylceramide. CC -!- Highly acceptor-specific; does not acts on globotetraosylceramide or CC lactosylceramide. CC -!- The product has a terminal beta-N-acetylgalactosamine residue. // ID 2.4.1.155 DE Alpha-1,6-mannosyl-glycoprotein 6-beta-N- DE acetylglucosaminyltransferase. AN N-acetylglucosaminyltransferase V. AN Alpha-mannoside beta-1,6-N-acetylglucosaminyltransferase. AN Uridine diphosphoacetylglucosamine-alpha-mannoside beta-1->6- AN acetylglucosaminyltransferase. AN UDP-N-acetylglucosamine:alpha-mannoside-beta-1,6 N- AN acetylglucosaminyltransferase. AN Alpha-1,3(6)-mannosylglycoprotein beta-1,6-N- AN acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + 6-(2-[N-acetyl-beta-D-glucosaminyl]- CA alpha-D-mannosyl)-beta-D-mannosyl-R = UDP + 6-(2,6-bis[N-acetyl-beta- CA D-glucosaminyl]-alpha-D-mannosyl)-beta-D-mannosyl-R. CC -!- R represents the remainder of the N-linked oligosaccharide in the CC glycoprotein acceptor. DR P97259, GNT5_CRIGR; Q09328, GNT5_HUMAN; Q08834, GNT5_RAT ; // ID 2.4.1.156 DE Indolylacetyl-myo-inositol galactosyltransferase. AN Indol-3-ylacetyl-myo-inositol galactoside synthase. CA UDP-galactose + indol-3-ylacetyl-myo-inositol = UDP + 5-O-(indol-3- CA ylacetyl-myo-inositol)-D-galactoside. // ID 2.4.1.157 DE 1,2-diacylglycerol 3-glucosyltransferase. AN UDP-glucose-diacylglycerol glucosyltransferase. CA UDP-glucose + 1,2-diacylglycerol = UDP + 3-D-glucosyl-1,2- CA diacylglycerol. CC -!- Many diacylglycerols with long-chain acyl groups can act as CC acceptors. // ID 2.4.1.158 DE 13-hydroxydocosanoate 13-beta-glucosyltransferase. AN 13-glucosyloxydocosanoate 2'-beta-glucosyltransferase. AN UDP-glucose-13-hydroxydocosanoate glucosyltransferase. CA UDP-glucose + 13-hydroxydocosanoate = UDP + 13-beta-D- CA glucosyloxydocosanoate. CC -!- 13-beta-D-glucosyloxydocosanoate can also act as acceptor, leading CC to the formation by Candida bogoriensis of the extracellular CC glycolipid, hydroxydocosanoate sophoroside diacetate. // ID 2.4.1.159 DE Flavonol-3-O-glucoside L-rhamnosyltransferase. CA UDP-L-rhamnose + flavonol 3-O-D-glucoside = UDP + flavonol 3-O-L- CA rhamnosylglucoside. CC -!- Converts flavonol 3-O-glucosides to 3-O-rutinosides. CC -!- Also acts, more slowly, on rutin, quercetin 3-O-galactoside and CC flavonol O-3-rhamnosides. // ID 2.4.1.160 DE Pyridoxine 5'-O-beta-D-glucosyltransferase. AN UDP-glucose-pyridoxine glucosyltransferase. CA UDP-glucose + pyridoxine = UDP + 5'-O-beta-D-glucosylpyridoxine. CC -!- 4'-deoxypyridoxine and pyridoxamine can also act as acceptors, more CC slowly. // ID 2.4.1.161 DE Oligosaccharide 4-alpha-D-glucosyltransferase. AN Amylase III. CA Transfers the non-reducing terminal alpha-D-glucose residue from a CA 1,4-alpha-D-glucan to the 4-position of an alpha-D-glucan, thus CA bringing about the hydrolysis of oligosaccharides. CC -!- Acts on amylose, amylopectin, glycogen, and maltooligosaccharides, CC but not maltose. CC -!- No detectable free glucose is formed. // ID 2.4.1.162 DE Aldose beta-D-fructosyltransferase. CA Alpha-D-aldosyl(1) beta-D-fructoside + D-aldose(2) = D-aldose(1) + CA alpha-D-aldosyl(2) beta-D-fructoside. // ID 2.4.1.163 DE Beta-galactosyl-N-acetylglucosaminylgalactosyl-glucosylceramide DE Beta-1,3-acetylglucosaminyltransferase. AN Poly-N-acetyllactosamine extension enzyme. CA UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-beta-D- CA glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide = UDP + CA N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-beta-D- CA glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide. CF Manganese. // ID 2.4.1.164 DE Galactosyl-N-acetylglucosaminylgalactosyl-glucosylceramide beta-1,6- DE N-acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + D-galactosyl-1,4-N-acetyl-beta-D- CA glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide = UDP + CA N-acetyl-D-glucosaminyl-1,6-beta-D-galactosyl-1,4-N-acetyl-beta-D- CA glucosaminyl-1,3-beta-D-galactosyl-1,4 beta-D-glucosylceramide. CF Manganese. // ID 2.4.1.165 DE N-acetylneuraminylgalactosylglucosylceramide beta-1,4-N- DE acetylgalactosaminyltransferase. CA UDP-N-acetyl-D-galactosamine + N-acetylneuraminyl-2,3-alpha-D-galactosyl- CA 1,4-beta-D-glucosylceramide = UDP + N-acetyl-beta-D-galactosaminyl- CA 1,4-(N-acetyl-alpha-neuraminyl-2,3)-beta-D-galactosyl-1,4-beta-D- CA glucosylceramide. CF Manganese. CC -!- Only substances containing sialic acid residues can act as acceptors; CC bovine fetuin is the best acceptor tested. // ID 2.4.1.166 DE Raffinose--raffinose alpha-galactosyltransferase. CA 2 raffinose = 1(F)-alpha-D-galactosylraffinose + sucrose. CC -!- The 3(F) position of raffinose can also act as galactosyl acceptor. CC -!- Involved in the accumulation of the tetrasaccharides lychnose and CC isolychnose in the leaves of cerastium arvense and other plants of CC the family caryophyllaceae during late autumn. // ID 2.4.1.167 DE Sucrose 6(F)-alpha-galactosyltransferase. CA UDP-galactose + sucrose = UDP + 6(F)-alpha-D-galactosylsucrose. CC -!- Involved in the synthesis of the trisaccharide planteose and higher CC analogs in the seeds of Plantago and Sesamum species. // ID 2.4.1.168 DE Xyloglucan 4-glucosyltransferase. CA Transfers a beta-D-glucosyl residue from UDP-glucose on to a glucose CA residue in xyloglucan, forming a beta-1,4-D-glucosyl-D-glucose linkage. CC -!- In association with EC 2.4.1.169, brings about the synthesis of CC xyloglucan. CC -!- Concurrent transfers of glucose and xylose are essential for this CC synthesis. CC -!- Not identical with EC 2.4.1.12. // ID 2.4.1.169 DE Xyloglucan 6-xylosyltransferase. CA Transfers an alpha-D-xylosyl residue from UDP-D-xylose to a glucose CA residue in xyloglucan, forming an alpha-1,6-D-xylosyl-D-glucose linkage. CC -!- In association with EC 2.4.1.168, brings about the synthesis of CC xyloglucan. CC -!- Concurrent transfers of glucose and xylose are necessary for this CC synthesis. // ID 2.4.1.170 DE Isoflavone 7-O-glucosyltransferase. CA UDP-glucose + isoflavone = UDP + isoflavone 7-O-beta-D-glucoside. CC -!- The 4'-methoxy isoflavones biochanin A and formononetin and, more CC slowly, the 4'-hydroxy isoflavones geneistein and daidzein, can act CC as acceptors. CC -!- Does not act on isoflavonones, flavones, flavonones, flavonols or CC coumarins. // ID 2.4.1.171 DE Methyl-ONN-azoxymethanol glucosyltransferase. AN Cycasin synthase. CA UDP-glucose + CH(3)-N(O)=N-CH(2)OH = UDP + cycasin. CC -!- Brings about the biosynthesis of the toxic substance cycasin in the CC leaves of japanese cycad, Cycas revoluta. // ID 2.4.1.172 DE Salicyl-alcohol glucosyltransferase. CA UDP-glucose + salicyl alcohol = UDP + salicin. // ID 2.4.1.173 DE Sterol glucosyltransferase. CA UDP-glucose + a sterol = UDP + an O-glucosylsterol. CC -!- Not identical with EC 2.4.1.192 or EC 2.4.1.193. // ID 2.4.1.174 DE Glucuronylgalactosylproteoglycan 4-beta-N- DE acetylgalactosaminyltransferase. AN N-acetylgalactosaminyltransferase I. AN Glucuronylgalactosylproteoglycan beta-1,4-N- AN acetylgalactosaminyltransferase. AN Uridine diphosphoacetylgalactosamine-chondroitin AN acetylgalactosaminyltransferase I. CA UDP-N-acetyl-D-galactosamine + beta-D-glucuronyl-1,3-D-galactosyl- CA proteoglycan = UDP + N-acetyl-D-galactosaminyl-1,4-beta-D- CA glucuronyl-1,3-beta-D-galactosylproteoglycan. CC -!- Involved in the biosynthesis of chondroitin sulfate. CC -!- Key enzyme activity for the initiation of chondroitin and dermatan CC sulfates, transferring GalNAc to the GlcA-Gal-Gal-Xyl-Ser core. // ID 2.4.1.175 DE Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N- DE acetylgalactosaminyltransferase. AN N-acetylgalactosaminyltransferase II. AN UDP-N-acetyl-D-galactosamine:D-glucuronyl-N-acetyl-1,3-beta-D- AN galactosaminylproteoglycan beta-1,4-N-acetylgalactosaminyltransferase. AN Chondroitin synthase. AN Glucuronyl-N-acetylgalactosaminylproteoglycan beta-1,4-N- AN acetylgalactosaminyltransferase. AN Uridine diphosphoacetylgalactosamine-chondroitin AN acetylgalactosaminyltransferase II. CA UDP-N-acetyl-D-galactosamine + beta-D-glucuronosyl-(1->3)-N-acetyl- CA beta-D-galactosaminyl-proteoglycan = UDP + N-acetyl-beta-D- CA galactosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D- CA galactosaminyl-proteoglycan. CC -!- Involved in the biosynthesis of chondroitin sulfate. CC -!- The human form of this enzyme is a bifunctional glycosyltransferase, CC which also has the EC 2.4.1.226 activity required for the synthesis CC of the chondroitin sulfate disaccharide repeats. CC -!- Similar chondroitin synthase co-polymerases can be found in CC Pasteurella multocida and Escherichia coli. // ID 2.4.1.176 DE Gibberellin beta-glucosyltransferase. CA UDP-glucose + gibberellin = UDP + gibberellin 2-O-beta-D-glucoside. CC -!- Acts on the plant hormone gibberellin ga(3) and closely related CC compounds. // ID 2.4.1.177 DE Cinnamate glucosyltransferase. CA UDP-glucose + trans-cinnamate = UDP + trans-cinnamoyl-beta-D-glucose. CC -!- 4-coumarate, 2-coumarate, benzoate, feruloate and caffeate can also CC act as acceptors, more slowly. CC -!- Involved in the biosynthesis of chlorogenic acid in the root of the CC sweet potato. // ID 2.4.1.178 DE Hydroxymandelonitrile glucosyltransferase. AN Cyanohydrin glucosyltransferase. CA UDP-glucose + 4-hydroxymandelonitrile = UDP + taxiphyllin. CC -!- 3,4-dihydroxymandelonitrile can also act as acceptor. // ID 2.4.1.179 DE Lactosylceramide beta-1,3-galactosyltransferase. CA UDP-galactose + D-galactosyl-1,4-beta-D-glucosyl-R = UDP + CA D-galactosyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosyl-R. CC -!- R may be an oligosaccharide or a glycolipid. CC -!- Lactose can also act as acceptor, more slowly. CC -!- Involved in the elongation of oligosaccharide chains, especially in CC glycolipids. // ID 2.4.1.180 DE Lipopolysaccharide N-acetylmannosaminouronosyltransferase. CA UDP-N-acetylmannosaminouronate + lipopolysaccharide = UDP + N-acetyl- CA beta-D-mannosaminouronosyl-1,4-lipopolysaccharide. CC -!- Involved in the biosynthesis of common antigen in Enterobacteriaceae. // ID 2.4.1.181 DE Hydroxyanthraquinone glucosyltransferase. CA UDP-glucose + a hydroxyanthraquinone = UDP + a glucosyloxyanthraquinone. CC -!- A range of anthraquinones and some flavones can act as acceptors; CC best substrates are emodin, anthrapurpurin, quinizarin, CC 2,6-dihydroanthraquinone and 1,8-dihydroxianthraquinone. // ID 2.4.1.182 DE Lipid-A-disaccharide synthase. CA UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + 2,3-bis(3- CA hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate = UDP + CA 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D-2,3-bis(3- CA hydroxytetradecanoyl)-beta-D-glucosaminyl 1-phosphate. CC -!- Involved with EC 2.3.1.129 and EC 2.7.1.130 in the biosynthesis of CC the phosphorylated glycolipid, lipid A, in the outer membrane of CC E.coli. DR O67420, LPXB_AQUAE; Q9PIK8, LPXB_CAMJE; Q9PJY4, LPXB_CHLMU; DR Q9Z6U3, LPXB_CHLPN; O84416, LPXB_CHLTR; Q8X8X7, LPXB_ECO57; DR P10441, LPXB_ECOLI; P45011, LPXB_HAEIN; Q9ZKY2, LPXB_HELPJ; DR O25537, LPXB_HELPY; Q9JX45, LPXB_NEIMA; Q9K1F5, LPXB_NEIMB; DR Q9CJK7, LPXB_PASMU; P72216, LPXB_PROMI; Q9HXY8, LPXB_PSEAE; DR Q92II0, LPXB_RICCN; Q9ZDK7, LPXB_RICPR; Q8Z9A1, LPXB_SALTI; DR Q8ZRN9, LPXB_SALTY; Q57310, LPXB_SYNY3; Q9KPW5, LPXB_VIBCH; DR Q87MF0, LPXB_VIBPA; Q8DBE8, LPXB_VIBVU; Q8D2H4, LPXB_WIGBR; DR Q8PML8, LPXB_XANAC; Q8PAW6, LPXB_XANCP; Q9PEI6, LPXB_XYLFA; DR Q87EI5, LPXB_XYLFT; Q8ZH55, LPXB_YERPE; // ID 2.4.1.183 DE Alpha-1,3-glucan synthase. CA UDP-glucose + {alpha-D-glucosyl-(1,3)}(N) = UDP + {alpha-D-glucosyl- CA (1,3)}(N+1). CC -!- A glucan primer is needed to begin the reaction, which brings CC about the elongation of the glucan chains. DR Q9USK8, MOK1_SCHPO; Q09854, MOKB_SCHPO; Q9UUL4, MOKC_SCHPO; DR Q9Y719, MOKD_SCHPO; Q9Y704, MOKE_SCHPO; // ID 2.4.1.184 DE Galactolipid galactosyltransferase. AN Galactolipid:galactolipid galactosyltransferase. CA 2 mono-beta-D-galactosyldiacylglycerol = alpha-D-galactosyl-beta-D- CA galactosyldiacylglycerol + diacylglycerol. CC -!- By further transfers of galactosyl residues to the digalactosyl- CC diacylglycerol, trigalactosyldiacylglycerol and tetragalactosyl- CC diacylglycerol are also formed. // ID 2.4.1.185 DE Flavonone 7-O-beta-glucosyltransferase. CA UDP-glucose + a flavonone = UDP + a flavonone 7-O-beta-D-glucoside. CC -!- Naringenin and hesperetin can act as acceptors. CC -!- No action on flavones or flavonols. // ID 2.4.1.186 DE Glycogenin glucosyltransferase. AN Glycogenin. CA UDP-glucose + glycogenin = UDP + glucosylglycogenin. CC -!- The glycogenin subunit of EC 2.4.1.11 catalyzes this reaction, i.e. CC the enzyme catalyzes its own autoglucosylation. CC -!- Five molecules of glucose can be transferred to one molecule of CC glycogenin. CC -!- The product acts as a primer for the reaction catalyzed by glycogen CC synthase. DR P46976, GLYG_HUMAN; Q9R062, GLYG_MOUSE; P13280, GLYG_RABIT; DR O08730, GLYG_RAT ; O15488, GYG2_HUMAN; // ID 2.4.1.187 DE N-acetylglucosaminyldiphosphoundecaprenol N-acetyl-beta-D- DE mannosaminyltransferase. CA UDP-N-acetyl-D-mannosamine + N-acetyl-D-glucosaminyldiphospho- CA undecaprenol = UDP + N-acetyl-beta-D-mannosaminyl-1,4-N-acetyl- CA D-glucosaminyldiphosphoundecaprenol. CC -!- Involved in the biosynthesis of teichoic acid linkage units in CC bacterial cell walls. DR P27620, TAGA_BACSU; Q8RKI7, TARA_BACSU; // ID 2.4.1.188 DE N-acetylglucosaminyldiphosphoundecaprenol glucosyltransferase. CA UDP-glucose + N-acetyl-D-glucosaminyldiphosphoundecaprenol = UDP + CA beta-D-glucosyl-1,4-N-acetyl-D-glucosaminyldiphosphoundecaprenol. // ID 2.4.1.189 DE Luteolin 7-O-glucoronosyltransferase. CA UDP-glucuronate + luteolin = UDP + luteolin 7-O-beta-D-glucuronide. // ID 2.4.1.190 DE Luteolin-7-O-glucuronide 7-O-glucuronosyltransferase. CA UDP-glucuronate + luteolin 7-O-glucuronide = UDP + luteolin 7-O-beta-D- CA diglucuronide. // ID 2.4.1.191 DE Luteolin-7-O-diglucuronide 4'-O-glucuronosyltransferase. CA UDP-glucuronate + luteolin 7-O-beta-D-glucuronide = UDP + luteolin CA 7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide]-4'-O-beta-D- CA glucuronide. // ID 2.4.1.192 DE Nuatigenin 3-beta-glucosyltransferase. CA UDP-glucose + (20S,22S,25S)-22,25-epoxyfurost-5-ene-3-beta,26-diol = CA UDP + (20S,22S,25S)-22,25-epoxyfurost-5-ene-3-beta,26-diol 3-O-beta-D- CA glucoside. CC -!- Some other sapogenins can act as glucosyl acceptors. CC -!- Involved in the biosynthesis of plant saponins. CC -!- Not identical with EC 2.4.1.173 or EC 2.4.1.193. // ID 2.4.1.193 DE Sarsapogenin 3-beta-glucosyltransferase. CA UDP-glucose + (25S)-5-beta-spirostan-3-beta-ol = UDP + (25S)-5-beta- CA spirostan-3-beta-ol 3-O-beta-D-glucoside. CC -!- Specific to 5-beta-spirostanols. CC -!- Involved in the biosynthesis of plant saponins. CC -!- Not identical with EC 2.4.1.173 or EC 2.4.1.192. // ID 2.4.1.194 DE 4-hydroxybenzoate 4-O-beta-D-glucosyltransferase. CA UDP-glucose + 4-hydroxybenzoate = UDP + 4-(beta-D-glucosyloxy)benzoate. // ID 2.4.1.195 DE Thiohydroximate beta-D-glucosyltransferase. CA UDP-glucose + phenylthioacetohydroximate = UDP + desulfoglucotropeolin. CC -!- Involved with EC 2.8.2.24 in the biosynthesis of thioglucosides in CC cruciferous plants. // ID 2.4.1.196 DE Nicotinate glucosyltransferase. CA UDP-glucose + nicotinate = UDP + N-glucosylnicotinate. // ID 2.4.1.197 DE High-mannose-oligosaccharide beta-1,4-N-acetyl-glucosaminyltransferase. CA Transfers an N-acetyl-D-glucosamine residue from UDP-N-acetyl- CA D-glucosamine to the 4-position of a mannose linked alpha-1,6 to the CA core mannose of high-mannose oligosaccharides produced by Dictyostelium CA discoideum. CC -!- The activity of the intersecting mannose residue as acceptor is CC dependent on two other mannose residues attached by alpha-1,3 and CC alpha-1,6 links. // ID 2.4.1.198 DE Phosphatidylinositol N-acetylglucosaminyltransferase. AN UDP-N-acetyl-D-glucosamine:phosphatidylinositol. AN N-acetyl-D-glucosaminyltransferase. AN Uridine diphosphoacetylglucosamine alpha-1,6-acetyl-D- AN glucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + CA 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol. CC -!- Involved in the first step of glycosylphosphatidylinositol (GPI) CC anchor formation in all eukaryotes. CC -!- In mammalian cells, the enzyme is composed of at least five subunits CC (PIG-A, PIG-H, PIG-C, GPI1 and PIG-P). CC -!- PIG-A subunit is the catalytic subunit. CC -!- In some species, the long-chain acyl groups of the phosphatidyl CC group are partly replaced by long-chain alkyl or alk-1-enyl groups. DI Paroxysmal nocturnal hemoglobinuria; MIM:311770. DR P53306, GPI1_YEAST; P46961, GPI2_YEAST; P32363, GPI3_YEAST; DR P37287, PIGA_HUMAN; Q92535, PIGC_HUMAN; Q14442, PIGH_HUMAN; DR P57054, PIGP_HUMAN; Q9BRB3, PIGQ_HUMAN; Q9QYT7, PIGQ_MOUSE; // ID 2.4.1.199 DE Beta-mannosylphosphodecaprenol-mannooligosaccharide DE 6-mannosyltransferase. CA Beta-D-mannosylphosphodecaprenol + 1,6-alpha-D-mannosyloligosaccharide = CA decaprenol phosphate + 1,6-alpha-D-mannosyl-1,6-alpha-D-mannosyl- CA oligosaccharide. CC -!- Involved in the formation of mannooligosaccharides in the membrane CC of Mycobacterium smegmatis. // ID 2.4.1.200 DE Inulin fructotransferase (depolymerizing, difructofuranose- DE 1,2':2',1-dianhydride-forming). AN Inulin fructotransferase (DFA-I-producing). CA Removes successive terminal D-fructosyl-D fructofuranosyl groups from CA inulin as the cyclic 1,2':2',1-dianhydride, leaving a residual tetra- CA or pentasaccharide. CC -!- Cf. EC 2.4.1.93. DR P19870, INU2_ARTGO; // ID 2.4.1.201 DE Alpha-1,6-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase. AN N-acetylglucosaminyltransferase VI. AN N-glycosyl-oligosaccharide-glycoprotein N- AN acetylglucosaminyltransferase VI. AN Uridine diphosphoacetylglucosamine-glycopeptide beta-1->4- AN acetylglucosaminyltransferase VI. AN Mannosyl-glycoprotein beta-1,4-N-acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + 2,6-bis(N-acetyl-beta-D-glucosaminyl)- CA alpha-D-mannosyl-R = UDP + 2,4,6-tris(N-acetyl-beta-D-glucosaminyl)- CA alpha-D-mannosyl-R. CC -!- R represents the remainder of the N-linked oligosaccharide in the CC glycoprotein acceptor. // ID 2.4.1.202 DE 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one DE 2-D-glucosyltransferase. CA UDP-glucose + 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one = CA UDP + 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucoside. // ID 2.4.1.203 DE Trans-zeatin O-beta-D-glucosyltransferase. AN Zeatin O-beta-D-glucosyltransferase. AN Uridine diphosphoglucose-zeatin O-glucosyltransferase. AN Zeatin O-glucosyltransferase. CA UDP-glucose + trans-zeatin = UDP + O-beta-D-glucosyl-trans-zeatin. CC -!- Unlike EC 2.4.1.215, UDP-xylose can also act as donor (cf. CC EC 2.4.1.204). DR Q9ZSK5, ZOG_PHALU ; // ID 2.4.1.204 DE Zeatin O-beta-D-xylosyltransferase. AN Zeatin O-xylosyltransferase. CA UDP-D-xylose + zeatin = UDP + O-beta-D-xylosylzeatin. CC -!- Does not act on UDP-glucose (cf. EC 2.4.1.103). DR P56725, ZOX_PHAVU ; // ID 2.4.1.205 DE Galactogen 6-beta-galactosyltransferase. AN 1,6-D-galactosyltransferase. CA UDP-galactose + galactogen = UDP + 1,6-beta-D-galactosylgalactogen. CC -!- Galactogen from Helix pomatia is the most effective acceptor. // ID 2.4.1.206 DE Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyl-transferase. CA UDP-N-acetyl-D-glucosamine + D-galactosyl-1,4-beta-D-glucosylceramide = CA UDP + N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D- CA glucosylceramide. // ID 2.4.1.207 DE Xyloglucan:xyloglucosyl transferase. AN Xyloglucan endotransglycosylase. AN Endo-xyloglucan transferase. CA Breaks a beta-(1->4) bond in the backbone of a xyloglucan and transfers CA the xyloglucanyl segment on to O-4 of the non-reducing terminal glucose CA residue of an acceptor, which can be a xyloglucan or an oligosaccharide CA of xyloglucan. CC -!- Does not use cello-oligosaccharides as either donor or acceptor. // ID 2.4.1.208 DE Diglucosyl diacylglycerol (DGlcDAG) synthase. AN Monoglucosyl diacylglycerol (1->2) glucosyltransferase. AN MGlcDAG (1->2) glucosyltransferase. AN DGlcDAG synthase. CA UDP-glucose + 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol = 1,2- CA diacyl-3-O-(alpha-D-glucopyranosyl(1->2)-O-alpha-D-glucopyranosyl)sn- CA glycerol + UDP. CF Magnesium. // ID 2.4.1.209 DE Cis-p-coumarate glucosyltransferase. CA UDP-glucose + cis-p-coumarate = 4'-O-beta-D-glucosyl-cis-p-coumarate CA + UDP. CC -!- Cis-caffeic acid also serves as a glucosyl acceptor with the CC enzyme from Sphagnum fallax kinggr. CC -!- The corresponding trans-isomers are not substrates. // ID 2.4.1.210 DE Limonoid glucosyltransferase. AN Limonoid UDP-glucosyltransferase. AN LGTase. CA UDP-glucose + limonin = glucosyl-limonin + UDP. CC -!- The enzyme purified from navel orange albedo tissue also acts on CC the related tetranortriterpenoid nomilin. PR PROSITE; PDOC00359; DR Q9MB73, LGT_CITUN ; // ID 2.4.1.211 DE 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase. CA Beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine + phosphate = CA alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine. CC -!- Reaction also occurs with beta-D-galactopyranosyl-(1->3)-N-acetyl- CC D-galactosamine as the substrate, giving N-acetyl-D-galactosamine CC as the product. // ID 2.4.1.212 DE Hyaluronan synthase. CA N UDP-N-acetyl-D-glucosamine + n UDP-D-glucuronate = [beta-N-acetyl- CA D-glucosaminyl(1->4)beta-D-glucuronosyl(1->3)](n)+ 2n UDP. CF Magnesium. CC -!- The enzyme is highly specific for UDP-GlcNAc and UDP-GlcA. CC -!- No copolymerization is observed if either is replaced by CC UDP-Glc, UDP-Gal, UDP-GalNAc or UDP-GalA. CC -!- Similar enzymes have been found in a variety of organisms. DR Q92839, HAS1_HUMAN; Q61647, HAS1_MOUSE; P13563, HAS1_XENLA; DR O97711, HAS2_BOVIN; O57424, HAS2_CHICK; Q92819, HAS2_HUMAN; DR P70312, HAS2_MOUSE; O35776, HAS2_RAT ; O57427, HAS2_XENLA; DR O57425, HAS3_CHICK; O00219, HAS3_HUMAN; O08650, HAS3_MOUSE; DR O57426, HAS3_XENLA; Q54865, HASA_STRPY; // ID 2.4.1.213 DE Glucosylglycerol-phosphate synthase. AN Glucosyl-glycerol-phosphate synthase. AN GG-phosphate synthase. AN GGPS. CA ADP-glucose + sn-glycerol 3-phosphate = 2-(beta-D-glucosyl)-sn-glycerol CA 3-phosphate + ADP. CC -!- Acts with EC 3.1.3.69 to form glucosylglycerol, an osmolyte that CC endows cyanobacteria with resistance to salt. DR Q93JY3, GGPS_PSEAG; O65979, GGPS_SYNP2; P74258, GGPS_SYNY3; // ID 2.4.1.214 DE Glycoprotein 3-alpha-L-fucosyltransferase. AN GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha 1,3-fucosyltransferase. AN GDP-L-Fuc:Asn-linked GlcNAc alpha-1,3-fucosyltransferase. AN GDP-fucose:beta-N-acetylglucosamine (Fuc to (Fuc-alpha-1->6-GlcNAc)- AN Asn-peptide) alpha-1->3-fucosyltransferase. CA GDP-L-fucose + N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D- CA mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl- CA (1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N- CA acetyl-beta-D-glucosaminyl}asparagine = GDP + N(4)-{N-acetyl-beta-D- CA glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D- CA glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-beta-D-mannosyl-(1->4)-N- CA acetyl-beta-D-glucosaminyl-(1->4)-[alpha-L-fucosyl-(1->3)]-N-acetyl- CA beta-D-glucosaminyl}asparagine. CF Manganese. CC -!- The enzyme transfers to N-linked oligosaccharide structures CC (N-glycans), generally with a specificity for N-glycans with one CC unsubstituted non-reducing terminal GlcNAc residue. CC -!- This enzyme catalyzes a reaction similar to that of EC 2.4.1.68, CC but transferring the L-fucosyl group from GDP-beta-L-fucose to CC form an alpha-1,3-linkage rather than an alpha-1,6-linkage. CC -!- The N-glycan products of this enzyme are present in plants, CC insects and some other invertebrates (e.g., Schistosoma, CC Haemonchus, Lymnaea). DR Q9LJK1, FU11_ARATH; Q9VUL9, FUTA_DROME; // ID 2.4.1.215 DE Cis-zeatin O-beta-D-glucosyltransferase. CA UDPglucose + cis-zeatin = UDP + O-beta-D-glucosyl-cis-zeatin. CC -!- The enzyme from maize can use cis-zeatin and UDPglucose as CC substrates, but not cis-ribosylzeatin, trans-zeatin or trans- CC ribosylzeatin. CC -!- Unlike EC 2.4.1.203 UDPxylose cannot act as a donor. // ID 2.4.1.216 DE Trehalose 6-phosphate phosphorylase. CA Trehalose 6-phosphate + phosphate = glucose 6-phosphate + CA beta-D-glucose 1-phosphate. CC -!- The enzyme from Lactococcus lactis is specific for trehalose CC 6-phosphate. CC -!- Differs from EC 2.4.1.64 in that trehalose is not a substrate. // ID 2.4.1.217 DE Mannosyl-3-phosphoglycerate synthase. AN MPG synthase. CA GDP-mannose + 3-phospho-D-glycerate = GDP + 2-(alpha-D-mannosyl)-3- CA phosphoglycerate. CF Magnesium. CC -!- The enzyme is absolutely specific for GDP-mannose and 3- CC phosphoglycerate, and transfers the mannosyl group with retention CC of configuration. CC -!- In the hyperthermophilic archaeon Pyrococcus horikoshii, the CC mannosyl-3-phosphoglycerate formed is subsequently dephosphorylated CC by a specific phosphatase, EC 3.1.3.70, producing mannosylglycerate. DR Q9YDM5, MPGS_AERPE; Q9UZC1, MPGS_PYRAB; Q8U380, MPGS_PYRFU; DR O58689, MPGS_PYRHO; // ID 2.4.1.218 DE Hydroquinone glucosyltransferase. AN Arbutin synthase. AN Hydroquinone:O-glucosyltransferase. CA UDP-glucose + hydroquinone = UDP + hydroquinone-O-beta-D- CA glucopyranoside. CC -!- Hydroquinone is the most effective acceptor, but over 40 phenolic CC compounds are also glucosylated, but at lower rates. DR Q9M156, HQGT_ARATH; Q9AR73, HQGT_RAUSE; // ID 2.4.1.219 DE Vomilenine glucosyltransferase. AN UDPG:vomilenine 21-beta-D-glucosyltransferase. CA UDP-glucose + vomilenine = UDP + raucaffricine. CC -!- The indole alkaloid raucaffricine accumulates during the culture CC of Rauvolfia cell suspensions. // ID 2.4.1.220 DE Indoxyl-UDPG glucosyltransferase. AN Indoxyl-UDPG-glucosyltransferase. CA UDP-glucose + indoxyl = UDP + indican. CC -!- Also acts to a limited extent on 4-, 5-, 6- and 7-hydroxyindole. CC -!- After enzymic or chemical hydrolysis, indican forms indoxyl, which, CC in turn, is converted in the presence of oxygen to the dye indigo. // ID 2.4.1.221 DE Peptide-O-fucosyltransferase. AN GDP-L-fucose:polypeptide fucosyltransferase. AN GDP-fucose protein O-fucosyltransferase. AN GDP-fucose:polypeptide fucosyltransferase. CA Transfers an alpha-L-fucosyl residue from GDP-beta-L-fucose to the CA serine hydroxy group of a protein acceptor. CC -!- Involved in the biosynthesis of O-fucosylated epidermal growth CC factor (EGF) and thrombospondin type 1 repeats. CC -!- The attachment of O-linked fucose to serine or threonine occurs on CC EGF domains within the sequence Cys-Xaa-Xaa-Gly-Gly-Ser/Thr-Cys. DR Q18014, OFU1_CAEEL; Q9V6X7, OFU1_DROME; Q9H488, OFU1_HUMAN; DR Q91ZW2, OFU1_MOUSE; // ID 2.4.1.222 DE O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase. AN O-fucosylpeptide beta-1,3-N-acetylglucosaminyltransferase. CA Transfers a beta-D-GlcNAc residue from UDP-D-GlcNAc to the fucose CA residue of a fucosylated protein acceptor. CC -!- O-Fucosylpeptide 3-beta-N-acetylglucosaminyltransferases are the CC products of fringe genes. CC -!- O-linked fucose is an unusual form of glycosylation where the fucose CC is attached directly to proteins through the hydroxy groups of Ser CC or Thr residues. DR Q24342, FNG_DROME ; Q8JHF2, LFNG_BRARE; O12971, LFNG_CHICK; DR Q8NES3, LFNG_HUMAN; O09010, LFNG_MOUSE; Q924T4, LFNG_RAT ; DR P79948, LFNG_XENLA; O00587, MFNG_HUMAN; O09008, MFNG_MOUSE; DR O12972, RFNG_CHICK; Q9Y644, RFNG_HUMAN; O09009, RFNG_MOUSE; DR Q9YHB3, RFNG_NOTVI; Q9R1U9, RFNG_RAT ; P79949, RFNG_XENLA; // ID 2.4.1.223 DE Glucuronyl-galactosyl-proteoglycan 4-alpha-N- DE acetylglucosaminyltransferase. AN Alpha-N-acetylglucosaminyltransferase I. AN Alpha-1,4-N-acetylglucosaminyltransferase. AN Glucuronosylgalactosyl-proteoglycan 4-alpha-N- AN acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-beta-D- CA galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl-proteoglycan CA = UDP + alpha-N-acetyl-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)- CA beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl- CA proteoglycan. CC -!- Enzyme involved in the initiation of heparin and heparan sulfate CC synthesis, transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core. CC -!- Apparently products of both the human EXTL2 and EXTL3 genes can CC catalyze this reaction. CC -!- In Caenorhabditis elegans, the product of the rib-2 gene displays CC this activity as well as that of EC 2.4.1.224. DR Q9UBQ6, EXL2_HUMAN; Q9ES89, EXL2_MOUSE; O43909, EXL3_HUMAN; DR O01705, EXT2_CAEEL; // ID 2.4.1.224 DE Glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N- DE acetylglucosaminyltransferase. AN Alpha-N-acetylglucosaminyltransferase II glucuronyl-N- AN acetylglucosaminylproteoglycan alpha-1,4-N-acetylglucosaminyltransferase. CA UDP-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->4)-N-acetyl-alpha- CA D-glucosaminyl-proteoglycan = UDP + N-acetyl-alpha-D-glucosaminyl-(1->4)- CA beta-D-glucuronosyl-(1->4)-N-acetyl-alpha-D-glucosaminyl-proteoglycan. CC -!- Involved in the biosynthesis of heparin and heparan sulfate. CC -!- Some forms of the enzyme from human (particularly the enzyme complex CC encoded by the EXT1 and EXT2 genes) act as bifunctional CC glycosyltransferases, which also have the EC 2.4.1.225 activity CC required for the synthesis of the heparan sulfate disaccharide CC repeats. CC -!- Other human forms of this enzyme (e.g. the product of the EXTL1 gene) CC have only the 4-alpha-N-acetylglucosaminyltransferase activity. CC -!- In Caenorhabditis elegans, the product of the rib-2 gene displays CC the activities of this enzyme as well as EC 2.4.1.223. DR Q92935, EXL1_HUMAN; Q9JKV7, EXL1_MOUSE; Q16394, EXT1_HUMAN; DR P97464, EXT1_MOUSE; O77783, EXT2_BOVIN; O01705, EXT2_CAEEL; DR Q93063, EXT2_HUMAN; P70428, EXT2_MOUSE; // ID 2.4.1.225 DE N-acetylglucosaminyl-proteoglycan 4-beta-glucuronosyltransferase. AN N-acetylglucosaminylproteoglycan beta-1,4-glucuronyltransferase heparan AN glucuronyltransferase II. CA UDP-alpha-D-glucuronate + N-acetyl-alpha-D-glucosaminyl-(1->4)-beta-D- CA glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->4)-N-acetyl- CA alpha-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan. CC -!- Involved in the biosynthesis of heparin and heparan sulfate. CC -!- Some forms of the human enzyme (particularly the enzyme complex CC encoded by the EXT1 and EXT2 genes) act as bifunctional CC glycosyltransferases, which also have the EC 2.4.1.244 activity CC required for the synthesis of the heparan sulfate disaccharide CC repeats. DR Q16394, EXT1_HUMAN; P97464, EXT1_MOUSE; O77783, EXT2_BOVIN; DR Q93063, EXT2_HUMAN; P70428, EXT2_MOUSE; // ID 2.4.1.226 DE N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase. AN Chondroitin glucuronyltransferase II. CA UDP-alpha-D-glucuronate + N-acetyl-beta-D-galactosaminyl-(1->4)-beta- CA D-glucuronosyl-proteoglycan = UDP + beta-D-glucuronosyl-(1->3)-N-acetyl- CA beta-D-galactosaminyl-(1->4)-beta-D-glucuronosyl-proteoglycan. CC -!- Involved in the biosynthesis of chondroitin and dermatan sulfate. CC -!- The human chondroitin synthetase is a bifunctional CC glycosyltransferase, which also has the EC 2.4.1.175 activity CC required for the synthesis of the chondroitin sulfate disaccharide CC repeats. CC -!- Similar chondroitin synthase 'co-polymerases' can be found in CC Pasteurella multocida and Escherichia coli. CC -!- There is also another human protein with apparently only the 3-beta- CC glucuronosyltransferase activity. // ID 2.4.1.227 DE Undecaprenyldiphospho-muramoylpentapeptide beta-N- DE acetylglucosaminyltransferase. AN MurG transferase. AN UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl- AN undecaprenol N-acetylglucosamine transferase. AN Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase. CA UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D- CA Ala)-diphosphoundecaprenol = UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma- CA D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. CC -!- The enzyme also works when the lysine residue is replaced by meso- CC 2,6-diaminoheptanedioate (meso-2,6-diaminopimelate, A2pm) combined CC with adjacent residues through its L-centre, as it is in Gram- CC negative and some Gram-positive organisms. CC -!- The undecaprenol involved is ditrans,octacis-undecaprenol. DR Q8UDM8, MURG_AGRT5; Q8YZI3, MURG_ANASP; O67238, MURG_AQUAE; DR Q9K9T0, MURG_BACHD; P37585, MURG_BACSU; O51708, MURG_BORBU; DR Q8YI66, MURG_BRUME; P57311, MURG_BUCAI; Q8K9T4, MURG_BUCAP; DR P59424, MURG_BUCBP; Q9PNQ2, MURG_CAMJE; Q9A5A1, MURG_CAUCR; DR Q9PLG2, MURG_CHLMU; Q9Z702, MURG_CHLPN; Q8KGD4, MURG_CHLTE; DR O84766, MURG_CHLTR; Q97GY4, MURG_CLOAB; Q8XIQ1, MURG_CLOPE; DR Q8NNN5, MURG_CORGL; Q8X9Y8, MURG_ECO57; Q8FL64, MURG_ECOL6; DR P17443, MURG_ECOLI; O07109, MURG_ENTFA; O07670, MURG_ENTHR; DR P45065, MURG_HAEIN; Q9ZK59, MURG_HELPJ; O25770, MURG_HELPY; DR Q9CF92, MURG_LACLA; Q929Y2, MURG_LISIN; Q8Y5M2, MURG_LISMO; DR O69552, MURG_MYCLE; O06224, MURG_MYCTU; Q9JSZ7, MURG_NEIMA; DR Q9K0Y2, MURG_NEIMB; P57817, MURG_PASMU; Q9HW01, MURG_PSEAE; DR Q8XVI7, MURG_RALSO; Q98KB3, MURG_RHILO; Q92NL9, MURG_RHIME; DR Q92I58, MURG_RICCN; Q9ZDC0, MURG_RICPR; Q8Z9G9, MURG_SALTI; DR Q8ZRU3, MURG_SALTY; Q9F1N0, MURG_SHEVI; Q99U69, MURG_STAAM; DR Q8NWR4, MURG_STAAW; Q9ZBA5, MURG_STRCO; Q9X4H4, MURG_STRCU; DR Q8K6R7, MURG_STRP3; Q9ZHA9, MURG_STRPN; Q99YV4, MURG_STRPY; DR P74657, MURG_SYNY3; Q9WY74, MURG_THEMA; Q8R9G6, MURG_THETN; DR O83535, MURG_TREPA; Q9KPG7, MURG_VIBCH; Q87SG4, MURG_VIBPA; DR Q8DEL0, MURG_VIBVU; Q8D2Z6, MURG_WIGBR; Q8PPA8, MURG_XANAC; DR Q8PCK0, MURG_XANCP; Q9PF81, MURG_XYLFA; Q87AF9, MURG_XYLFT; DR Q8ZIE9, MURG_YERPE; Q9RNM6, MURG_ZYMMO; // ID 2.4.1.228 DE Lactosylceramide 4-alpha-galactosyltransferase. AN Gal-beta-1-4Glc-beta-1-Cer alpha-1,4-galactosyltransferase. AN Globotriaosylceramide/CD77 synthase. AN Histo-blood group Pk UDP-galactose. CA UDP-galactose + beta-D-galactosyl-(1->4)-D-glucosylceramide = UDP + CA alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-D-glucosylceramide. DR Q9N290, A4GT_GORGO; Q9NPC4, A4GT_HUMAN; Q9N291, A4GT_PANTR; DR Q9N289, A4GT_PONPY; // ID 2.4.2.1 DE Purine-nucleoside phosphorylase. AN Inosine phosphorylase. AN PNPase. CA Purine nucleoside + phosphate = purine + alpha-D-ribose CA 1-phosphate. CC -!- Specificity not completely determined. Can also catalyze CC ribosyltransferase reactions of the type catalyzed by EC 2.4.2.5. DI T-cell immunodeficiency with neurologic disorder; MIM:164050. PR PROSITE; PDOC00946; PR PROSITE; PDOC00954; DR P94164, DEOD_ACTPL; P77835, DEOD_BACST; O34925, DEOD_BACSU; DR P57606, DEOD_BUCAI; Q8K937, DEOD_BUCAP; P09743, DEOD_ECOLI; DR P44417, DEOD_HAEIN; Q9ZK38, DEOD_HELPJ; P56463, DEOD_HELPY; DR Q59482, DEOD_KLEPN; Q9CH10, DEOD_LACLA; O32810, DEOD_LACLC; DR P47295, DEOD_MYCGE; P47724, DEOD_MYCPI; P75053, DEOD_MYCPN; DR Q56037, DEOD_STRTR; O83716, DEOD_TREPA; P55859, PNPH_BOVIN; DR P00491, PNPH_HUMAN; P23492, PNPH_MOUSE; Q05788, PNPH_YEAST; DR P77834, PUNA_BACST; P46354, PUNA_BACSU; P81989, PUNA_CELSP; DR P46862, PUNA_MYCLE; O53359, PUNA_MYCTU; // ID 2.4.2.2 DE Pyrimidine-nucleoside phosphorylase. CA Pyrimidine nucleoside + phosphate = pyrimidine + alpha-D-ribose CA 1-phosphate. PR PROSITE; PDOC00557; DR P77836, PDP_BACST ; P39142, PDP_BACSU ; // ID 2.4.2.3 DE Uridine phosphorylase. AN Pyrimidine phosphorylase. CA Uridine + phosphate = uracil + alpha-D-ribose 1-phosphate. PR PROSITE; PDOC00946; DR P12758, UDP_ECOLI ; P43770, UDP_HAEIN ; Q16831, UDP_HUMAN ; DR O08444, UDP_KLEAE ; P52671, UDP_KLEPN ; P19662, UDP_LACRH ; DR P52624, UDP_MOUSE ; O33808, UDP_SALTY ; O83990, UDP_TREPA ; // ID 2.4.2.4 DE Thymidine phosphorylase. AN Pyrimidine phosphorylase. CA Thymidine + phosphate = thymine + 2-deoxy-D-ribose 1-phosphate. CC -!- In some tissues also catalyzes deoxyribosyltransferase reactions of CC the type catalyzed by EC 2.4.2.6. PR PROSITE; PDOC00557; DR O53366, DEOA_MYCTU; P07650, TYPH_ECOLI; P19971, TYPH_HUMAN; DR P19663, TYPH_LACRH; Q58081, TYPH_METJA; P47297, TYPH_MYCGE; DR P43050, TYPH_MYCHO; P47717, TYPH_MYCPI; P75052, TYPH_MYCPN; // ID 2.4.2.5 DE Nucleoside ribosyltransferase. CA D-ribosyl-base(1) + base(2) = D-ribosyl-base(2) + base(1). CC -!- Base(1) and base(2) represent various purines and pyrimidines. // ID 2.4.2.6 DE Nucleoside deoxyribosyltransferase. CA 2-deoxy-D-ribosyl-base(1) + base(2) = 2-deoxy-D-ribosyl-base(2) + CA base(1). CC -!- Base(1) and base(2) represent various purines and pyrimidines. // ID 2.4.2.7 DE Adenine phosphoribosyltransferase. AN AMP pyrophosphorylase. AN AMP diphosphorylase. AN Transphosphoribosidase. AN APRT. CA AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate. CC -!- 5-amino-4-imidazolecarboxymide can replace adenine. DI Urolithiasis, 2,8-dihydroxyadenine; MIM:102600. PR PROSITE; PDOC00096; DR P31166, APT1_ARATH; Q43199, APT1_WHEAT; P49435, APT1_YEAST; DR Q42563, APT2_ARATH; P36973, APT2_YEAST; Q8UD91, APT_AGRT5 ; DR Q8YNI3, APT_ANASP ; Q9KDH2, APT_BACHD ; O34443, APT_BACSU ; DR O51718, APT_BORBU ; Q8YIG8, APT_BRUME ; O31060, APT_BUTFI ; DR P91455, APT_CAEEL ; Q9PP06, APT_CAMJE ; Q8KFM9, APT_CHLTE ; DR Q97GU0, APT_CLOAB ; Q8XJ22, APT_CLOPE ; O87330, APT_CORGL ; DR P47952, APT_CRILO ; P12426, APT_DROME ; P54363, APT_DROPS ; DR Q8XD48, APT_ECO57 ; P07672, APT_ECOLI ; Q8RDM9, APT_FUSNN ; DR Q64414, APT_GERCA ; P43856, APT_HAEIN ; Q9HRT1, APT_HALN1 ; DR Q9ZLQ9, APT_HELPJ ; O25296, APT_HELPY ; P07741, APT_HUMAN ; DR Q9CHT5, APT_LACLA ; Q925X9, APT_LISMO ; Q64427, APT_MASHI ; DR Q59049, APT_METJA ; Q8TXQ0, APT_METKA ; O27375, APT_METTH ; DR O33174, APT_METTM ; P08030, APT_MOUSE ; P47956, APT_MUSPA ; DR P47957, APT_MUSSI ; Q9RFQ2, APT_MYCFE ; P47518, APT_MYCGE ; DR P75388, APT_MYCPN ; Q98QN9, APT_MYCPU ; Q50637, APT_MYCTU ; DR Q9JT95, APT_NEIMA ; Q9JYB4, APT_NEIMB ; P57841, APT_PASMU ; DR Q04633, APT_PSEAE ; P47202, APT_PSEST ; Q8Y2B9, APT_RALSO ; DR P36972, APT_RAT ; Q9RQF8, APT_RHIGA ; Q98HV0, APT_RHILO ; DR Q92N62, APT_RHIME ; Q8Z8T4, APT_SALTI ; Q8ZRA2, APT_SALTY ; DR Q8EFG1, APT_SHEON ; O32418, APT_STAAM ; P47958, APT_STOLO ; DR Q93AJ8, APT_STRCL ; P52561, APT_STRCO ; Q8KLQ0, APT_STRGB ; DR Q97PM8, APT_STRPN ; Q9A053, APT_STRPY ; Q8DGH9, APT_SYNEL ; DR P73935, APT_SYNY3 ; Q9X1A4, APT_THEMA ; Q8RAL9, APT_THETN ; DR O84001, APT_TREPA ; Q9PQ02, APT_UREPA ; Q9KT52, APT_VIBCH ; DR Q87MQ1, APT_VIBPA ; Q8DB25, APT_VIBVU ; Q8PJY6, APT_XANAC ; DR Q8P8F9, APT_XANCP ; Q8ZC94, APT_YERPE ; // ID 2.4.2.8 DE Hypoxanthine phosphoribosyltransferase. AN Hypoxanthine-guanine phosphoribosyltransferase. AN HGPRTase. AN IMP pyrophosphorylase. AN IMP diphosphorylase. AN Transphosphoribosidase. AN Guanine phosphoribosyltransferase. CA IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose CA 1-diphosphate. CC -!- Guanine and 6-mercaptopurine can replace hypoxanthine. DI Lesch-Nyhan syndrome; MIM:308000. PR PROSITE; PDOC00096; DR O66821, HPRT_AQUAE; P37472, HPRT_BACSU; P57291, HPRT_BUCAI; DR Q8K9U8, HPRT_BUCAP; Q9W719, HPRT_CHICK; Q27541, HPRT_CRIFA; DR P00494, HPRT_CRIGR; P36766, HPRT_ECOLI; P45078, HPRT_HAEIN; DR P00492, HPRT_HUMAN; Q02522, HPRT_LACLA; P43152, HPRT_LEIDO; DR P47959, HPRT_MERUN; P00493, HPRT_MOUSE; Q64531, HPRT_MUSSP; DR P96794, HPRT_MYCAV; P47696, HPRT_MYCGE; O69537, HPRT_MYCLE; DR P75119, HPRT_MYCPN; O06383, HPRT_MYCTU; P27605, HPRT_RAT ; DR P37171, HPRT_RHOCA; O33799, HPRT_SALTY; P09383, HPRT_SCHMA; DR Q07010, HPRT_TRYBB; P18134, HPRT_VIBHA; // ID 2.4.2.9 DE Uracil phosphoribosyltransferase. AN UMP pyrophosphorylase. AN UMP diphosphorylase. CA UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. DR P71479, PYR1_LACPL; P59389, PYR2_LACPL; Q8YV98, PYRR_ANASP; DR P41007, PYRR_BACCL; Q9K9V4, PYRR_BACHD; P39765, PYRR_BACSU; DR Q97HA0, PYRR_CLOAB; Q8XJB2, PYRR_CLOPE; P59011, PYRR_CORGL; DR Q9RVB9, PYRR_DEIRA; O52707, PYRR_ENTFA; Q8RG90, PYRR_FUSNN; DR P44722, PYRR_HAEIN; Q92AG8, PYRR_LISIN; Q8Y660, PYRR_LISMO; DR P71807, PYRR_MYCTU; Q9CLL7, PYRR_PASMU; Q9X6W6, PYRR_PSEAE; DR Q9F4I7, PYRR_PSEFL; Q9Z441, PYRR_PSEPU; Q8Y1L3, PYRR_RALSO; DR Q99US0, PYRR_STAAM; Q9KXR1, PYRR_STRCO; Q8K7Y5, PYRR_STRP3; DR P59013, PYRR_STRP8; Q97QE1, PYRR_STRPN; Q9A0D0, PYRR_STRPY; DR Q55758, PYRR_SYNY3; P96078, PYRR_THEAQ; Q8R9R3, PYRR_THETN; DR O13867, UPP1_SCHPO; Q9HE15, UPP2_SCHPO; Q9YEN3, UPP_AERPE ; DR Q8UJ06, UPP_AGRT5 ; Q8YVB5, UPP_ANASP ; O67914, UPP_AQUAE ; DR O65583, UPP_ARATH ; P70881, UPP_BACCL ; Q9K6G5, UPP_BACHD ; DR P39149, UPP_BACSU ; Q8YDE5, UPP_BRUME ; Q9PN13, UPP_CAMJE ; DR Q9A627, UPP_CAUCR ; Q9PJJ6, UPP_CHLMU ; Q97F73, UPP_CLOAB ; DR Q8XIC4, UPP_CLOPE ; P58998, UPP_CORGL ; Q9RU32, UPP_DEIRA ; DR P25532, UPP_ECOLI ; Q8RG35, UPP_FUSNN ; P43857, UPP_HAEIN ; DR Q9HN05, UPP_HALN1 ; Q9RGY8, UPP_LACAC ; Q9CEC9, UPP_LACLA ; DR P50926, UPP_LACLC ; Q9RE01, UPP_LACPL ; Q93CX7, UPP_LACSK ; DR Q927V5, UPP_LISIN ; Q8Y4B3, UPP_LISMO ; O27186, UPP_METTH ; DR P47276, UPP_MYCGE ; P43049, UPP_MYCHO ; P75081, UPP_MYCPN ; DR Q98QP6, UPP_MYCPU ; P94928, UPP_MYCTU ; Q9JV58, UPP_NEIMA ; DR Q9K048, UPP_NEIMB ; Q9CPL8, UPP_PASMU ; Q9ZNF8, UPP_PORGI ; DR Q9HVE6, UPP_PSEAE ; Q9V0K1, UPP_PYRAB ; Q8ZWV9, UPP_PYRAE ; DR Q8U1G7, UPP_PYRFU ; Q8XXC7, UPP_RALSO ; Q98GV3, UPP_RHILO ; DR Q92T49, UPP_RHIME ; Q93A76, UPP_SALTY ; Q99SE6, UPP_STAAM ; DR Q9AK76, UPP_STRCO ; Q97RQ3, UPP_STRPN ; Q9A194, UPP_STRPY ; DR P36399, UPP_STRSL ; Q980Q4, UPP_SULSO ; Q975Z7, UPP_SULTO ; DR P72753, UPP_SYNY3 ; Q9WZI0, UPP_THEMA ; Q8RD94, UPP_THETN ; DR P93394, UPP_TOBAC ; Q26998, UPP_TOXGO ; O83462, UPP_TREPA ; DR Q9PR28, UPP_UREPA ; Q9KPY7, UPP_VIBCH ; Q87MH1, UPP_VIBPA ; DR P59001, UPP_XANAC ; Q9RBJ3, UPP_XANCP ; P18562, UPP_YEAST ; DR Q8ZCX9, UPP_YERPE ; // ID 2.4.2.10 DE Orotate phosphoribosyltransferase. AN Orotidylic acid phosphorylase. AN Orotidine-5'-phosphate pyrophosphorylase. AN Orotidine-5'-phosphate diphosphorylase. AN OPRT. CA Orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha- CA D-ribose 1-diphosphate. CC -!- The enzyme from higher eukaryotes also catalyzes the reaction listed CC as EC 4.1.1.23. DI Oroticaciduria I; MIM:258900. PR PROSITE; PDOC00096; DR Q98AN7, PYE1_RHILO; Q985B1, PYE2_RHILO; Q8YSY4, PYFE_ANASP; DR Q42586, PYR5_ARATH; P31754, PYR5_BOVIN; P09556, PYR5_DICDI; DR Q01637, PYR5_DROME; P11172, PYR5_HUMAN; P13439, PYR5_MOUSE; DR Q25566, PYR5_NAEGR; Q42942, PYR5_TOBAC; Q9Y9D8, PYRE_AERPE; DR Q8UI98, PYRE_AGRT5; Q8YM41, PYRE_ANASP; O67742, PYRE_AQUAE; DR O28533, PYRE_ARCFU; P46534, PYRE_BACCL; Q9K9W3, PYRE_BACHD; DR P25972, PYRE_BACSU; Q8G661, PYRE_BIFLO; Q8YG66, PYRE_BRUME; DR P57622, PYRE_BUCAI; P59575, PYRE_BUCBP; Q9PIR1, PYRE_CAMJE; DR Q9A810, PYRE_CAUCR; Q9Z7U6, PYRE_CHLPN; Q97N11, PYRE_CLOAB; DR Q8XL65, PYRE_CLOPE; O93849, PYRE_COCPO; P35788, PYRE_COLGR; DR Q8NM11, PYRE_CORGL; Q45918, PYRE_COXBU; P18132, PYRE_CRYNE; DR Q9RX68, PYRE_DEIRA; Q8XD99, PYRE_ECO57; P00495, PYRE_ECOLI; DR O07657, PYRE_ENTFA; P58856, PYRE_FUSNN; P43855, PYRE_HAEIN; DR Q9HNG2, PYRE_HALN1; Q9ZJX0, PYRE_HELPJ; P56162, PYRE_HELPY; DR O13474, PYRE_KLULA; Q9CGM8, PYRE_LACLA; P77889, PYRE_LACPL; DR Q92AH7, PYRE_LISIN; Q8Y668, PYRE_LISMO; P58859, PYRE_METAC; DR O42767, PYRE_METAN; Q8VR31, PYRE_METCA; Q58509, PYRE_METJA; DR P58860, PYRE_METKA; Q8Q0J4, PYRE_METMA; O27888, PYRE_METTH; DR Q9CB28, PYRE_MYCLE; Q8EUY4, PYRE_MYCPE; O53717, PYRE_MYCTU; DR Q9JR25, PYRE_NEIMA; Q8ER35, PYRE_OCEIH; Q9CJW4, PYRE_PASMU; DR P08309, PYRE_PODAN; P50587, PYRE_PSEAE; P56814, PYRE_PYRAB; DR Q8ZTG3, PYRE_PYRAE; P58861, PYRE_PYRFU; O58855, PYRE_PYRHO; DR Q8Y342, PYRE_RALSO; P42719, PYRE_RHILT; Q92SC6, PYRE_RHIME; DR Q8Z2H5, PYRE_SALTI; P08870, PYRE_SALTY; O94331, PYRE_SCHPO; DR Q8E9L5, PYRE_SHEON; P18904, PYRE_SORMA; Q99UR3, PYRE_STAAM; DR Q8NX25, PYRE_STAAW; Q8CSW7, PYRE_STAEP; Q8E5F1, PYRE_STRA3; DR Q9X8R7, PYRE_STRCO; Q8DTV2, PYRE_STRMU; P58857, PYRE_STRP3; DR Q97RT8, PYRE_STRPN; Q9A076, PYRE_STRPY; Q8DQL5, PYRE_STRR6; DR O08359, PYRE_SULAC; Q9UX09, PYRE_SULSO; Q970X1, PYRE_SULTO; DR Q8DHW5, PYRE_SYNEL; Q55574, PYRE_SYNY3; Q9HM15, PYRE_THEAC; DR Q9WYG6, PYRE_THEMA; Q60016, PYRE_THETH; P58858, PYRE_THETN; DR Q97CT9, PYRE_THEVO; P21846, PYRE_TRIRE; Q9KVD5, PYRE_VIBCH; DR Q8DDX5, PYRE_VIBVU; Q8PFS5, PYRE_XANAC; Q8P469, PYRE_XANCP; DR Q9PGZ3, PYRE_XYLFA; Q87F16, PYRE_XYLFT; P41923, PYRE_YARLI; DR P13298, PYRE_YEAST; Q8ZJP7, PYRE_YERPE; P30402, PYRX_YEAST; // ID 2.4.2.11 DE Nicotinate phosphoribosyltransferase. AN Nicotinic acid phosphoribosyltransferase. AN Nicotinic acid mononucleotide glycohydrolase. AN Nicotinic acid mononucleotide pyrophosphorylase. AN Niacin ribonucleotidase. CA Nicotinate D-ribonucleotide + diphosphate = nicotinate + 5-phospho- CA alpha-D-ribose 1-diphosphate. DR Q9UTK3, NPT1_SCHPO; P39683, NPT1_YEAST; Q9HUP4, PNB1_PSEAE; DR Q9HW26, PNB2_PSEAE; Q8UIS9, PNCB_AGRT5; Q8YEP2, PNCB_BRUME; DR P57442, PNCB_BUCAI; Q8K9I6, PNCB_BUCAP; Q8XDE8, PNCB_ECO57; DR P18133, PNCB_ECOLI; Q8TMW6, PNCB_METAC; Q8PSJ3, PNCB_METMA; DR Q9JTM8, PNCB_NEIMA; Q9JYM9, PNCB_NEIMB; Q8Y0L2, PNCB_RALSO; DR Q98D24, PNCB_RHILO; Q92S49, PNCB_RHIME; Q8Z7Y9, PNCB_SALTI; DR P22253, PNCB_SALTY; Q9KN67, PNCB_VIBCH; Q8PGU5, PNCB_XANAC; DR Q8PCP3, PNCB_XANCP; Q9PED1, PNCB_XYLFA; Q87EC4, PNCB_XYLFT; DR Q8ZG93, PNCB_YERPE; // ID 2.4.2.12 DE Nicotinamide phosphoribosyltransferase. AN NMN pyrophosphorylase. AN NMN diphosphorylase. CA Nicotinamide D-ribonucleotide + diphosphate = nicotinamide + CA 5-phospho-alpha-D-ribose 1-diphosphate. // ID 2.4.2.13 DE Transferred entry: 2.5.1.6. // ID 2.4.2.14 DE Amidophosphoribosyltransferase. AN Glutamine phosphoribosylpyrophosphate amidotransferase. AN Phosphoribosyldiphosphate 5-amidotransferase. CA 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = CA L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H(2)O. PR PROSITE; PDOC00096; PR PROSITE; PDOC00406; DR O29388, PUR1_ARCFU; P00497, PUR1_BACSU; P28173, PUR1_CHICK; DR Q27601, PUR1_DROME; P00496, PUR1_ECOLI; P43854, PUR1_HAEIN; DR Q06203, PUR1_HUMAN; P35853, PUR1_LACCA; Q57657, PUR1_METJA; DR O26742, PUR1_METTH; Q50028, PUR1_MYCLE; O06626, PUR1_MYCTU; DR Q9L6B8, PUR1_PASMU; Q51342, PUR1_PSEAE; Q9V253, PUR1_PYRAB; DR O57979, PUR1_PYRHO; P35433, PUR1_RAT ; P77935, PUR1_RHIET; DR Q12698, PUR1_SACKL; P41390, PUR1_SCHPO; P52418, PUR1_SOYBN; DR Q55038, PUR1_SYNP7; Q55621, PUR1_SYNY3; P52419, PUR1_VIGAC; DR P04046, PUR1_YEAST; // ID 2.4.2.15 DE Guanosine phosphorylase. CA Guanosine + phosphate = guanine + D-ribose 1-phosphate. CC -!- Also acts on deoxyguanosine. // ID 2.4.2.16 DE Urate-ribonucleotide phosphorylase. CA Urate D-ribonucleotide + phosphate = urate + D-ribose 1-phosphate. // ID 2.4.2.17 DE ATP phosphoribosyltransferase. AN Phosphoribosyl-ATP pyrophosphorylase. AN Phosphoribosyl-ATP diphosphorylase. CA 1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha- CA D-ribose 1-diphosphate. PR PROSITE; PDOC01020; DR Q8UHK1, HIS1_AGRT5; Q8YVL0, HIS1_ANASP; O67543, HIS1_AQUAE; DR O29665, HIS1_ARCFU; Q9K6Z1, HIS1_BACHD; O34520, HIS1_BACSU; DR Q8YB47, HIS1_BRUME; P57200, HIS1_BUCAI; Q9ZHE7, HIS1_BUCAP; DR P59453, HIS1_BUCBP; Q9RQ89, HIS1_BUCDN; Q9RQ83, HIS1_BUCMH; DR Q9RQ86, HIS1_BUCSC; Q9PM78, HIS1_CAMJE; P46586, HIS1_CANAL; DR Q9A2P5, HIS1_CAUCR; Q97KI3, HIS1_CLOAB; Q9Z472, HIS1_CORGL; DR Q9RUE2, HIS1_DEIRA; Q8X8T4, HIS1_ECO57; P10366, HIS1_ECOLI; DR P43853, HIS1_HAEIN; Q9HN53, HIS1_HALN1; P05148, HIS1_KLEPN; DR Q02129, HIS1_LACLA; Q92E83, HIS1_LISIN; Q8Y9G0, HIS1_LISMO; DR Q8TU56, HIS1_METAC; Q58601, HIS1_METJA; Q8TYD5, HIS1_METKA; DR Q8PWS3, HIS1_METMA; O27550, HIS1_METTH; Q49776, HIS1_MYCLE; DR O33256, HIS1_MYCTU; Q9JQS2, HIS1_NEIMA; P57919, HIS1_PASMU; DR Q9HVW8, HIS1_PSEAE; Q8ZY36, HIS1_PYRAE; Q8U0D4, HIS1_PYRFU; DR Q987S8, HIS1_RHILO; Q92RR6, HIS1_RHIME; Q8Z5K1, HIS1_SALTI; DR P00499, HIS1_SALTY; P40373, HIS1_SCHPO; Q99QW2, HIS1_STAAM; DR O33771, HIS1_SULSO; Q970Z3, HIS1_SULTO; Q55503, HIS1_SYNY3; DR Q9X0D2, HIS1_THEMA; Q8R881, HIS1_THETN; Q9KSX4, HIS1_VIBCH; DR Q87QL2, HIS1_VIBPA; Q8D8P9, HIS1_VIBVU; Q8PLH0, HIS1_XANAC; DR Q8P9P3, HIS1_XANCP; Q9PBC4, HIS1_XYLFA; Q87C28, HIS1_XYLFT; DR Q99145, HIS1_YARLI; P00498, HIS1_YEAST; Q8ZFX4, HIS1_YERPE; DR Q9RH04, HIS1_ZYMMO; // ID 2.4.2.18 DE Anthranilate phosphoribosyltransferase. AN Phosphoribosyl-anthranilate pyrophosphorylase. AN Phosphoribosyl-anthranilate diphosphorylase. CA Anthranilate + phosphoribosylpyrophosphate = N-5'-phosphoribosyl- CA anthranilate + diphosphate. CC -!- In some organisms, this enzyme is part of a multifunctional protein CC together with one or more components of the system for biosynthesis CC of tryptophan (EC 4.1.1.48, EC 4.1.3.27, EC 4.2.1.20, and CC EC 5.3.1.24). DR O28668, TRCD_ARCFU; Q8YZP8, TRD1_ANASP; Q8XVE7, TRD1_RALSO; DR O68608, TRD1_STRCO; Q8YXQ9, TRD2_ANASP; Q8XS00, TRD2_RALSO; DR Q9Z4W9, TRD2_STRCO; P00500, TRPD_ACICA; Q9Y8T2, TRPD_AERPE; DR Q8UER8, TRPD_AGRT5; O66576, TRPD_AQUAE; Q02166, TRPD_ARATH; DR P26924, TRPD_AZOBR; P30525, TRPD_BACCA; Q9KCB3, TRPD_BACHD; DR P70936, TRPD_BACME; P18261, TRPD_BACPU; Q9X6J5, TRPD_BACST; DR P03947, TRPD_BACSU; P94326, TRPD_BRAJA; Q8YHF7, TRPD_BRUME; DR P57367, TRPD_BUCAI; P42392, TRPD_BUCAP; P59415, TRPD_BUCBP; DR O68426, TRPD_BUCDN; Q9RQ35, TRPD_BUCMH; Q44602, TRPD_BUCSC; DR Q9A728, TRPD_CAUCR; Q97EF2, TRPD_CLOAB; P06559, TRPD_CORGL; DR Q9RTJ5, TRPD_DEIRA; P12320, TRPD_ERWCA; P43858, TRPD_HAEIN; DR Q9HPG3, TRPD_HALN1; P52562, TRPD_HALVO; Q9ZJU7, TRPD_HELPJ; DR P56737, TRPD_HELPY; P17170, TRPD_LACCA; Q02000, TRPD_LACLA; DR Q92B78, TRPD_LISIN; Q8Y6Q3, TRPD_LISMO; Q8TLP5, TRPD_METAC; DR Q57686, TRPD_METJA; Q8TXJ5, TRPD_METKA; Q8PT97, TRPD_METMA; DR O27698, TRPD_METTH; P26925, TRPD_METTM; O69581, TRPD_MYCLE; DR Q10382, TRPD_MYCTU; Q9JQM3, TRPD_NEIMA; P57856, TRPD_PASMU; DR P20574, TRPD_PSEAE; P20575, TRPD_PSEPU; Q9V1G4, TRPD_PYRAB; DR Q8ZV45, TRPD_PYRAE; Q8U089, TRPD_PYRFU; Q9YGB4, TRPD_PYRKO; DR Q98ME4, TRPD_RHILO; Q92PS0, TRPD_RHIME; Q9ZFA8, TRPD_RHOSH; DR O60122, TRPD_SCHPO; P12321, TRPD_SERMA; Q99UB2, TRPD_STAAM; DR Q97P29, TRPD_STRPN; P50384, TRPD_SULSO; Q971Z7, TRPD_SULTO; DR P73617, TRPD_SYNY3; Q9HK06, TRPD_THEAC; Q8R9M6, TRPD_THETN; DR Q979V5, TRPD_THEVO; Q9KST4, TRPD_VIBCH; P22096, TRPD_VIBPA; DR Q8D8B4, TRPD_VIBVU; Q8PQ48, TRPD_XANAC; Q8PD71, TRPD_XANCP; DR Q9PGT6, TRPD_XYLFA; Q87EX3, TRPD_XYLFT; P07285, TRPD_YEAST; DR Q8ZEG7, TRPD_YERPE; P00904, TRPG_ECOLI; P00905, TRPG_SALTY; DR P00906, TRPG_SHIDY; Q08654, TRPG_THEMA; // ID 2.4.2.19 DE Nicotinate-nucleotide pyrophosphorylase (carboxylating). AN Nicotinate-nucleotide diphosphorylase (carboxylating). AN Quinolinate phosphoribosyltransferase (decarboxylating). CA Nicotinate D-ribonucleotide + diphosphate + CO(2) = CA pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate. DR O28439, NADC_ARCFU; P39666, NADC_BACSU; P30011, NADC_ECOLI; DR Q9ZJN2, NADC_HELPJ; O25909, NADC_HELPY; Q15274, NADC_HUMAN; DR Q57916, NADC_METJA; O27860, NADC_METTH; Q91X91, NADC_MOUSE; DR P46714, NADC_MYCLE; O06594, NADC_MYCTU; P30819, NADC_PSEAE; DR P77938, NADC_RHORU; P30012, NADC_SALTY; P74301, NADC_SYNY3; DR P43619, NADC_YEAST; // ID 2.4.2.20 DE Dioxotetrahydropyrimidine phosphoribosyltransferase. AN Dioxotetrahydropyrimidine-ribonucleotide pyrophosphorylase. AN Dioxotetrahydropyrimidine-ribonucleotide diphosphorylase. CA A 2,4-dioxotetrahydropyrimidine D-ribonucleotide + diphosphate = A CA 2,4-dioxotetrahydropyrimidine + 5-phospho-alpha-D-ribose 1-diphosphate. CC -!- Acts, in the reverse direction, on uracil and other pyrimidines and CC pteridines containing a 2,4-diketo structure. // ID 2.4.2.21 DE Nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase. AN N(1)-alpha-phosphoribosyltransferase. CA Beta-nicotinate D-ribonucleotide + dimethylbenzimidazole = nicotinate CA + N(1)-(5-phospho-alpha-D-ribosyl)-5,6-dimethylbenzimidazole. CC -!- Also acts on benzimidazole, and the clostridial enzyme acts on CC adenine to form 7-alpha-D-ribosyladenine 5'-phosphate. DR Q9KG31, COBT_BACHD; Q9RYR8, COBT_DEIRA; P36562, COBT_ECOLI; DR Q9X7F4, COBT_METSQ; O32953, COBT_MYCLE; Q10396, COBT_MYCTU; DR Q52679, COBT_RHOCA; Q05603, COBT_SALTY; Q9S2R1, COBT_STRCO; DR P29935, COBU_PSEDE; // ID 2.4.2.22 DE Xanthine-guanine phosphoribosyltransferase. CA 5-phospho-alpha-D-ribose 1-diphosphate + xanthine = (9-D- CA ribosylxanthine)-5'-phosphate + diphosphate. PR PROSITE; PDOC00096; DR P57339, XGPT_BUCAI; Q8K9R8, XGPT_BUCAP; P00501, XGPT_ECOLI; DR P43859, XGPT_HAEIN; P26972, XGPT_SALTY; // ID 2.4.2.23 DE Deoxyuridine phosphorylase. CA Deoxyuridine + phosphate = uracil + deoxy-D-ribose 1-phosphate. // ID 2.4.2.24 DE 1,4-beta-D-xylan synthase. CA UDP-D-xylose + {(1,4)-beta-D-xylan}(N) = UDP + {(1,4)-beta-D-xylan}(N+1). CC -!- Formerly EC 2.4.1.72. // ID 2.4.2.25 DE Flavone apiosyltransferase. CA UDP-apiose + 7-O-beta-D-glucosyl-5,7,4'-trihydroxyflavone = UDP + 7-O- CA (beta-D-apiofuranosyl-1,2-beta-D-glucosyl)-5,7,4'-trihydroxyflavone. CC -!- 7-O-beta-D-glucosides of a number of flavonoids and of 4-substituted CC phenols can act as acceptors. // ID 2.4.2.26 DE Protein xylosyltransferase. AN UDP-D-xylose:core protein beta-D-xylosyltransferase. AN UDP-D-xylose:core protein xylosyltransferase. AN UDP-D-xylose:proteoglycan core protein beta-D-xylosyltransferase. AN UDP-xylose-core protein beta-D-xylosyltransferase. AN Uridine diphosphoxylose-core protein beta-xylosyltransferase. AN Uridine diphosphoxylose-protein xylosyltransferase. CA Transfers a beta-D-xylosyl residue from UDP-D-xylose to the serine CA hydroxy group of an acceptor protein substrate. CC -!- Involved in the biosynthesis of the linkage region of CC glycosaminoglycan chains as part of proteoglycan biosynthesis CC (chondroitin, dermatan and heparan sulfates). // ID 2.4.2.27 DE dTDP-dihydrostreptose-streptidine-6-phosphate DE dihydrostreptosyltransferase. CA dTDP-L-dihydrostreptose + streptidine 6-phosphate = dTDP + CA O-1,4-alpha-L-dihydrostreptosyl-streptidine 6-phosphate. DR P09399, STRH_STRGR; // ID 2.4.2.28 DE 5'-methylthioadenosine phosphorylase. CA 5'-methylthioadenosine + phosphate = adenine + 5-methylthio-D- CA ribose 1-phosphate. CC -!- Also acts on 5'-deoxyadenosine and other analogs having 5'-deoxy CC groups. PR PROSITE; PDOC00946; PR PROSITE; PDOC00954; DR Q09438, MTAP_CAEEL; Q9V813, MTAP_DROME; Q13126, MTAP_HUMAN; DR Q9CQ65, MTAP_MOUSE; P50389, MTAP_SULSO; // ID 2.4.2.29 DE Queuine tRNA-ribosyltransferase. AN tRNA-guanine transglycosylase. AN Guanine insertion enzyme. CA tRNA guanine + queuine = tRNA queuine + guanine. CC -!- Also catalyzes the exchange of precursors of queuine and of CC guanine itself for guanine located in the first position of CC certain tRNA anticodons. DR Q8UES8, TGT_AGRT5 ; Q8YVT9, TGT_ANASP ; O67331, TGT_AQUAE ; DR O28787, TGT_ARCFU ; Q9KDI5, TGT_BACHD ; O32053, TGT_BACSU ; DR O51749, TGT_BORBU ; Q8YHB2, TGT_BRUME ; P57233, TGT_BUCAI ; DR Q8KA09, TGT_BUCAP ; Q23623, TGT_CAEEL ; Q9PNT0, TGT_CAMJE ; DR Q9A7Y1, TGT_CAUCR ; Q9PKK0, TGT_CHLMU ; Q9Z8W5, TGT_CHLPN ; DR O84196, TGT_CHLTR ; Q97GT3, TGT_CLOAB ; Q8XJ16, TGT_CLOPE ; DR Q9RRB5, TGT_DEIRA ; Q9VPY8, TGT_DROME ; P19675, TGT_ECOLI ; DR Q8RDN0, TGT_FUSNN ; P44594, TGT_HAEIN ; Q9ZMF4, TGT_HELPJ ; DR O08314, TGT_HELPY ; Q9BXR0, TGT_HUMAN ; Q9CJ54, TGT_LACLA ; DR Q92BI4, TGT_LISIN ; Q8Y700, TGT_LISMO ; Q9JMA2, TGT_MOUSE ; DR Q9JVA4, TGT_NEIMA ; Q9K096, TGT_NEIMB ; P57831, TGT_PASMU ; DR Q9HXH9, TGT_PSEAE ; Q8XVW4, TGT_RALSO ; Q98M57, TGT_RHILO ; DR Q92PY4, TGT_RHIME ; Q92GM6, TGT_RICCN ; Q9ZCK8, TGT_RICPR ; DR Q8Z8Y0, TGT_SALTI ; Q8ZRD8, TGT_SALTY ; O94460, TGT_SCHPO ; DR Q54177, TGT_SHIFL ; Q99TL4, TGT_STAAM ; Q8CML7, TGT_STAEP ; DR Q8P2S1, TGT_STRP3 ; Q97NH1, TGT_STRPN ; Q9A1L6, TGT_STRPY ; DR Q55983, TGT_SYNY3 ; Q9X1P7, TGT_THEMA ; Q8RAM9, TGT_THETN ; DR Q9KTY9, TGT_VIBCH ; Q87S36, TGT_VIBPA ; Q8DEY0, TGT_VIBVU ; DR Q8PJL7, TGT_XANAC ; Q8P868, TGT_XANCP ; Q9PGS5, TGT_XYLFA ; DR Q87EW6, TGT_XYLFT ; Q8ZC33, TGT_YERPE ; P28720, TGT_ZYMMO ; // ID 2.4.2.30 DE NAD(+) ADP-ribosyltransferase. AN Poly(ADP-ribose)polymerase. AN Poly(adenosine diphosphate ribose) polymerase. AN ADP-ribosyltransferase (polymerizing). AN Poly(ADP-ribose) synthetase. CA NAD(+) + {ADP-D-ribosyl}(N)-acceptor = nicotinamide + CA {ADP-D-ribosyl}(N+1)-acceptor. CC -!- The ADP-D-ribosyl group of NAD(+) is transferred to an acceptor CC carboxyl group on a histone or the enzyme itself, and further ADP- CC ribosyl groups are transferred to the 2'-position of the terminal CC adenosine moiety, building up a polymer with an average chain CC length of 20-30 units. PR PROSITE; PDOC00360; DR Q09525, PME2_CAEEL; Q9UGN5, PPO2_HUMAN; O88554, PPO2_MOUSE; DR Q9Y6F1, PPO3_HUMAN; Q11207, PPOL_ARATH; P18493, PPOL_BOVIN; DR P26446, PPOL_CHICK; Q9R152, PPOL_CRIGR; P35875, PPOL_DROME; DR P09874, PPOL_HUMAN; P11103, PPOL_MOUSE; Q08824, PPOL_ONCMA; DR P27008, PPOL_RAT ; Q11208, PPOL_SARPE; P31669, PPOL_XENLA; DR Q9UKK3, PPOV_HUMAN; O95271, TNK1_HUMAN; Q9H2K2, TNK2_HUMAN; // ID 2.4.2.31 DE NAD(P)(+)--arginine ADP-ribosyltransferase. AN ADP-ribosyltransferase. AN Mono(ADP-ribosyl)transferase. CA NAD(+) + L-arginine = nicotinamide + N(2)-(ADP-D-ribosyl)-L-arginine. CC -!- NADP(+) can act as donor. CC -!- Arginine residues in proteins can act as acceptors. CC -!- Agmatine, arginine methyl ester and guanidine can also act as CC acceptors. CC -!- Catalyzes the NAD-dependent activation of EC 4.6.1.1. CC -!- Some bacterial enterotoxins possess similar enzymatic activities. CC -!- Cf. EC 2.4.2.36. PR PROSITE; PDOC00993; DR P52961, NAR1_HUMAN; Q60935, NAR1_MOUSE; Q03515, NAR1_RABIT; DR Q13508, NAR3_HUMAN; Q8R2G4, NAR3_MOUSE; Q93070, NAR4_HUMAN; DR Q95NE0, NAR4_PANTR; Q96L15, NAR5_HUMAN; P70352, NAR5_MOUSE; DR P17981, NARA_MOUSE; P17982, NARA_RAT ; O35975, NARB_MOUSE; DR P20974, NARB_RAT ; Q92080, NARE_CHICK; P55806, NRT1_CHICK; DR P55807, NRT2_CHICK; // ID 2.4.2.32 DE Dolichyl-phosphate D-xylosyltransferase. CA UDP-D-xylose + dolichyl phosphate = UDP + dolichyl D-xylosyl phosphate. // ID 2.4.2.33 DE Dolichyl-xylosyl-phosphate--protein xylosyltransferase. CA Dolichyl D-xylosyl phosphate + protein = dolichyl phosphate + CA D-xylosylprotein. // ID 2.4.2.34 DE Indolylacetylinositol arabinosyltransferase. AN Arabinosylindolylacetylinositol synthase. CA UDP-L-arabinose + indol-3-ylacetyl-myo-inositol = UDP + indol-3-ylacetyl- CA myo-inositol L-arabinoside. // ID 2.4.2.35 DE Flavonol-3-O-glycoside xylosyltransferase. CA UDP-D-xylose + flavonol 3-O-glycoside = UDP + flavonol CA 3-O-D-xylosylglycoside. CC -!- Flavonol 3-O-glucoside, flavonol 3-O-galactoside, and, more slowly, CC rutin can act as acceptors. // ID 2.4.2.36 DE NAD(+)--diphthamide ADP-ribosyltransferase. AN ADP-ribosyltransferase. AN Mono(ADP-ribosyl)transferase. CA NAD(+) + peptide diphthamide = nicotinamide + peptide N-(ADP-D- CA ribosyl)diphthamide. CC -!- Diphteria toxin and some other bacterial toxins catalyze this CC reaction. The acceptor is a diphthamide residue in elongation factor CC 2 (cf. EC 2.4.2.31). DR P01555, CHTA_VIBCH; P00588, DTX_CORBE ; P00587, DTX_COROM ; // ID 2.4.2.37 DE NAD(+)--dinitrogen-reductase ADP-D-ribosyltransferase. AN NAD--azoferredoxin (ADP-ribose)transferase. AN ADP-ribosyltransferase. CA NAD(+) + [dinitrogen reductase] = nicotinamide + ADP-D-ribosyl- CA [dinitrogen reductase]. CC -!- Together with EC 3.2.2.24, controls the level of activity of CC EC 1.18.6.1. DR P14299, DRAT_RHORU; // ID 2.4.2.38 DE Glycoprotein 2-beta-D-xylosyltransferase. AN Beta-1,2-xylosyltransferase. CA UDP-L-xylose + N(4)-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D- CA mannosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl- CA (1->6)]-beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N- CA acetyl-beta-D-glucosaminyl}asparagine = UDP + N(4)-{N-acetyl-beta-D- CA glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-acetyl-beta-D- CA glucosaminyl-(1->2)-alpha-D-mannosyl-(1->6)]-[beta-D-xylosyl-(1->2)]- CA beta-D-mannosyl-(1->4)-N-acetyl-beta-D-glucosaminyl-(1->4)-N-acetyl- CA beta-D-glucosaminyl}asparagine. CC -!- Specific for N-linked oligosaccharides (N-glycans). DR Q9LDH0, XYLT_ARATH; // ID 2.4.99.1 DE Beta-galactosamide alpha-2,6-sialyltransferase. AN Beta-galactoside alpha-2,6-sialyltransferase. AN CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase. CA CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-acetyl-beta-D- CA glucosamine = CMP + alpha-N-acetylneuraminyl-2,6-beta-D-galactosyl- CA 1,4-N-acetyl-beta-D-glucosamine. CC -!- The terminal beta-D-galactosyl residue of the oligosaccharide of CC glycoproteins, as well as lactose, can act as acceptor. DR Q92182, SIA1_CHICK; P15907, SIA1_HUMAN; Q64685, SIA1_MOUSE; DR P13721, SIA1_RAT ; // ID 2.4.99.2 DE Monosialoganglioside sialyltransferase. CA CMP-N-acetylneuraminate + D-galactosyl-N-acetyl-D-galactosaminyl- CA (N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide = CMP + CA N-acetylneuraminyl-D-galactosyl-N-acetyl-D-galactosaminyl- CA (N-acetylneuraminyl)-D-galactosyl-D-glucosylceramide. CC -!- May be identical with EC 2.4.99.4. // ID 2.4.99.3 DE Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase. AN GalNAc alpha-2,6-sialyltransferase I. CA CMP-N-acetylneuraminate + glycano-1,3-(N-acetyl-D-galactosaminyl)- CA glycoprotein = CMP + glycano-(2,6-alpha-N-acetylneuraminyl)-(N-acetyl- CA D-galactosaminyl)-glycoprotein. CC -!- Alpha-N-acetylgalactosamine linked to threonine or serine is also an CC acceptor, when substituted at the 3-position. DR Q92183, SI7A_CHICK; Q9NSC7, SI7A_HUMAN; Q9QZ39, SI7A_MOUSE; // ID 2.4.99.4 DE Beta-galactoside alpha-2,3-sialyltransferase. AN CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase. CA CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D- CA galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl- CA 1,3-N-acetyl-alpha-D-galactosaminyl-R. CC -!- The acceptor is Gal-beta-1,3-GalNAc-R, where R is H, a CC threonine or serine residue in a glycoprotein, or a glycolipid. CC -!- Lactose can also act as acceptor. CC -!- May be identical with EC 2.4.99.2. DR Q11200, SI4A_CHICK; Q11201, SI4A_HUMAN; P54751, SI4A_MOUSE; DR Q02745, SI4A_PIG ; // ID 2.4.99.5 DE Galactosyldiacylglycerol alpha-2,3-sialyltransferase. CA CMP-N-acetylneuraminate + 1,2-diacyl-3-beta-D-galactosyl-sn-glycerol = CA CMP + 1,2-diacyl-3-[3-(alpha-D-N-acetylneuraminyl)-beta-D-galactosyl]- CA sn-glycerol. CC -!- The beta-D-galactosyl residue of the oligosaccharide of glycoproteins CC may also act as acceptor. // ID 2.4.99.6 DE N-acetyllactosaminide alpha-2,3-sialyltransferase. CA CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl- CA glycoprotein = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4- CA N-acetyl-D-glucosaminyl-glycoprotein. CC -!- Acts on beta-D-galactosyl-1,4-N-acetyl-D-glucosaminyl termini on CC glycoprotein. DR Q11203, SIA6_HUMAN; P97325, SIA6_MOUSE; Q02734, SIA6_RAT ; // ID 2.4.99.7 DE (Alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N- DE acetylgalactosaminide alpha-2,6-sialyltransferase. CA CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl- CA 1,3-N-acetyl-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-2,3- CA beta-D-galactosyl-1,3-(alpha-N-acetylneuraminyl-2,6)-N-acetyl-D- CA galactosaminyl-R. CC -!- Attaches N-acetylneuraminic acid in alpha-2,6-linkage to CC N-acetylgalactosamine only when present in the structure alpha-N- CC acetylneuraminyl-2,3-beta-galactosyl-1,3-N-acetylgalactosaminyl-R, CC where R may be protein or P-nitrophenol. CC -!- Not identical with EC 2.4.99.3. DR Q9H4F1, SI7D_HUMAN; Q9R2B6, SI7D_MOUSE; // ID 2.4.99.8 DE Alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase. CA CMP-N-acetylneuraminate + alpha-N-acetylneuraminyl-2,3-beta-D- CA galactosyl-R = CMP + alpha-N-acetylneuraminyl-2,8-alpha-N- CA acetylneuraminyl-2,3-beta-D-galactosyl-R. CC -!- Gangliosides act as acceptors. DR Q92185, SI8A_HUMAN; Q64687, SI8A_MOUSE; // ID 2.4.99.9 DE Lactosylceramide alpha-2,3-sialyltransferase. AN Ganglioside GM3 synthase. CA CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide = CA CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-beta-D- CA glucosylceramide. CC -!- Lactose cannot act as acceptor. DR Q9UNP4, SIA9_HUMAN; O88829, SIA9_MOUSE; // ID 2.4.99.10 DE Neolactotetraosylceramide alpha-2,3-sialyltransferase. AN Sialyltransferase. CA CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-N-acetyl-beta-D- CA glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide = CMP + CA alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,4-N-acetyl-beta-D- CA glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide. // ID 2.4.99.11 DE Lactosylceramide alpha-2,6-N-sialyltransferase. CA CMP-N-acetylneuraminate + beta-D-galactosyl-1,4-beta-D-glucosylceramide = CA CMP + alpha-N-acetylneuraminyl-2,6-beta-galactosyl-1,4-beta-D-glucosyl- CA ceramide. // ID 2.5.1.1 DE Dimethylallyltransferase. AN Prenyltransferase. AN Geranyl-diphosphate synthase. AN Dimethylallyltransferase. CA Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + CA geranyl diphosphate. CC -!- Will not accept larger prenyl diphosphates as efficient donors. PR PROSITE; PDOC00407; DR Q09152, FPP1_ARATH; P49351, FPP1_LUPAL; O24241, FPP1_PARAR; DR Q43315, FPP2_ARATH; P49352, FPP2_LUPAL; O24242, FPP2_PARAR; DR P49350, FPPS_ARTAN; P08836, FPPS_CHICK; Q92235, FPPS_GIBFU; DR O64905, FPPS_HELAN; P14324, FPPS_HUMAN; P49349, FPPS_KLULA; DR P49353, FPPS_MAIZE; Q92250, FPPS_NEUCR; P05369, FPPS_RAT ; DR O14230, FPPS_SCHPO; P08524, FPPS_YEAST; P34802, GGPP_ARATH; DR P56966, GGPP_BOVIN; P80042, GGPP_CAPAN; Q42698, GGPP_CATRO; DR Q92236, GGPP_GIBFU; O95749, GGPP_HUMAN; Q9WTN0, GGPP_MOUSE; DR Q50727, GGPP_MYCTU; P24322, GGPP_NEUCR; Q43133, GGPP_SINAL; DR P39464, GGPP_SULAC; P95999, GGPP_SULSO; Q58270, IDSA_METJA; DR O26156, IDSA_METTH; Q53479, IDSA_METTM; // ID 2.5.1.2 DE Thiamine pyridinylase. AN Pyrimidine transferase. AN Thiaminase I. AN Thiamin hydrolase. AN Thiamin pyridinolase. AN Thiaminase. AN Thiamine pyridinolase. AN Thiamin pyridinylase. AN Thiamin:base 2-methyl-4-aminopyrimidine-5-methenyltransferase. CA Thiamine + pyridine = 1-[(4-amino-2-methylpyrimidin-5- CA yl)methyl]pyridinium + 4-methyl-5-(2-hydroxyethyl)thiazole. CC -!- Various bases and thiol compounds can act instead of pyridine. DR P45741, THI1_PANTH; // ID 2.5.1.3 DE Thiamine-phosphate pyrophosphorylase. AN Thiamine-phosphate diphosphorylase. AN TMP pyrophosphorylase. AN TMP diphosphorylase. AN Thiamine-phosphate synthase. CA 2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-4-methyl-5- CA (2-phosphonooxyethyl)-thiazole = diphosphate + thiamine monophosphate. DR Q97RS5, THE1_STRPN; Q97RR8, THE2_STRPN; P40386, THI4_SCHPO; DR P41835, THI6_YEAST; Q8UAS8, THIE_AGRT5; Q8YX72, THIE_ANASP; DR O66833, THIE_AQUAE; O28205, THIE_ARCFU; Q9KCY8, THIE_BACHD; DR P39594, THIE_BACSU; Q9PNL3, THIE_CAMJE; Q8KD79, THIE_CHLTE; DR Q97LQ9, THIE_CLOAB; Q8XKQ8, THIE_CLOPE; Q8X6Y0, THIE_ECO57; DR Q8FB78, THIE_ECOL6; P30137, THIE_ECOLI; Q8RI59, THIE_FUSNN; DR P71350, THIE_HAEIN; Q9ZL01, THIE_HELPJ; O25514, THIE_HELPY; DR Q9CG48, THIE_LACLA; Q92EW5, THIE_LISIN; Q8YA44, THIE_LISMO; DR Q8TMD6, THIE_METAC; Q8PS49, THIE_METMA; Q9ZBL5, THIE_MYCLE; DR P96260, THIE_MYCTU; P57930, THIE_PASMU; Q9UZQ5, THIE_PYRAB; DR Q8U192, THIE_PYRFU; O58878, THIE_PYRHO; O34294, THIE_RHIET; DR Q8Z325, THIE_SALTI; Q9L9I8, THIE_SALTY; Q99SG6, THIE_STAAM; DR Q8NVH5, THIE_STAAW; Q8CNK2, THIE_STAEP; Q9S2V2, THIE_STRCO; DR P72965, THIE_SYNY3; Q9HIQ4, THIE_THEAC; Q97BE8, THIE_THEVO; DR Q87JW8, THIE_VIBPA; Q8ZAQ1, THIE_YERPE; // ID 2.5.1.4 DE Adenosylmethionine cyclotransferase. CA S-adenosyl-L-methionine = 5'-methylthioadenosine + 2-aminobutan-4-olide. // ID 2.5.1.5 DE Galactose-6-sulfurylase. AN Porphyran sulfatase. AN Galactose-6-sulfatase. CA Eliminates sulfur from the galactose 6-sulfate residues of porphyran CA producing 3,6-anhydrogalactose residues. // ID 2.5.1.6 DE Methionine adenosyltransferase. AN S-adenosylmethionine synthetase. AN Adomet synthetase. CA ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl- CA L-methionine. CC -!- Formerly EC 2.4.2.13. DI Hypermethioninemia due to methionine adenosyltransferase; MIM:250850. PR PROSITE; PDOC00369; DR Q95032, METK_ACACA; P50301, METK_ACTCH; Q9YBK2, METK_AERPE; DR O09486, METK_AMOPR; O67222, METK_AQUAE; P23686, METK_ARATH; DR O30186, METK_ARCFU; P50304, METK_ASCIM; Q9K7Q9, METK_BACHD; DR P54419, METK_BACSU; Q8G3H4, METK_BIFLO; O50163, METK_BORBU; DR P49611, METK_BRAJU; P57486, METK_BUCAI; Q8K9E5, METK_BUCAP; DR P50305, METK_CAEEL; Q96551, METK_CATRO; Q8KEG7, METK_CHLTE; DR Q97F85, METK_CLOAB; Q8FT48, METK_COREF; Q9K5E4, METK_CORGL; DR Q9RWM6, METK_DEIRA; P40320, METK_DROME; P04384, METK_ECOLI; DR Q8RGE5, METK_FUSNN; P43762, METK_HAEIN; Q9HQ73, METK_HALN1; DR Q9ZMN5, METK_HELPJ; P56460, METK_HELPY; P50299, METK_HORVU; DR P31153, METK_HUMAN; Q9CEE0, METK_LACLA; O43938, METK_LEIIN; DR Q92AZ5, METK_LISIN; Q8Y6M0, METK_LISMO; P43280, METK_LYCES; DR P80616, METK_MAIZE; P93254, METK_MESCR; Q8TU57, METK_METAC; DR Q58605, METK_METJA; Q8TV85, METK_METKA; Q8PWS4, METK_METMA; DR Q9HHD2, METK_METMP; O27429, METK_METTH; P26498, METK_METTM; DR O22338, METK_MUSAC; P47293, METK_MYCGE; Q9CCQ4, METK_MYCLE; DR P78003, METK_MYCPN; Q98PM0, METK_MYCPU; P77899, METK_MYCTU; DR Q9JVV6, METK_NEIMA; Q9JY09, METK_NEIMB; P48466, METK_NEUCR; DR Q8EP05, METK_OCEIH; P46611, METK_ORYSA; P57897, METK_PASMU; DR P49612, METK_PEA ; P31155, METK_PETCR; P48498, METK_PETHY; DR P50300, METK_PINBN; P47916, METK_POPDE; Q9I5Z0, METK_PSEAE; DR Q9V1P7, METK_PYRAB; Q8ZYP7, METK_PYRAE; Q8TZW1, METK_PYRFU; DR O59488, METK_PYRHO; Q8Y347, METK_RALSO; P18298, METK_RAT ; DR Q98A80, METK_RHILO; P56878, METK_RICPR; Q9RL99, METK_RICTY; DR Q8XF85, METK_SALTY; O60198, METK_SCHPO; Q8EIB4, METK_SHEON; DR Q99T79, METK_STAAM; P50307, METK_STAAU; Q8NVZ9, METK_STAAW; DR Q8CNT5, METK_STAEP; Q8E5Y0, METK_STRA3; Q8E0A3, METK_STRA5; DR Q9L0Y3, METK_STRCO; Q938W7, METK_STRFR; Q8DT23, METK_STRMU; DR Q8K715, METK_STRP3; Q8P0G6, METK_STRP8; Q97RN9, METK_STRPN; DR Q99Z77, METK_STRPY; Q8DQH0, METK_STRR6; Q9X4Q2, METK_STRST; DR Q980S9, METK_SULSO; Q976F3, METK_SULTO; Q8DK88, METK_SYNEL; DR P72871, METK_SYNY3; Q9HM12, METK_THEAC; Q9X1Y8, METK_THEMA; DR Q8RCE4, METK_THETN; Q97CT6, METK_THEVO; O83772, METK_TREPA; DR Q9KUP3, METK_VIBCH; Q87LK6, METK_VIBPA; Q8DCA3, METK_VIBVU; DR Q8D2N8, METK_WIGBR; Q8PP75, METK_XANAC; Q8PCH3, METK_XANCP; DR Q9PGB0, METK_XYLFA; Q87AY6, METK_XYLFT; P10659, METK_YEAST; DR Q8ZHG7, METK_YERPE; P50302, METL_ACTCH; O67275, METL_AQUAE; DR P17562, METL_ARATH; P50306, METL_CAEEL; Q96552, METL_CATRO; DR P24260, METL_DIACA; Q00266, METL_HUMAN; P43281, METL_LYCES; DR P93438, METL_ORYSA; P49613, METL_PEA ; P31156, METL_PETCR; DR P13444, METL_RAT ; P19358, METL_YEAST; P50303, METM_ACTCH; DR O17680, METM_CAEEL; Q96553, METM_CATRO; P43282, METM_LYCES; DR Q27522, METN_CAEEL; // ID 2.5.1.7 DE UDP-N-acetylglucosamine 1-carboxyvinyltransferase. AN Enoylpyruvate transferase. AN UDP-N-acetylglucosamine enolpyruvyl transferase. AN MurA transferase. AN UDP-N-acetylglucosamine 1-carboxyvinyl-transferase. AN Phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase. AN Phosphoenolpyruvate:UDP-2-acetamido-2-deoxy-D-glucose 2-enoyl-1- AN carboxyethyltransferase. AN Phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine AN enolpyruvyltransferase. AN Phosphoenolpyruvate:uridine-5'-diphospho-N-acetyl-2-amino-2- AN deoxyglucose 3-enolpyruvyltransferase. AN Phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase. AN Pyruvate-UDP-acetylglucosamine transferase. AN Pyruvate-uridine diphospho-N-acetylglucosamine transferase. AN Pyruvate-uridine diphospho-N-acetyl-glucosamine transferase. AN Pyruvic-uridine diphospho-N-acetylglucosaminyltransferase. CA Phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + CA UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine. DR Q9K6I0, MUA1_BACHD; P70965, MUA1_BACSU; Q97F79, MUA1_CLOAB; DR Q8XID7, MUA1_CLOPE; Q9CI17, MUA1_LACLA; Q927W7, MUA1_LISIN; DR Q8Y4C4, MUA1_LISMO; Q989E5, MUA1_RHILO; Q99SF8, MUA1_STAAN; DR Q8CRN6, MUA1_STAEP; Q8K825, MUA1_STRP3; Q97NQ4, MUA1_STRPN; DR Q9A0I4, MUA1_STRPY; Q8RD88, MUA1_THETN; Q9K6E5, MUA2_BACHD; DR P19670, MUA2_BACSU; Q97DD9, MUA2_CLOAB; Q8XH79, MUA2_CLOPE; DR Q9CIP4, MUA2_LACLA; Q927U1, MUA2_LISIN; Q8Y4A2, MUA2_LISMO; DR Q986Q6, MUA2_RHILO; Q99SD4, MUA2_STAAM; Q8NVG3, MUA2_STAAW; DR Q8CRM7, MUA2_STAEP; Q8P0G7, MUA2_STRP8; Q97QW6, MUA2_STRPN; DR Q99Z78, MUA2_STRPY; Q8R9G7, MUA2_THETN; Q8R6V0, MUA3_THETN; DR P33986, MURA_ACIGB; Q8UHW9, MURA_AGRT5; Q8Z0C4, MURA_ANASP; DR O67315, MURA_AQUAE; O51428, MURA_BORBU; Q8YF61, MURA_BRUME; DR P57466, MURA_BUCAI; Q8K9G4, MURA_BUCAP; Q89AE9, MURA_BUCBP; DR Q9PP65, MURA_CAMJE; Q9A5U7, MURA_CAUCR; Q9PJT7, MURA_CHLMU; DR Q9Z7Y2, MURA_CHLPN; Q8KEX7, MURA_CHLTE; O84461, MURA_CHLTR; DR Q8NML5, MURA_CORGL; Q9RVA6, MURA_DEIRA; Q9ZH21, MURA_DESTE; DR Q8X9J9, MURA_ECO57; P28909, MURA_ECOLI; P33038, MURA_ENTCL; DR Q8RIQ1, MURA_FUSNN; P45025, MURA_HAEIN; Q9ZLI6, MURA_HELPJ; DR P56189, MURA_HELPY; O32849, MURA_MYCAB; O32857, MURA_MYCCH; DR O32858, MURA_MYCFO; P45821, MURA_MYCLE; O33159, MURA_MYCNE; DR O33160, MURA_MYCPH; Q59561, MURA_MYCSM; Q10604, MURA_MYCTU; DR Q9JWS7, MURA_NEIMA; Q9K1Q9, MURA_NEIMB; P57821, MURA_PASMU; DR Q9HVW7, MURA_PSEAE; Q9Z3Z6, MURA_PSEPU; Q8XV78, MURA_RALSO; DR Q92S27, MURA_RHIME; Q92H88, MURA_RICCN; Q9ZCX3, MURA_RICPR; DR Q8XF63, MURA_SALTY; Q55673, MURA_SYNY3; Q9WXW3, MURA_THEMA; DR O54312, MURA_TREPA; Q9KP62, MURA_VIBCH; Q87LF4, MURA_VIBPA; DR Q8DEB6, MURA_VIBVU; Q8D2M5, MURA_WIGBR; Q8PID3, MURA_XANAC; DR Q8P719, MURA_XANCP; Q9PDG4, MURA_XYLFA; Q87DN8, MURA_XYLFT; DR Q8ZB56, MURA_YERPE; // ID 2.5.1.8 DE tRNA isopentenyltransferase. AN Isopentenyl-diphosphate:tRNA isopentenyltransferase. AN IPP transferase. CA Isopentenyl diphosphate + tRNA = diphosphate + tRNA containing CA 6-isopentenyladenosine. CC -!- Formerly EC 1.8.6.1. DR P38436, MIAA_AGRT5; Q8YLN2, MIAA_ANASP; O67162, MIAA_AQUAE; DR Q9KAC3, MIAA_BACHD; O31795, MIAA_BACSU; O51761, MIAA_BORBU; DR Q8YI29, MIAA_BRUME; P57632, MIAA_BUCAI; P59507, MIAA_BUCBP; DR Q9PIW2, MIAA_CAMJE; Q9A6J5, MIAA_CAUCR; Q9PLF7, MIAA_CHLMU; DR Q9Z6Z6, MIAA_CHLPN; Q8KDS2, MIAA_CHLTE; O84771, MIAA_CHLTR; DR Q97I21, MIAA_CLOAB; Q8XL85, MIAA_CLOPE; Q8NP72, MIAA_CORGL; DR Q9RTR6, MIAA_DEIRA; Q8XDN3, MIAA_ECO57; P16384, MIAA_ECOLI; DR Q8R5Z6, MIAA_FUSNN; P44495, MIAA_HAEIN; Q9ZJJ7, MIAA_HELPJ; DR O25961, MIAA_HELPY; Q9CHU2, MIAA_LACLA; Q92C59, MIAA_LISIN; DR Q8Y7I3, MIAA_LISMO; P46811, MIAA_MYCLE; O33232, MIAA_MYCTU; DR Q9JUU5, MIAA_NEIMA; Q9JZR0, MIAA_NEIMB; Q9CMC7, MIAA_PASMU; DR Q9HUL9, MIAA_PSEAE; O30762, MIAA_PSEPU; Q8XWB0, MIAA_RALSO; DR Q98KJ4, MIAA_RHILO; Q92NR2, MIAA_RHIME; Q92HW4, MIAA_RICCN; DR Q9ZD37, MIAA_RICPR; Q8Z186, MIAA_SALTI; P37724, MIAA_SALTY; DR P59197, MIAA_SHIFL; Q99UH0, MIAA_STAAM; O69967, MIAA_STRCO; DR Q8P1A9, MIAA_STRP3; Q97RW5, MIAA_STRPN; Q9A059, MIAA_STRPY; DR P74040, MIAA_SYNY3; Q9WYZ5, MIAA_THEMA; Q8R5S5, MIAA_THETN; DR O83644, MIAA_TREPA; Q9KV12, MIAA_VIBCH; Q87L06, MIAA_VIBPA; DR Q8CWK9, MIAA_VIBVU; Q8D318, MIAA_WIGBR; Q8PLQ5, MIAA_XANAC; DR Q8P9X8, MIAA_XANCP; Q9PH56, MIAA_XYLFA; Q87F70, MIAA_XYLFT; DR Q8ZIW3, MIAA_YERPE; Q9X5G1, MIAA_ZYMMO; P07884, MOD5_YEAST; // ID 2.5.1.9 DE Riboflavin synthase. CA 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D- CA ribitylamino)-5-amino-2,6-dihydroxypyrimidine. PR PROSITE; PDOC00581; DR Q9A9S4, RIB1_CAUCR; Q01994, RIB1_PHOLE; Q92QU0, RIB1_RHIME; DR Q9A8J4, RIB2_CAUCR; Q93E92, RIB2_PHOLE; Q92NI1, RIB2_RHIME; DR Q9UUB1, RIB4_SCHPO; P50861, RIB4_YEAST; P50854, RISA_ACTPL; DR O67604, RISA_AQUAE; Q44680, RISA_BACAM; P16440, RISA_BACSU; DR P57212, RISA_BUCAI; Q8KA22, RISA_BUCAP; Q9PJZ1, RISA_CHLMU; DR Q9Z820, RISA_CHLPN; O84410, RISA_CHLTR; P29015, RISA_ECOLI; DR P45273, RISA_HAEIN; P71680, RISA_MYCTU; Q01993, RISA_PHOLE; DR P51961, RISA_PHOPO; P38145, RISA_YEAST; P50856, RISB_ACTPL; DR Q9YC88, RISB_AERPE; O66529, RISB_AQUAE; O80575, RISB_ARATH; DR O28152, RISB_ARCFU; Q44681, RISB_BACAM; Q9KCL4, RISB_BACHD; DR P11998, RISB_BACSU; Q44668, RISB_BRUME; Q9ZNM0, RISB_BUCAI; DR Q8K9A6, RISB_BUCAP; Q89AB1, RISB_BUCBP; Q9PIB9, RISB_CAMJE; DR Q9PLJ4, RISB_CHLMU; Q9Z733, RISB_CHLPN; O84737, RISB_CHLTR; DR Q97LG8, RISB_CLOAB; O24753, RISB_CORAM; Q9RXZ8, RISB_DEIRA; DR P25540, RISB_ECOLI; P45149, RISB_HAEIN; Q9HRM5, RISB_HALN1; DR Q9ZN56, RISB_HELPJ; O24854, RISB_HELPY; Q9CGU6, RISB_LACLA; DR Q57751, RISB_METJA; O27443, RISB_METTH; Q9CCP3, RISB_MYCLE; DR P71685, RISB_MYCTU; Q9JQV6, RISB_NEIMA; P57869, RISB_PASMU; DR P51963, RISB_PHOPO; Q9HWX5, RISB_PSEAE; Q8ZTE3, RISB_PYRAE; DR Q8U4L8, RISB_PYRFU; Q986N2, RISB_RHILO; Q53107, RISB_RHOER; DR Q9XH32, RISB_SPIOL; Q931N8, RISB_STAAM; Q9EWJ9, RISB_STRCO; DR Q97SY8, RISB_STRPN; P73527, RISB_SYNY3; Q9X2E5, RISB_THEMA; DR Q9KPU4, RISB_VIBCH; Q8G9G4, RISB_VIBFI; Q87RU4, RISB_VIBPA; DR Q8DF99, RISB_VIBVU; Q8D291, RISB_WIGBR; Q9PES4, RISB_XYLFA; DR Q87AS7, RISB_XYLFT; Q9YDC5, RISC_AERPE; O28856, RISC_ARCFU; DR Q58584, RISC_METJA; O26237, RISC_METTH; Q59587, RISC_METTM; // ID 2.5.1.10 DE Geranyltranstransferase. AN Farnesyl-diphosphate synthase. AN Farnesyl pyrophosphate synthetase. AN Farnesyl diphosphate synthetase. AN FPP synthetase. CA Geranyl diphosphate + isopentenyl diphosphate = diphosphate + CA trans,trans-farnesyl diphosphate. CC -!- Some forms of this enzyme will also use dimethylallyl diphosphate CC as a substrate. CC -!- Will not accept larger prenyl diphosphates as efficient donors. PR PROSITE; PDOC00407; DR Q09152, FPP1_ARATH; P49351, FPP1_LUPAL; O24241, FPP1_PARAR; DR Q43315, FPP2_ARATH; P49352, FPP2_LUPAL; O24242, FPP2_PARAR; DR P49350, FPPS_ARTAN; P08836, FPPS_CHICK; Q92235, FPPS_GIBFU; DR O64905, FPPS_HELAN; P14324, FPPS_HUMAN; P49349, FPPS_KLULA; DR P49353, FPPS_MAIZE; Q92250, FPPS_NEUCR; P05369, FPPS_RAT ; DR O14230, FPPS_SCHPO; P08524, FPPS_YEAST; P34802, GGPP_ARATH; DR P56966, GGPP_BOVIN; P80042, GGPP_CAPAN; Q42698, GGPP_CATRO; DR Q92236, GGPP_GIBFU; O95749, GGPP_HUMAN; Q9WTN0, GGPP_MOUSE; DR Q50727, GGPP_MYCTU; P24322, GGPP_NEUCR; Q43133, GGPP_SINAL; DR P39464, GGPP_SULAC; P95999, GGPP_SULSO; Q58270, IDSA_METJA; DR O26156, IDSA_METTH; Q53479, IDSA_METTM; O66952, ISPA_AQUAE; DR Q08291, ISPA_BACST; P54383, ISPA_BACSU; Q45220, ISPA_BRAJA; DR P57537, ISPA_BUCAI; Q8K9A0, ISPA_BUCAP; P22939, ISPA_ECOLI; DR P45204, ISPA_HAEIN; O66126, ISPA_MICLU; P55539, ISPA_RHISN; // ID 2.5.1.11 DE Trans-octaprenyltranstransferase. AN All-trans-nonaprenyl-diphosphate synthase. AN Solanesyl-diphosphate synthase. CA All-trans-octaprenyl diphosphate + isopentenyl diphosphate = CA diphosphate + all-trans-nonaprenyl diphosphate. CC -!- Will also use geranyl diphosphate and all-trans-prenyl diphosphates CC of intermediate size as donors, but not dimethylallyl diphosphate. // ID 2.5.1.12 DE Transferred entry: 2.5.1.18. // ID 2.5.1.13 DE Transferred entry: 2.5.1.18. // ID 2.5.1.14 DE Transferred entry: 2.5.1.18. // ID 2.5.1.15 DE Dihydropteroate synthase. AN Dihydropteroate pyrophosphorylase. AN Dihydropteroate diphosphorylase. AN DHPS. CA 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate + CA 4-aminobenzoate = diphosphate + dihydropteroate. PR PROSITE; PDOC00630; DR P11744, DHP1_ECOLI; O06274, DHP1_MYCTU; P19539, DHP2_ECOLI; DR O05308, DHP2_MYCTU; P28822, DHPS_BACSU; Q05621, DHPS_CLOBE; DR P26282, DHPS_ECOLI; P43776, DHPS_HAEIN; P46812, DHPS_MYCLE; DR Q9JT70, DHPS_NEIMA; Q51161, DHPS_NEIMB; P57696, DHPS_NEIMC; DR O05701, DHPS_STAAU; Q59919, DHPS_STAHA; Q8K7K8, DHPS_STRP3; DR Q8P152, DHPS_STRP8; P05382, DHPS_STRPN; O33724, DHPS_STRPY; DR P59655, DHPS_STRR6; P73248, DHPS_SYNY3; P29251, FAS_PNECA ; DR P53848, FAS_YEAST ; P82602, FOKP_CHLMU; Q9Z7E8, FOKP_CHLPN; DR O84619, FOKP_CHLTR; // ID 2.5.1.16 DE Spermidine synthase. AN Putrescine aminopropyltransferase. AN Aminopropyltransferase. CA S-adenosylmethioninamine + putrescine = 5'-methylthioadenosine + CA spermidine. CC -!- The mammalian enzyme is highly specific but the bacterial enzyme can CC use other acceptors and can synthesize spermine. CC -!- Not identical with EC 2.5.1.22. PR PROSITE; PDOC01033; DR Q9ZUB3, SPD1_ARATH; Q96556, SPD1_DATST; O48658, SPD1_HYONI; DR Q9SMB1, SPD1_ORYSA; Q9ZTR1, SPD1_PEA ; O48661, SPD2_ARATH; DR Q96557, SPD2_DATST; O48659, SPD2_HYONI; Q9ZTR0, SPD2_PEA ; DR O82147, SPDE_COFAR; Q9ZS45, SPDE_LYCES; O48660, SPDE_NICSY; DR Q9YE02, SPEE_AERPE; O66473, SPEE_AQUAE; O27950, SPEE_ARCFU; DR Q9K6B8, SPEE_BACHD; P70998, SPEE_BACSU; P57305, SPEE_BUCAI; DR Q8K9T5, SPEE_BUCAP; Q97FX3, SPEE_CLOAB; Q8XMY8, SPEE_CLOPE; DR Q9XY92, SPEE_DICDI; Q8X951, SPEE_ECOL6; P09158, SPEE_ECOLI; DR P19623, SPEE_HUMAN; Q57761, SPEE_METJA; Q64674, SPEE_MOUSE; DR Q9Y8H7, SPEE_NEUCR; Q9X6R0, SPEE_PSEAE; Q9V277, SPEE_PYRAB; DR Q8U4G1, SPEE_PYRFU; O57950, SPEE_PYRHO; Q8Z9E2, SPEE_SALTI; DR Q8ZRS3, SPEE_SALTY; Q09741, SPEE_SCHPO; Q97RA7, SPEE_STRPN; DR Q9HL75, SPEE_THEAC; Q9WZC2, SPEE_THEMA; Q8RA94, SPEE_THETN; DR Q97BN7, SPEE_THEVO; Q8PFQ4, SPEE_XANAC; Q8P447, SPEE_XANCP; DR Q12074, SPEE_YEAST; Q8ZBJ8, SPEE_YERPE; // ID 2.5.1.17 DE Cob(I)alamin adenosyltransferase. AN Aquacob(I)alamin adenosyltransferase. CA ATP + cob(I)alamin + H(2)O = phosphate + diphosphate + adenosylcobalamin. CF Manganese. DR P13040, BTUR_ECOLI; P31570, BTUR_SALTY; P29930, COBO_PSEDE; DR P76554, EUTT_ECOLI; Q9ZFV4, EUTT_SALTY; // ID 2.5.1.18 DE Glutathione transferase. AN Glutathione S-alkyltransferase. AN Glutathione S-aryltransferase. AN S-(hydroxyalkyl)glutathione lyase. AN Glutathione S-aralkyltransferase. CA RX + glutathione = HX + R-S-glutathione. CC -!- A group of enzymes of broad specificity. CC -!- R may be an aliphatic, aromatic or heterocyclic group. CC -!- X may be a sulfate, nitrite or halide group. CC -!- Also catalyzes the addition of aliphatic epoxides and arene oxides CC to glutathione; the reduction of polyol nitrate by glutathione to CC polyol and nitrite; certain isomerization reactions and disulfide CC interchange. CC -!- Formerly EC 1.8.6.1, EC 2.5.1.12, EC 2.5.1.13, EC 2.5.1.14 and CC EC 4.4.1.7. DR P10620, GST1_HUMAN; P79382, GST1_PIG ; P08011, GST1_RAT ; DR Q99735, GST2_HUMAN; O14880, GST3_HUMAN; P57108, GSTZ_EUPES; DR O04437, GSTZ_WHEAT; P46434, GT1_ONCVO ; P30112, GT26_FASHE; DR P08515, GT26_SCHJA; P15964, GT26_SCHMA; P31670, GT27_FASHE; DR P35661, GT27_SCHMA; P31671, GT28_FASHE; P30113, GT28_SCHBO; DR P30114, GT28_SCHHA; P26624, GT28_SCHJA; P09792, GT28_SCHMA; DR P56598, GT29_FASHE; P82607, GT67_DICLA; P46435, GT6_SCHMA ; DR P82608, GT82_DICLA; P80894, GTA1_ANTST; Q28035, GTA1_BOVIN; DR P81706, GTA1_CAVPO; Q08392, GTA1_CHICK; P08263, GTA1_HUMAN; DR P13745, GTA1_MOUSE; P51781, GTA1_PIG ; Q08863, GTA1_RABIT; DR P00502, GTA1_RAT ; O18879, GTA2_BOVIN; Q08393, GTA2_CHICK; DR P09210, GTA2_HUMAN; P10648, GTA2_MOUSE; P04903, GTA2_RAT ; DR P26697, GTA3_CHICK; Q16772, GTA3_HUMAN; P14942, GTA3_RAT ; DR O15217, GTA4_HUMAN; P24472, GTA4_MOUSE; P30568, GTA_PLEPL ; DR P04904, GTC1_RAT ; P46418, GTC2_RAT ; P30115, GTC_MOUSE ; DR Q08862, GTC_RABIT ; P42760, GTH1_ARATH; P12653, GTH1_MAIZE; DR Q9Y7Q2, GTH1_SCHPO; P30109, GTH1_TOBAC; P30110, GTH1_WHEAT; DR P40582, GTH1_YEAST; O59827, GTH2_SCHPO; P46440, GTH2_TOBAC; DR P30111, GTH2_WHEAT; Q12390, GTH2_YEAST; P42761, GTH3_ARATH; DR P04907, GTH3_MAIZE; Q9P6M1, GTH3_SCHPO; P46422, GTH4_ARATH; DR P46420, GTH4_MAIZE; P42769, GTH5_ARATH; Q96266, GTH6_ARATH; DR Q96324, GTH7_ARATH; Q9SRY5, GTHB_ARATH; Q9SLM6, GTHC_ARATH; DR P48438, GTH_BRAOL ; P46423, GTH_HYOMU ; Q04522, GTH_SILCU ; DR Q9Y2Q3, GTK1_HUMAN; P24473, GTK1_RAT ; P46419, GTM1_DERPT; DR P09488, GTM1_HUMAN; P10649, GTM1_MOUSE; P04905, GTM1_RAT ; DR P20136, GTM2_CHICK; P28161, GTM2_HUMAN; P15626, GTM2_MOUSE; DR P08010, GTM2_RAT ; P21266, GTM3_HUMAN; P19639, GTM3_MOUSE; DR P08009, GTM3_RAT ; Q03013, GTM4_HUMAN; P46439, GTM5_HUMAN; DR P48774, GTM5_MOUSE; O35660, GTM6_MOUSE; P16413, GTMU_CAVPO; DR Q00285, GTMU_CRILO; P30116, GTMU_MESAU; P46409, GTMU_RABIT; DR P78417, GTO1_HUMAN; O09131, GTO1_MOUSE; Q9N1F5, GTO1_PIG ; DR Q9Z339, GTO1_RAT ; P81942, GTP1_BUFBU; P10299, GTP1_CAEEL; DR P46425, GTP1_MOUSE; P83325, GTP2_BUFBU; P19157, GTP2_MOUSE; DR P28801, GTP_BOVIN ; P46424, GTP_CRILO ; P47954, GTP_CRIMI ; DR P46426, GTP_DIRIM ; P09211, GTP_HUMAN ; Q28514, GTP_MACMU ; DR Q60550, GTP_MESAU ; P46427, GTP_ONCVO ; P80031, GTP_PIG ; DR P04906, GTP_RAT ; P46436, GTS1_ASCSU; O18598, GTS1_BLAGE; DR Q09607, GTS1_CAEEL; P41043, GTS1_DROME; P48429, GTS2_ASCSU; DR O16115, GTS2_CAEEL; P46429, GTS2_MANSE; O16116, GTS3_CAEEL; DR Q21355, GTS4_CAEEL; Q09596, GTS5_CAEEL; P20137, GTS5_CHICK; DR P91252, GTS6_CAEEL; P91253, GTS7_CAEEL; P91254, GTS8_CAEEL; DR Q21743, GTS9_CAEEL; Q9N4X8, GTSA_CAEEL; P46428, GTS_ANOGA ; DR P83246, GTS_ASADI ; P46437, GTS_MUSDO ; P46088, GTS_OMMSL ; DR Q94999, GTT1_ANOGA; P20135, GTT1_CHICK; P30104, GTT1_DROER; DR P30105, GTT1_DROMA; P20432, GTT1_DROME; P30106, GTT1_DROSE; DR P30107, GTT1_DROTE; P30108, GTT1_DROYA; P30711, GTT1_HUMAN; DR P42860, GTT1_LUCCU; P46430, GTT1_MANSE; Q64471, GTT1_MOUSE; DR P28338, GTT1_MUSDO; Q01579, GTT1_RAT ; Q9VG98, GTT2_DROME; DR P30712, GTT2_HUMAN; Q61133, GTT2_MOUSE; P46431, GTT2_MUSDO; DR P30713, GTT2_RAT ; Q9VG97, GTT3_DROME; P46432, GTT3_MUSDO; DR Q9VG96, GTT4_DROME; P46433, GTT4_MUSDO; Q93112, GTT5_ANOGA; DR Q9VG95, GTT5_DROME; Q93113, GTT6_ANOGA; Q9VG94, GTT6_DROME; DR Q9VG93, GTT7_DROME; P50471, GTX1_NICPL; P32111, GTX1_SOLTU; DR Q03662, GTX1_TOBAC; P50472, GTX2_MAIZE; Q03663, GTX2_TOBAC; DR Q03664, GTX3_TOBAC; Q03666, GTX4_TOBAC; P32110, GTX6_SOYBN; DR P46421, GTXA_ARATH; P25317, GTXA_TOBAC; Q06398, GTXC_ORYSA; DR P49332, GTXC_TOBAC; P30102, GTY2_ISSOR; Q9ZVQ3, GTZ1_ARATH; DR P28342, GTZ1_DIACA; Q9ZVQ4, GTZ2_ARATH; Q03425, GTZ2_DIACA; DR P39100, GT_ECOLI ; P44521, GT_HAEIN ; P81065, GT_OCHAN ; DR P15214, GT_PROMI ; P22416, GT_SERMA ; P45875, GT_XANCP ; DR O43708, MAAI_HUMAN; Q9WVL0, MAAI_MOUSE; P57113, MAAI_RAT ; // ID 2.5.1.19 DE 3-phosphoshikimate 1-carboxyvinyltransferase. AN 5-enolpyruvylshikimate-3-phosphate synthase. AN EPSP synthase. AN 3-enol-pyruvoylshikimate-5-phosphate synthase. CA Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O- CA (1-carboxyvinyl)-3-phosphoshikimate. PR PROSITE; PDOC00097; DR Q9KCA6, ARA1_BACHD; Q9L213, ARA1_STRCO; Q9K9D5, ARA2_BACHD; DR Q9K4A7, ARA2_STRCO; P07547, ARO1_EMENI; Q12659, ARO1_PNECA; DR Q9P7R0, ARO1_SCHPO; P23981, ARO1_TOBAC; P08566, ARO1_YEAST; DR P23281, ARO2_TOBAC; Q9YEK9, AROA_AERPE; Q03321, AROA_AERSA; DR Q9R4E4, AROA_AGRSP; Q8YMB5, AROA_ANASP; O67494, AROA_AQUAE; DR P05466, AROA_ARATH; O28775, AROA_ARCFU; Q46550, AROA_BACNO; DR P20691, AROA_BACSU; Q9RND7, AROA_BORBR; P12421, AROA_BORPE; DR Q89WF2, AROA_BRAJA; P17688, AROA_BRANA; Q9AGV2, AROA_BRUAB; DR Q8YEG1, AROA_BRUME; Q8G3C4, AROA_BRUSU; P57396, AROA_BUCAI; DR Q59178, AROA_BUCAP; P59416, AROA_BUCBP; P39915, AROA_BURPS; DR P52312, AROA_CAMJE; Q9A2H2, AROA_CAUCR; Q9PK28, AROA_CHLMU; DR Q9Z6M0, AROA_CHLPN; Q8KB71, AROA_CHLTE; O84371, AROA_CHLTR; DR Q97KM2, AROA_CLOAB; Q8XMJ2, AROA_CLOPE; Q894D2, AROA_CLOTE; DR Q8FRI2, AROA_COREF; Q9Z470, AROA_CORGL; Q9RVD3, AROA_DEIRA; DR Q8FJB6, AROA_ECOL6; P07638, AROA_ECOLI; Q9X4H2, AROA_EDWIC; DR Q03421, AROA_HAEIN; P52310, AROA_HAESO; Q9HQC1, AROA_HALN1; DR Q9ZKF7, AROA_HELPJ; P56197, AROA_HELPY; P24497, AROA_KLEPN; DR Q9CEU0, AROA_LACLA; P43905, AROA_LACLC; Q88VL2, AROA_LACPL; DR Q8F6P5, AROA_LEPIN; Q92A85, AROA_LISIN; Q8Y5Y0, AROA_LISMO; DR P10748, AROA_LYCES; Q8THH3, AROA_METAC; Q57925, AROA_METJA; DR Q8TXN4, AROA_METKA; Q8PXI0, AROA_METMA; O26860, AROA_METTH; DR Q9CCI3, AROA_MYCLE; P22487, AROA_MYCTU; Q9JTT3, AROA_NEIMA; DR Q9JYU1, AROA_NEIMB; Q8EQC1, AROA_OCEIH; P54220, AROA_PASHA; DR Q04570, AROA_PASMU; Q8VP65, AROA_PASPI; P11043, AROA_PETHY; DR P56952, AROA_PSES2; Q9V1H1, AROA_PYRAB; Q8U0A0, AROA_PYRFU; DR Q8Y0Y6, AROA_RALSO; Q98CC1, AROA_RHILO; Q92SV5, AROA_RHIME; DR P22299, AROA_SALGL; P19786, AROA_SALTI; P07637, AROA_SALTY; DR Q8EEH8, AROA_SHEON; O87006, AROA_SHIDY; Q9ZFF7, AROA_SHISO; DR Q99U25, AROA_STAAM; Q05615, AROA_STAAU; Q8NWN5, AROA_STAAW; DR Q8CSI1, AROA_STAEP; Q8E6F8, AROA_STRA3; Q8E0U0, AROA_STRA5; DR Q8DUV8, AROA_STRMU; Q8K719, AROA_STRP3; Q8P0H1, AROA_STRP8; DR Q9S400, AROA_STRPN; Q99Z83, AROA_STRPY; Q8CWQ7, AROA_STRR6; DR Q980I5, AROA_SULSO; Q96Y91, AROA_SULTO; Q8DLY3, AROA_SYNEL; DR Q59975, AROA_SYNY3; Q9HLE6, AROA_THEAC; Q9WYI0, AROA_THEMA; DR Q8RB11, AROA_THETN; Q978S3, AROA_THEVO; Q9KRB0, AROA_VIBCH; DR Q87QX9, AROA_VIBPA; Q8PLY5, AROA_XANAC; Q8PA95, AROA_XANCP; DR Q8RLV9, AROA_XENNE; Q9PB21, AROA_XYLFA; Q87BU2, AROA_XYLFT; DR P19688, AROA_YEREN; Q60112, AROA_YERPE; Q93ED4, AROA_YERRU; // ID 2.5.1.20 DE Rubber cis-polyprenylcistransferase. AN Rubber allyltransferase. AN Rubber transferase. CA Poly-cis-polyprenyl diphosphate + isopentenyl diphosphate = CA diphosphate + a poly-cis-polyprenyl diphosphate longer by one C5 unit. CC -!- Rubber particles act as acceptor. // ID 2.5.1.21 DE Farnesyl-diphosphate farnesyltransferase. AN Farnesyltransferase. AN Presqualene-di-diphosphate synthase. AN Squalene synthase. CA 2 farnesyl diphosphate = diphosphate + presqualene diphosphate. CC -!- The polymeric form of the enzyme also catalyzes the reduction of CC presqualene diphosphate by NADPH to squalene. PR PROSITE; PDOC00802; DR P53799, FDFT_ARATH; P78589, FDFT_CANAL; Q9HGZ6, FDFT_CANGA; DR P37268, FDFT_HUMAN; P53798, FDFT_MOUSE; P53800, FDFT_NICBE; DR Q02769, FDFT_RAT ; P36596, FDFT_SCHPO; Q92459, FDFT_USTMA; DR P29704, FDFT_YEAST; // ID 2.5.1.22 DE Spermine synthase. AN Spermidine aminopropyltransferase. CA S-adenosylmethioninamine + spermidine = 5'-methylthioadenosine + CA spermine. CC -!- Not identical with EC 2.5.1.16 or EC 2.5.1.23. PR PROSITE; PDOC01033; DR P52788, SPSY_HUMAN; P97355, SPSY_MOUSE; Q12455, SPSY_YEAST; // ID 2.5.1.23 DE Sym-norspermidine synthase. CA S-adenosylmethioninamine + propane-1,3-diamine = 5'-methylthioadenosine + CA bis(3-aminopropyl)amine. CC -!- Not identical with EC 2.5.1.16 or EC 2.5.1.22. // ID 2.5.1.24 DE Discadenine synthase. CA S-adenosyl-L-methionine + N(6)-(delta(2)-isopentenyl)adenine = CA 5'-methylthioadenosine + discadenine. CC -!- Discadenine is 3-(3-amino-3-carboxypropyl)-N(6)-(delta(2)- CC isopentenyl)-adenine. // ID 2.5.1.25 DE tRNA-uridine aminocarboxypropyltransferase. CA S-adenosyl-L-methionine + tRNA uridine = 5'-methylthioadenosine + tRNA CA 3-(3-amino-3-carboxypropyl)-uridine. // ID 2.5.1.26 DE Alkylglycerone-phosphate synthase. AN Alkyldihydroxyacetonephosphate synthase. AN Alkyl-DHAP synthase. CA 1-acyl-glycerone 3-phosphate + a long-chain alcohol = 1-alkyl-glycerone CA 3-phosphate + a long-chain acid anion. CC -!- The ester-linked fatty acid of the substrate is cleaved and replaced CC by a long-chain alcohol in an ether linkage. DI Alkylglycerone-phosphate synthase deficiency; MIM:600121. DR O45218, ADAS_CAEEL; P97275, ADAS_CAVPO; O96759, ADAS_DICDI; DR Q9V778, ADAS_DROME; O00116, ADAS_HUMAN; O97157, ADAS_TRYBB; // ID 2.5.1.27 DE Adenylate dimethylallyltransferase. AN Cytokinin synthase. AN Isopentenyltransferase. CA Dimethylallyl diphosphate + AMP = diphosphate + N(6)- CA (dimethylallyl)adenosine 5'-phosphate. // ID 2.5.1.28 DE Dimethylallylcistransferase. AN Neryl-diphosphate synthase. CA Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + CA neryl diphosphate. CC -!- Will not use larger prenyl diphosphates as efficient donors. // ID 2.5.1.29 DE Farnesyltranstransferase. AN Geranylgeranyl-diphosphate synthase. CA Trans-trans-farnesyl diphosphate + isopentenyl diphosphate = CA diphosphate + geranylgeranyl diphosphate. CC -!- Some forms of this enzyme will also use geranyl diphosphate and CC dimethylallyl diphosphate as donors; it will not use larger prenyl CC diphosphates as efficient donors. PR PROSITE; PDOC00407; DR P48368, CRTE_CYAPA; P22873, CRTE_ERWHE; P21684, CRTE_PANAN; DR P17060, CRTE_RHOCA; P54976, CRTE_RHOSH; P34802, GGPP_ARATH; DR P56966, GGPP_BOVIN; P80042, GGPP_CAPAN; Q42698, GGPP_CATRO; DR Q92236, GGPP_GIBFU; O95749, GGPP_HUMAN; Q9WTN0, GGPP_MOUSE; DR Q50727, GGPP_MYCTU; P24322, GGPP_NEUCR; Q43133, GGPP_SINAL; DR P39464, GGPP_SULAC; P95999, GGPP_SULSO; // ID 2.5.1.30 DE Trans-hexaprenyltranstransferase. AN All-trans-heptaprenyl-diphosphate synthase. AN Heptaprenyl diphosphate synthase. AN Heptaprenyl pyrophosphate synthetase. CA All-trans-hexaprenyl diphosphate + isopentenyl diphosphate = CA diphosphate + all-trans-heptaprenyl diphosphate. CC -!- Will also use trans-trans-farnesyl diphosphate and all-trans-prenyl CC diphosphates of intermediate size as donors, but not dimethylallyl CC diphosphate. DR P55784, HEP1_BACST; P31112, HEP1_BACSU; P55785, HEP2_BACST; DR P31114, HEP2_BACSU; // ID 2.5.1.31 DE Di-trans-poly-cis-decaprenylcistransferase. AN Di-trans-poly-cis-undecaprenyl-diphosphate synthase. AN Undecaprenyl pyrophosphate synthetase. AN Undecaprenyl pyrophosphate synthase. AN UPP synthetase. AN Undecaprenyl-diphosphate synthase. AN Bactoprenyl-diphosphate synthase. CA Di-trans-poly-cis-decaprenyl diphosphate + isopentenyl diphosphate = CA diphosphate + di-trans-poly-cis-undecaprenyl diphosphate. CC -!- Will also use trans,trans-farnesyl diphosphate and di-trans,poly- CC cis-prenyl diphosphates of intermediate size as donors. CC -!- The two trans bonds in the substrate and product are those furthest CC from the diphosphate group. PR PROSITE; PDOC00817; DR P58563, UPPS_ANASP; Q9ZEJ7, UPPS_ANAVA; O67291, UPPS_AQUAE; DR O29049, UPPS_ARCFU; Q9KA67, UPPS_BACHD; O31751, UPPS_BACSU; DR O51146, UPPS_BORBU; P57330, UPPS_BUCAI; Q8K9S6, UPPS_BUCAP; DR Q9PJU2, UPPS_CHLMU; Q9Z7Y7, UPPS_CHLPN; O84456, UPPS_CHLTR; DR Q47675, UPPS_ECOLI; P44938, UPPS_HAEIN; Q9ZK05, UPPS_HELPJ; DR P55984, UPPS_HELPY; Q58767, UPPS_METJA; O26334, UPPS_METTH; DR O82827, UPPS_MICLU; P38119, UPPS_MYCLE; O05837, UPPS_MYCTU; DR Q9V157, UPPS_PYRAB; O59258, UPPS_PYRHO; Q9ZDA7, UPPS_RICPR; DR Q55482, UPPS_SYNY3; O83612, UPPS_TREPA; // ID 2.5.1.32 DE Geranylgeranyl-diphosphate geranylgeranyltransferase. AN Prephytoene-diphosphate synthase. CA 2 geranylgeranyl diphosphate = diphosphate + prephytoene diphosphate. // ID 2.5.1.33 DE Trans-pentaprenyltransferase. AN All-trans-hexaprenyl-diphosphate synthase. CA All-trans-pentaprenyl diphosphate + isopentenyl diphosphate = CA diphosphate + all-trans-hexaprenyl diphosphate. CC -!- Will also use trans,trans-farnesyl diphosphate and all-trans- CC geranylgeranyl diphosphate as donors. // ID 2.5.1.34 DE Tryptophan dimethylallyltransferase. CA Dimethylallyl diphosphate + L-tryptophan = diphosphate + CA 4-(3-methylbut-2-enyl)-L-tryptophan. // ID 2.5.1.35 DE Aspulvinone dimethylallyltransferase. CA 2 dimethylallyl diphosphate + aspulvinone E = 2 diphosphate + CA aspulvinone H. CC -!- Will also use as acceptor aspulvinone G, a hydroxylated derivative CC of the complex phenolic pigment aspulvinone E. // ID 2.5.1.36 DE Trihydroxypterocarpan dimethylallyltransferase. AN Glyceollin synthase. CA Dimethylallyl diphosphate + (6AS,11AS)-3,6A,9-trihydroxypterocarpan = CA diphosphate + glyceollin. CC -!- Part of the glyceollin biosynthesis system in soybean. // ID 2.5.1.37 DE Leukotriene-C4 synthase. CA Leukotriene A4 + glutathione = leukotriene C4 + H(2)O. CC -!- Not identical with EC 2.5.1.8. PR PROSITE; PDOC00999; DR Q16873, LC4S_HUMAN; Q60860, LC4S_MOUSE; // ID 2.5.1.38 DE Isonocardicin synthase. CA S-adenosyl-L-methionine + nocardicin E = 5'-methylthioadenosine + CA isonocardicin A. CC -!- Involved in the biosynthesis of the beta-lactam antibiotic CC nocardicin A. // ID 2.5.1.39 DE 4-hydroxybenzoate nonaprenyltransferase. CA Solanesyl diphosphate + 4-hydroxybenzoate = diphosphate + CA nonaprenyl-4-hydroxybenzoate. CC -!- Involved in the biosynthesis of ubiquinone. // ID 2.5.1.40 DE Transferred entry: 4.2.3.9. // ID 2.5.1.41 DE Phosphoglycerol geranylgeranyltransferase. CA Geranylgeranyl diphosphate + sn-glyceryl phosphate = diphosphate + CA sn-3-O-(geranylgeranyl)glyceryl 1-phosphate. // ID 2.5.1.42 DE Geranylgeranylglycerol-phosphate geranylgeranyltransferase. CA Geranylgeranyl diphosphate + sn-3-O-(geranylgeranyl)glycerol 1-phosphate CA = diphosphate + 2,3-bis-O-(geranylgeranyl)glycerol 1-phosphate. // ID 2.5.1.43 DE Nicotianamine synthase. CA 3 S-adenosyl-L-methionine = 3 5'-S-methyl-5'-thioadenosine + CA nicotianamine. DR Q9FF79, NAS1_ARATH; Q9ZQV9, NAS1_HORVU; Q9SXQ7, NAS1_ORYSA; DR Q9FKT9, NAS2_ARATH; Q9ZQV7, NAS2_HORVU; Q9FEG8, NAS2_ORYSA; DR O80483, NAS3_ARATH; Q9ZQV8, NAS3_HORVU; Q9FXW5, NAS3_ORYSA; DR Q9C7X5, NAS4_ARATH; Q9ZQV6, NAS4_HORVU; Q9ZQV3, NAS6_HORVU; DR Q9ZWH8, NAS7_HORVU; Q9XFB6, NAS8_HORVU; Q9XFB7, NAS9_HORVU; DR Q9XGI7, NAS_LYCES ; // ID 2.5.1.44 DE Homospermidine synthase. CA 2 putrescine = sym-homospermidine + NH(3). CF NAD. CC -!- The reaction of this enzyme occurs in three steps: CC (1) NAD-dependent dehydrogenation of putrescine. CC (2) Transfer of the 4-aminobutylidene group from dehydroputrescine CC to a second molecule of putrescine. CC (3) Reduction of the imine intermediate to form homospermidine. CC -!- Hence the overall reaction is transfer of a 4-aminobutyl group. CC -!- In the presence of putrescine, spermidine can function as a donor CC of the aminobutyl group, in which case, propane-1,3-diamine is CC released instead of ammonia. CC -!- Differs from EC 2.5.1.45, which cannot use putrescine as donor of CC the aminobutyl group. DR Q98H64, HSS_RHILO ; O32323, HSS_RHOVI ; // ID 2.5.1.45 DE Homospermidine synthase (spermidine-specific). CA Spermidine + putrescine = sym-homospermidine + propane-1,3-diamine. CF NAD. CC -!- The reaction of this enzyme occurs in three steps: CC (1) NAD-dependent dehydrogenation of spermidine. CC (2) Transfer of the 4-aminobutylidene group from dehydrospermidine CC to a second molecule of putrescine. CC (3) Reduction of the imine intermediate to form homospermidine. CC -!- Hence the overall reaction is transfer of a 4-aminobutyl group. CC -!- This enzyme is more specific than EC 2.5.1.44 which is found in CC bacteria, as it cannot use putrescine as donor of the 4-aminobutyl CC group. CC -!- Forms part of the biosynthetic pathway of the poisonous CC pyrrolizidine alkaloids of the ragworts (Senecio). // ID 2.5.1.46 DE Deoxyhypusine synthase. AN [eIF-5A]-deoxyhypusine synthase. AN Spermidine dehydrogenase. AN (4-aminobutyl)lysine synthase. CA [eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]- CA deoxyhypusine + propane-1,3-diamine. CF NAD. CC -!- The eukaryotic initiation factor eIF5A contains a hypusine residue CC that is essential for activity. CC -!- This enzyme catalyzes the first reaction of hypusine formation CC from one specific lysine residue of the eIF5A precursor, the CC second reaction being catalyzed by EC 1.14.99.29. CC -!- The reaction of this enzyme occurs in four steps: CC (1) NAD-dependent dehydrogenation of spermidine. CC (2) Formation of an enzyme-imine intermediate by transfer of the CC 4-aminobutylidene group from dehydrospermidine to the active CC site lysine residue. CC (3) Transfer of the same 4-aminobutylidene group from the enzyme CC intermediate to the e1F5A precursor. CC (4) Reduction of the e1F5A-imine intermediate to form a CC deoxyhypusine residue. CC -!- Hence the overall reaction is transfer of a 4-aminobutyl group. CC -!- For the plant enzyme, homospermidine can substitute for spermidine CC and putrescine can substitute for the lysine residue of the eIF5A CC precursor. CC -!- Formerly EC 1.1.1.249. DR O28088, DHY1_ARCFU; Q8TS38, DHY1_METAC; Q8PV89, DHY1_METMA; DR O27984, DHY2_ARCFU; Q8TLM3, DHY2_METAC; Q8Q051, DHY2_METMA; DR Q9YE72, DHYS_AERPE; Q9XXJ0, DHYS_CAEEL; Q9VSF4, DHYS_DROME; DR Q9HPX2, DHYS_HALN1; P49366, DHYS_HUMAN; Q58224, DHYS_METJA; DR Q8TXD7, DHYS_METKA; Q977X6, DHYS_METTE; O26230, DHYS_METTH; DR P49365, DHYS_NEUCR; Q9V0N5, DHYS_PYRAB; Q8ZT09, DHYS_PYRAE; DR Q8U407, DHYS_PYRFU; O50105, DHYS_PYRHO; O94337, DHYS_SCHPO; DR Q97ZF1, DHYS_SULSO; Q971T3, DHYS_SULTO; Q9HL74, DHYS_THEAC; DR Q97BN6, DHYS_THEVO; P38791, DHYS_YEAST; // ID 2.5.1.47 DE Cysteine synthase. AN O-acetylserine (thiol)-lyase. AN O-acetylserine sulfhydrylase. AN OAS sulfhydrylase. AN O-acetyl-L-serine sulfhydrylase. AN O-acetyl-L-serine sulfohydrolase. AN O-acetylserine (thiol)-lyase A. AN O(3)-acetyl-L-serine acetate-lyase (adding hydrogen-sulfide). AN Acetylserine sulfhydrylase; cysteine synthetase. CA O(3)-acetyl-L-serine + H(2)S = L-cysteine + acetate. CF Pyridoxal-phosphate. CC -!- Some alkyl thiols, cyanide, pyrazole and some other heterocyclic CC compounds can act as acceptors. CC -!- Not identical with EC 2.5.1.51, EC 2.5.1.52 and EC 2.5.1.53. CC -!- Formerly EC 4.2.99.8. PR PROSITE; PDOC00700; DR O23733, CYK1_BRAJU; Q9XEA6, CYK1_ORYSA; O23735, CYK2_BRAJU; DR Q9XEA8, CYK2_ORYSA; P47998, CYSK_ARATH; P37887, CYSK_BACSU; DR P57171, CYSK_BUCAI; Q8KA48, CYSK_BUCAP; Q43317, CYSK_CITLA; DR P81340, CYSK_CLOPA; P11096, CYSK_ECOLI; P50867, CYSK_EMENI; DR Q59447, CYSK_FLASP; P45040, CYSK_HAEIN; P80608, CYSK_MAIZE; DR O32978, CYSK_MYCLE; P95230, CYSK_MYCTU; P12674, CYSK_SALTY; DR P87131, CYSK_SCHPO; O81154, CYSK_SOLTU; Q00834, CYSK_SPIOL; DR Q59918, CYSK_STAHA; P73410, CYSK_SYNY3; P38076, CYSK_WHEAT; DR P53206, CYSK_YEAST; P47999, CYSL_ARATH; P31300, CYSL_CAPAN; DR O81155, CYSL_SOLTU; P32260, CYSL_SPIOL; Q44004, CYSM_ALCEU; DR O67507, CYSM_AQUAE; Q43725, CYSM_ARATH; O34476, CYSM_BACSU; DR P71128, CYSM_CAMJE; P16703, CYSM_ECOLI; Q9ZMW6, CYSM_HELPJ; DR P56067, CYSM_HELPY; Q10624, CYSM_MYCTU; P48028, CYSM_PSESY; DR P29848, CYSM_SALTY; O22682, CYSN_ARATH; Q92441, MT17_KLULA; DR P06106, MT17_YEAST; Q59966, SRPG_SYNP7; P55708, Y4XP_RHISN; // ID 2.5.1.48 DE Cystathionine gamma-synthase. AN O-succinyl-L-homoserine succinate-lyase (adding cysteine). AN O-succinylhomoserine (thiol)-lyase. AN Homoserine O-transsuccinylase. AN O-succinylhomoserine synthase. AN O-succinylhomoserine synthetase. AN Cystathionine synthase. AN Cystathionine synthetase. AN Homoserine transsuccinylase. CA O-succinyl-L-homoserine + L-cysteine = cystathionine + succinate. CF Pyridoxal-phosphate. CC -!- Also reacts with H(2)S and methanethiol as replacing agents, CC producing homocysteine and methionine, respectively. CC -!- In the absence of thiol, can also catalyze beta,gamma-elimination CC to form 2-oxobutanoate, succinate and ammonia. CC -!- Formerly EC 4.2.99.9. PR PROSITE; PDOC00677; DR P38675, MET7_NEUCR; O74314, MET7_SCHPO; P47164, MET7_YEAST; DR P55217, METB_ARATH; P00935, METB_ECOLI; P44502, METB_HAEIN; DR Q9ZMW7, METB_HELPJ; P56069, METB_HELPY; P24601, METB_HERAU; DR P46807, METB_MYCLE; O53427, METB_MYCTU; Q12198, METW_YEAST; DR Q04533, METX_YEAST; // ID 2.5.1.49 DE O-acetylhomoserine aminocarboxypropyltransferase. AN Methionine synthase. AN O-acetyl-L-homoserine sulfhydrolase. AN OAH sulfhydrylase. AN O-acetyl-L-homoserine acetate-lyase (adding methanethiol). AN O-acetylhomoserine (thiol)-lyase. AN O-acetylhomoserine sulfhydrolase. CA O-acetyl-L-homoserine + methanethiol = L-methionine + acetate. CC -!- Also reacts with other thiols and H(2)S, producing homocysteine or CC thioethers. CC -!- The name methionine synthase is more commonly applied to CC EC 2.1.1.13. CC -!- The enzyme from baker's yeast also catalyzes the reaction of CC EC 2.5.1.47, but more slowly. CC -!- Formerly EC 4.2.99.10. PR PROSITE; PDOC00677; DR Q92441, MT17_KLULA; P06106, MT17_YEAST; // ID 2.5.1.50 DE Zeatin 9-aminocarboxyethyltransferase. AN Beta-(9-cytokinin)-alanine synthase. AN Beta-(9-cytokinin)alanine synthase. AN O-acetyl-L-serine acetate-lyase (adding N(6)-substituted adenine). AN Lupinate synthetase. AN Lupinic acid synthase. AN Lupinic acid synthetase. CA O-acetyl-L-serine + zeatin = lupinate + acetate. CC -!- The enzyme acts not only on zeatin but also on other N(6)- CC substituted adenines. CC -!- The reaction destroys their cytokinin activity and forms the CC corresponding 3-(adenin-9-yl)-L-alanine. CC -!- Formerly EC 4.2.99.13. // ID 2.5.1.51 DE Beta-pyrazolylalanine synthase. AN Beta-(1-pyrazolyl)alanine synthase. AN Beta-pyrazolealanine synthase. AN Beta-pyrazolylalanine synthase (acetylserine). AN O(3)-acetyl-L-serine acetate-lyase (adding pyrazole). AN BPA-synthase. AN Pyrazolealanine synthase. AN Pyrazolylalaninase. CA O-acetyl-L-serine + pyrazole = 3-(pyrazol-1-yl)-L-alanine + acetate. CC -!- The enzyme is highly specific for acetylserine and pyrazole. CC -!- Not identical with EC 2.5.1.52. CC -!- Formerly EC 4.2.99.14 and EC 4.2.99.17. DR Q43317, CYSK_CITLA; // ID 2.5.1.52 DE L-mimosine synthase. AN O(3)-acetyl-L-serine acetate-lyase (adding 3,4-dihydroxypyridin-1-yl). CA O(3)-acetyl-L-serine + 3,4-dihydroxypyridine = 3-(3,4-dihydroxypyridin- CA 1-yl)-L-alanine + acetate. CC -!- Brings about the biosynthesis of L-mimosine in Mimosa and Leucaena sp. CC -!- Not identical with EC 2.5.1.51. CC -!- Formerly EC 4.2.99.15. DR Q43317, CYSK_CITLA; // ID 2.5.1.53 DE Uracilylalanine synthase. AN O(3)-acetyl-L-serine acetate-lyase (adding uracil). AN Isowillardiine synthase. AN Willardiine synthase. CA O(3)-acetyl-L-serine + uracil = 3-(uracil-1-yl)-L-alanine + acetate. CC -!- Both L-willardiine and L-isowillardiine are produced in the reaction. CC -!- Not identical with EC 2.5.1.47. CC -!- Formerly EC 4.2.99.16. // ID 2.5.1.54 DE 3-deoxy-7-phosphoheptulonate synthase. AN 2-dehydro-3-deoxy-phosphoheptonate aldolase. AN 2-keto-3-deoxy-D-arabino-heptonic acid 7-phosphate synthetase. AN 3-deoxy-D-arabino-2-heptulosonic acid 7-phosphate synthetase. AN 3-deoxy-D-arabino-heptolosonate-7-phosphate synthetase. AN 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase. AN 7-phospho-2-keto-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate AN lyase (pyruvate-phosphorylating). AN 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate D-erythrose-4-phosphate AN lyase (pyruvate-phosphorylating). AN D-erythrose-4-phosphate-lyase. AN D-erythrose-4-phosphate-lyase (pyruvate-phosphorylating). AN DAH7-P synthase. AN DAHP synthase. AN DHAP synthase. AN DS-Co. AN DS-Mn. AN KDPH synthase. AN KDPH synthetase. AN Deoxy-D-arabino-heptulosonate-7-phosphate synthetase. AN Phospho-2-dehydro-3-deoxyheptonate aldolase. AN Phospho-2-keto-3-deoxyheptanoate aldolase. AN Phospho-2-keto-3-deoxyheptonate aldolase. AN Phospho-2-keto-3-deoxyheptonic aldolase. AN Phospho-2-oxo-3-deoxyheptonate aldolase. CA Phosphoenolpyruvate + D-erythrose 4-phosphate + H(2)O = 3-deoxy-D- CA erythro-hept-2-ulosonate 7-phosphate + phosphate. CC -!- Formerly EC 4.1.2.15. DR P29976, AROF_ARATH; P34725, AROF_CANAL; P00888, AROF_ECOLI; DR Q02285, AROF_ERWHE; P37215, AROF_LYCES; P80576, AROF_NEUCR; DR P21307, AROF_SALTY; Q09755, AROF_SCHPO; P21357, AROF_SOLTU; DR P80574, AROF_STRCO; P55911, AROF_STRLI; P80575, AROF_STRRM; DR P27608, AROF_TOBAC; P14843, AROF_YEAST; Q44093, AROG_AMYME; DR Q00218, AROG_ARATH; P39912, AROG_BACSU; P79023, AROG_CANAL; DR P35170, AROG_CORGL; P00886, AROG_ECOLI; P44303, AROG_HAEIN; DR P37216, AROG_LYCES; P37822, AROG_SOLTU; P32449, AROG_YEAST; DR P57224, AROH_BUCAI; P46245, AROH_BUCAP; Q8X5W4, AROH_ECO57; DR Q8FH32, AROH_ECOL6; P00887, AROH_ECOLI; O54459, AROH_ERWHE; DR Q8Z6I9, AROH_SALTI; Q8ZPS4, AROH_SALTY; P59736, AROH_SHIFL; DR Q51517, PHZC_PSECL; Q51789, PHZC_PSEFL; // ID 2.5.1.55 DE 3-deoxy-8-phosphooctulonate synthase. AN 2-dehydro-3-deoxy-phosphooctonate aldolase. AN 2-dehydro-3-deoxy-D-octonate-8-phosphate D-arabinose-5-phosphate-lyase AN (pyruvate-phosphorylating). AN 2-keto-3-deoxy-8-phosphooctonic synthetase. AN 3-deoxy-D-manno-octulosonate-8-phosphate synthase. AN 3-deoxy-D-manno-octulosonic acid 8-phosphate synthetase. AN 3-deoxy-D-mannooctulosonate-8-phosphate synthetase. AN 3-deoxyoctulosonic 8-phosphate synthetase. AN KDOP synthase. AN KDO-8-P synthase. AN KDO-8-phosphate synthetase. AN Phospho-2-keto-3-deoxyoctonate aldolase. CA Phosphoenolpyruvate + D-arabinose 5-phosphate + H(2)O = CA 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate. CC -!- Formerly EC 4.1.2.16. DR O68662, KDSA_ACTPL; Q8UFH3, KDSA_AGRT5; O66496, KDSA_AQUAE; DR Q9AV97, KDSA_ARATH; Q89KV0, KDSA_BRAJA; Q8YHF1, KDSA_BRUME; DR Q8G0G2, KDSA_BRUSU; Q9PIB8, KDSA_CAMJE; Q9A8C5, KDSA_CAUCR; DR Q9PLS0, KDSA_CHLMU; Q9Z7I4, KDSA_CHLPN; Q46225, KDSA_CHLPS; DR P77849, KDSA_CHLTR; Q8XDE7, KDSA_ECO57; Q8FHZ8, KDSA_ECOL6; DR P17579, KDSA_ECOLI; Q8RE91, KDSA_FUSNN; P45251, KDSA_HAEIN; DR Q9ZN55, KDSA_HELPJ; P56060, KDSA_HELPY; Q9JU48, KDSA_NEIMA; DR Q9JZ55, KDSA_NEIMB; P95514, KDSA_PASHA; P57853, KDSA_PASMU; DR O50044, KDSA_PEA ; Q9ZFK4, KDSA_PSEAE; Q88MG0, KDSA_PSEPK; DR Q886M4, KDSA_PSESM; Q8Y0B7, KDSA_RALSO; Q98MZ6, KDSA_RHILO; DR Q92Q99, KDSA_RHIME; Q92JH7, KDSA_RICCN; Q9ZE84, KDSA_RICPR; DR Q8XGR9, KDSA_SALTY; Q9KQ29, KDSA_VIBCH; Q87RN0, KDSA_VIBPA; DR Q8DFG3, KDSA_VIBVU; Q8PLS2, KDSA_XANAC; Q8P9Z5, KDSA_XANCP; DR Q9PDU0, KDSA_XYLFA; Q87DY7, KDSA_XYLFT; Q8ZEX4, KDSA_YERPE; // ID 2.5.1.56 DE N-acetylneuraminate synthase. AN N-acetylneuraminic acid synthase. AN (NANA)condensing enzyme. AN N-acetylneuraminate pyruvate-lyase (pyruvate-phosphorylating). AN NeuAc synthase. CA Phosphoenolpyruvate + N-acetyl-D-mannosamine + H(2)O = phosphate + CA N-acetylneuraminate. CC -!- Formerly EC 4.1.3.19. DR Q9NR45, SIAS_HUMAN; // ID 2.5.1.57 DE N-acylneuraminate-9-phosphate synthase. AN N-acetylneuraminate 9-phosphate lyase. AN N-acetylneuraminate 9-phosphate sialic acid 9-phosphate synthase. AN N-acetylneuraminate 9-phosphate synthetase. AN N-acylneuraminate-9-phosphate pyruvate-lyase (pyruvate-phosphorylating). AN Sialic acid 9-phosphate synthetase. CA Phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H(2)O = CA N-acylneuraminate 9-phosphate + phosphate. CC -!- Acts on N-glycoloyl and N-acetyl-derivatives. CC -!- Formerly EC 4.1.3.20. DR Q9NR45, SIAS_HUMAN; // ID 2.6.1.1 DE Aspartate aminotransferase. AN Transaminase A. AN Glutamic--oxaloacetic transaminase. AN Glutamic--aspartic transaminase. CA L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. CF Pyridoxal-phosphate. CC -!- Also acts on L-tyrosine, L-phenylalanine and L-tryptophan. This CC activity can be formed from EC 2.6.1.57 by controlled proteolysis. PR PROSITE; PDOC00098; DR P58350, AAB1_RHIME; Q06191, AAB2_RHIME; P46643, AAT1_ARATH; DR P53001, AAT1_BACSU; P28011, AAT1_MEDSA; Q60317, AAT1_METJA; DR P46645, AAT2_ARATH; P39643, AAT2_BACSU; Q58097, AAT2_METJA; DR P46644, AAT3_ARATH; P46646, AAT4_ARATH; P46248, AAT5_ARATH; DR Q02635, AATA_RHIME; P33097, AATC_BOVIN; Q22067, AATC_CAEEL; DR P00504, AATC_CHICK; P28734, AATC_DAUCA; P08906, AATC_HORSE; DR P17174, AATC_HUMAN; P05201, AATC_MOUSE; P37833, AATC_ORYSA; DR P00503, AATC_PIG ; P12343, AATC_RABIT; P13221, AATC_RAT ; DR P23542, AATC_YEAST; P12344, AATM_BOVIN; P00508, AATM_CHICK; DR P08907, AATM_HORSE; P00505, AATM_HUMAN; P26563, AATM_LUPAN; DR P05202, AATM_MOUSE; P00506, AATM_PIG ; P12345, AATM_RABIT; DR P00507, AATM_RAT ; Q01802, AATM_YEAST; O67781, AAT_AQUAE ; DR P23034, AAT_BACSP ; Q59228, AAT_BACST ; P00509, AAT_ECOLI ; DR P44425, AAT_HAEIN ; P52069, AAT_METEX ; O33267, AAT_MYCTU ; DR P72173, AAT_PSEAE ; Q9V0L2, AAT_PYRAB ; O58489, AAT_PYRHO ; DR O93744, AAT_PYRKO ; O86459, AAT_RHILP ; Q92JE7, AAT_RICCN ; DR Q9ZE56, AAT_RICPR ; Q56114, AAT_SALTI ; P58661, AAT_SALTY ; DR P36692, AAT_STRGR ; Q60013, AAT_STRVG ; P14909, AAT_SULSO ; DR Q55128, AAT_SYNY3 ; O33822, AAT_THEAQ ; Q9X0Y2, AAT_THEMA ; DR Q56232, AAT_THETH ; // ID 2.6.1.2 DE Alanine aminotransferase. AN Glutamic--pyruvic transaminase. AN Glutamic--alanine transaminase. CA L-alanine + 2-oxoglutarate = pyruvate + L-glutamate. CF Pyridoxal-phosphate. CC -!- 2-aminobutanoate acts slowly instead of alanine. DR P52894, ALA2_HORVU; P34106, ALA2_PANMI; P52893, ALAM_YEAST; DR P24298, ALAT_HUMAN; P13191, ALAT_PIG ; P25409, ALAT_RAT ; DR Q10334, ALAT_SCHPO; P52892, ALAT_YEAST; // ID 2.6.1.3 DE Cysteine aminotransferase. CA L-cysteine + 2-oxoglutarate = mercaptopyruvate + L-glutamate. CF Pyridoxal-phosphate. // ID 2.6.1.4 DE Glycine aminotransferase. CA Glycine + 2-oxoglutarate = glyoxylate + L-glutamate. CF Pyridoxal-phosphate. // ID 2.6.1.5 DE Tyrosine aminotransferase. AN Tyrosine transaminase. CA L-tyrosine + 2-oxoglutarate = 4-hydroxyphenylpyruvate + L-glutamate. CF Pyridoxal-phosphate. CC -!- L-phenylalanine can act instead of L-tyrosine. CC -!- The mitochondrial enzyme may be identical with EC 2.6.1.1. CC -!- The three isoenzymic forms are interconverted by EC 3.4.22.4. DI Tyrosinemia II (Richner-Hanhart syndrome); MIM:276600. PR PROSITE; PDOC00098; DR P17735, ATTY_HUMAN; P04694, ATTY_RAT ; Q02636, ATTY_RHIME; DR P33447, ATTY_TRYCR; // ID 2.6.1.6 DE Leucine aminotransferase. CA L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. CF Pyridoxal-phosphate. // ID 2.6.1.7 DE Kynurenine--oxoglutarate aminotransferase. AN Kynurenine aminotransferase. CA L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + CA L-glutamate. CF Pyridoxal-phosphate. CC -!- Also acts on 3-hydroxykynurenine. // ID 2.6.1.8 DE 2,5-diaminovalerate aminotransferase. AN Diamino-acid aminotransferase. CA 2,5-diaminopentanoate + 2-oxoglutarate = 5-amino-2-oxopentanoate + CA L-glutamate. CF Pyridoxal-phosphate. CC -!- 2,5-diaminoglutarate can act instead of diaminopentanoate. // ID 2.6.1.9 DE Histidinol-phosphate aminotransferase. AN Imidazolylacetolphosphate aminotransferase. AN Imidazole acetol-phosphate transaminase. CA L-histidinol-phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2- CA oxopropyl phosphate + L-glutamate. CF Pyridoxal-phosphate. PR PROSITE; PDOC00518; DR Q8YV89, HI81_ANASP; O28277, HI81_ARCFU; Q9A671, HI81_CAUCR; DR P44423, HI81_HAEIN; O06591, HI81_MYCTU; Q9CLM3, HI81_PASMU; DR Q9HVX0, HI81_PSEAE; Q8XV80, HI81_RALSO; Q987C8, HI81_RHILO; DR Q92MG0, HI81_RHIME; P16246, HI81_STRCO; Q8YMG7, HI82_ANASP; DR O28255, HI82_ARCFU; Q9A5B6, HI82_CAUCR; Q57004, HI82_HAEIN; DR P72039, HI82_MYCTU; Q9CMI7, HI82_PASMU; Q9HZ68, HI82_PSEAE; DR Q8Y0Y8, HI82_RALSO; Q98G10, HI82_RHILO; Q92L21, HI82_RHIME; DR Q9ZBY8, HI82_STRCO; Q98B00, HI83_RHILO; Q930J0, HI83_RHIME; DR P45358, HIS8_ACEPA; Q8U9W3, HIS8_AGRT5; O67857, HIS8_AQUAE; DR Q9KCA8, HIS8_BACHD; P17731, HIS8_BACSU; Q8YJK3, HIS8_BRUME; DR P57202, HIS8_BUCAI; Q9ZHE5, HIS8_BUCAP; Q9PII2, HIS8_CAMJE; DR P56099, HIS8_CANMA; Q8KD01, HIS8_CHLTE; Q97ES6, HIS8_CLOAB; DR Q9KJU4, HIS8_CORGL; Q9RRM7, HIS8_DEIRA; Q9S5G6, HIS8_ECO57; DR P06986, HIS8_ECOLI; Q9HQS0, HIS8_HALN1; P17736, HIS8_HALVO; DR Q02135, HIS8_LACLA; Q92A83, HIS8_LISIN; Q8Y5X8, HIS8_LISMO; DR Q8TUE9, HIS8_METAC; O07131, HIS8_METFL; Q58365, HIS8_METJA; DR Q8TVG3, HIS8_METKA; Q8PX17, HIS8_METMA; O27624, HIS8_METTH; DR Q9X7B8, HIS8_MYCLE; P28735, HIS8_MYCSM; Q9JTH8, HIS8_NEIMA; DR Q9JYH7, HIS8_NEIMB; Q51687, HIS8_PARDE; Q9RI00, HIS8_PSEST; DR Q8TH25, HIS8_PYRFU; P55683, HIS8_RHISN; Q8Z5J9, HIS8_SALTI; DR P10369, HIS8_SALTY; P36605, HIS8_SCHPO; Q99VP9, HIS8_STAAM; DR Q8NXN3, HIS8_STAAW; O33770, HIS8_SULSO; Q970Z4, HIS8_SULTO; DR P73807, HIS8_SYNY3; Q9X0D0, HIS8_THEMA; Q9L6I2, HIS8_THIRO; DR Q9KSX2, HIS8_VIBCH; P58891, HIS8_XANAC; P58892, HIS8_XANCP; DR Q9PBC6, HIS8_XYLFA; Q87C30, HIS8_XYLFT; P07172, HIS8_YEAST; DR Q8ZFX6, HIS8_YERPE; P34037, HIS8_ZYMMO; Q8R5Q4, HISC_THETN; // ID 2.6.1.10 DE Transferred entry: 2.6.1.21. // ID 2.6.1.11 DE Acetylornithine aminotransferase. CA N(2)-acetyl-L-ornithine + 2-oxoglutarate = N-acetyl-L-glutamate CA 5-semialdehyde + L-glutamate. CF Pyridoxal-phosphate. PR PROSITE; PDOC00519; DR Q9YBY6, ARGD_AERPE; Q8UI71, ARGD_AGRT5; O04866, ARGD_ALNGL; DR P54752, ARGD_ANASP; O66442, ARGD_AQUAE; O30156, ARGD_ARCFU; DR Q9ZJ10, ARGD_BACAM; Q9K8V5, ARGD_BACHD; Q07907, ARGD_BACST; DR P36839, ARGD_BACSU; P59315, ARGD_BIFLO; Q8YFA1, ARGD_BRUME; DR P57600, ARGD_BUCAI; P59086, ARGD_BUCAP; Q9PIR7, ARGD_CAMJE; DR Q9A652, ARGD_CAUCR; P59316, ARGD_CHLTE; Q97GH9, ARGD_CLOAB; DR Q59282, ARGD_CORGL; Q9RW75, ARGD_DEIRA; Q8X4S6, ARGD_ECO57; DR P59317, ARGD_ECOL6; P18335, ARGD_ECOLI; O14433, ARGD_KLULA; DR Q9CHD3, ARGD_LACLA; O08321, ARGD_LACPL; P24087, ARGD_LEPIN; DR Q92BC0, ARGD_LISIN; Q8Y6U4, ARGD_LISMO; Q8TUE8, ARGD_METAC; DR Q58131, ARGD_METJA; Q8TUZ5, ARGD_METKA; Q8PX16, ARGD_METMA; DR O27392, ARGD_METTH; Q9CC12, ARGD_MYCLE; P94990, ARGD_MYCTU; DR P59318, ARGD_MYXXA; Q9JTX9, ARGD_NEIMA; Q9JYY4, ARGD_NEIMB; DR Q9CNT1, ARGD_PASMU; P59319, ARGD_PSEPK; Q9V1I4, ARGD_PYRAB; DR Q8ZV07, ARGD_PYRAE; Q8U0B4, ARGD_PYRFU; O59401, ARGD_PYRHO; DR Q8XWN8, ARGD_RALSO; Q98BB7, ARGD_RHILO; Q92SA0, ARGD_RHIME; DR P30900, ARGD_RHOCA; Q8Z1Z3, ARGD_SALTI; P40732, ARGD_SALTY; DR O74548, ARGD_SCHPO; P59320, ARGD_SHEON; P59321, ARGD_SHIFL; DR Q99X36, ARGD_STAAM; Q8NYM5, ARGD_STAAW; Q9LCS5, ARGD_STRCL; DR Q9L1A4, ARGD_STRCO; Q59928, ARGD_STRMU; Q980W6, ARGD_SULSO; DR Q976K0, ARGD_SULTO; P59322, ARGD_SYNEL; P73133, ARGD_SYNY3; DR Q9X2A5, ARGD_THEMA; Q93R93, ARGD_THETH; Q8R7C1, ARGD_THETN; DR Q9KNW2, ARGD_VIBCH; P59323, ARGD_VIBVU; Q8PH31, ARGD_XANAC; DR Q8P5Q4, ARGD_XANCP; Q9PDF2, ARGD_XYLFA; Q87DM8, ARGD_XYLFT; DR P18544, ARGD_YEAST; P59324, ARGD_YERPE; O30508, ARUC_PSEAE; // ID 2.6.1.12 DE Alanine--oxo-acid aminotransferase. CA L-alanine + a 2-oxo acid = pyruvate + an L-amino acid. CF Pyridoxal-phosphate. // ID 2.6.1.13 DE Ornithine--oxo-acid aminotransferase. AN Ornithine aminotransferase. AN Ornithine ketoacid aminotransferase. CA L-ornithine + a 2-oxo acid = L-glutamate 5-semialdehyde + an L-amino CA acid. CF Pyridoxal-phosphate. DI Ornithinemia with gyrate atrophy of choroid and retina; MIM:258870. PR PROSITE; PDOC00519; DR P38021, OAT_BACSU ; Q18040, OAT_CAEEL ; P49724, OAT_DROAN ; DR Q9VW26, OAT_DROME ; P42588, OAT_ECOLI ; Q92413, OAT_EMENI ; DR P04181, OAT_HUMAN ; P29758, OAT_MOUSE ; Q07805, OAT_PLAFD ; DR P04182, OAT_RAT ; Q9P7L5, OAT_SCHPO ; P31893, OAT_VIGAC ; DR P07991, OAT_YEAST ; // ID 2.6.1.14 DE Asparagine--oxo-acid aminotransferase. CA L-asparagine + a 2-oxo acid = 2-oxosuccinamate + an amino acid. CF Pyridoxal-phosphate. // ID 2.6.1.15 DE Glutamine--pyruvate aminotransferase. AN Glutaminase II. AN Glutamine--oxo-acid transaminase. AN Glutamine transaminase L. CA L-glutamine + pyruvate = 2-oxoglutaramate + L-alanine. CF Pyridoxal-phosphate. CC -!- L-methionine can act as donor. CC -!- Glyoxylate can act as acceptor. // ID 2.6.1.16 DE Glutamine-fructose-6-phosphate transaminase (isomerizing). AN Glucosamine--fructose-6-phosphate aminotransferase (isomerizing). AN Hexosephosphate aminotransferase. AN D-fructose-6-phosphate amidotransferase. AN Glucosamine-6-phosphate isomerase (glutamine-forming). AN L-glutamine-d-fructose-6-phosphate amidotransferase. AN Glucosamine-6-phosphate synthase. AN GlcN6P synthase. CA L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine CA 6-phosphate. CC -!- Although the overall reaction is that of a transferase, the CC mechanism involves the formation of ketimine between fructose CC 6-phosphate and a 6-amino group from a lysine residue at the CC active site, which is subsequently displaced by ammonia CC (transamidination). CC -!- Formerly EC 5.3.1.19. PR PROSITE; PDOC00406; DR P53704, GFA1_CANAL; Q06210, GFA1_HUMAN; P47856, GFA1_MOUSE; DR Q09740, GFA1_SCHPO; P14742, GFA1_YEAST; O94808, GFA2_HUMAN; DR Q9Z2Z9, GFA2_MOUSE; Q9YCQ6, GLMS_AERPE; Q8UEH1, GLMS_AGRT5; DR O66648, GLMS_AQUAE; Q9KG45, GLMS_BACHD; P39754, GLMS_BACSU; DR Q8AAB1, GLMS_BACTN; P59362, GLMS_BRAJA; Q8YC47, GLMS_BRUME; DR Q8CY30, GLMS_BRUSU; P57138, GLMS_BUCAI; Q8KA75, GLMS_BUCAP; DR P59499, GLMS_BUCBP; Q9PMT4, GLMS_CAMJE; Q9ABV2, GLMS_CAUCR; DR Q9PLA4, GLMS_CHLMU; Q9Z6U0, GLMS_CHLPN; Q8KG38, GLMS_CHLTE; DR O84823, GLMS_CHLTR; Q97MN6, GLMS_CLOAB; Q8XHZ7, GLMS_CLOPE; DR Q890U2, GLMS_CLOTE; Q8FNH2, GLMS_COREF; Q8NND3, GLMS_CORGL; DR O19908, GLMS_CYACA; Q8XEG2, GLMS_ECO57; Q8FBT4, GLMS_ECOL6; DR P17169, GLMS_ECOLI; Q8RG65, GLMS_FUSNN; P44708, GLMS_HAEIN; DR Q9HT00, GLMS_HALN1; Q9ZJ94, GLMS_HELPJ; O26060, GLMS_HELPY; DR Q9CGT6, GLMS_LACLA; Q88YE7, GLMS_LACPL; Q8EZQ1, GLMS_LEPIN; DR Q92DS8, GLMS_LISIN; Q8Y915, GLMS_LISMO; Q8TLL3, GLMS_METAC; DR Q8TZ14, GLMS_METKA; Q8Q038, GLMS_METMA; O26273, GLMS_METTH; DR P40831, GLMS_MYCLE; O68956, GLMS_MYCSM; O06253, GLMS_MYCTU; DR Q9JWN9, GLMS_NEIMA; Q9K1P9, GLMS_NEIMB; O68280, GLMS_NOSS9; DR Q8ETM5, GLMS_OCEIH; P57963, GLMS_PASMU; Q9HT25, GLMS_PSEAE; DR Q88BX8, GLMS_PSEPK; Q87TT8, GLMS_PSESM; Q9V249, GLMS_PYRAB; DR Q8ZTZ0, GLMS_PYRAE; Q8U4D1, GLMS_PYRFU; O57981, GLMS_PYRHO; DR Q8Y303, GLMS_RALSO; Q98LX5, GLMS_RHILO; Q92PS4, GLMS_RHIME; DR Q8Z2Q2, GLMS_SALTI; Q8ZKX1, GLMS_SALTY; Q8CX33, GLMS_SHEON; DR Q56206, GLMS_SPHYA; Q99SA5, GLMS_STAAM; Q8NVE6, GLMS_STAAW; DR Q8CRL1, GLMS_STAEP; Q8E5P8, GLMS_STRA3; Q8DZZ7, GLMS_STRA5; DR O86781, GLMS_STRCO; Q8DTY0, GLMS_STRMU; Q8P0S7, GLMS_STRP8; DR Q97SQ9, GLMS_STRPN; Q99ZD3, GLMS_STRPY; Q8DRA8, GLMS_STRR6; DR Q8DJI6, GLMS_SYNEL; P72720, GLMS_SYNY3; Q9WXZ5, GLMS_THEMA; DR Q56213, GLMS_THETH; Q8R841, GLMS_THETN; Q56275, GLMS_THIFE; DR O83833, GLMS_TREPA; Q9KUM8, GLMS_VIBCH; Q87SR3, GLMS_VIBPA; DR Q8DEF3, GLMS_VIBVU; Q8D3J0, GLMS_WIGBR; Q8PGH9, GLMS_XANAC; DR Q8PCY1, GLMS_XANCP; Q9PH05, GLMS_XYLFA; Q87F28, GLMS_XYLFT; DR Q8Z9S8, GLMS_YERPE; P94323, NODM_BRAJA; Q52846, NODM_RHILT; DR P08633, NODM_RHILV; Q92ZK3, NOM1_RHIME; P25195, NOM2_RHIME; // ID 2.6.1.17 DE Succinyldiaminopimelate aminotransferase. AN Succinyldiaminopimelate transferase. CA N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl- CA L-2-amino-6-oxoheptanedioate + L-glutamate. CF Pyridoxal-phosphate. PR PROSITE; PDOC00094; DR P57600, ARGD_BUCAI; P59086, ARGD_BUCAP; Q8X4S6, ARGD_ECO57; DR P59317, ARGD_ECOL6; P18335, ARGD_ECOLI; Q8Z1Z3, ARGD_SALTI; DR P40732, ARGD_SALTY; P59321, ARGD_SHIFL; P59324, ARGD_YERPE; // ID 2.6.1.18 DE Beta-alanine--pyruvate aminotransferase. AN Omega-amino acid--pyruvate aminotransferase. CA L-alanine + 3-oxopropanoate = pyruvate + beta-alanine. CF Pyridoxal-phosphate. DR P28269, OAPT_PSEPU; // ID 2.6.1.19 DE 4-aminobutyrate aminotransferase. AN Gamma-amino-N-butyrate transaminase. AN GABA transaminase. AN Beta-alanine--oxoglutarate aminotransferase. CA 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + CA L-glutamate. CC -!- Some preparations also act on beta-alanine, 5-aminopentanoate and CC (R,S)-3-amino-2-methylpropanoate. DI GABA-transaminase deficiency; MIM:137150. PR PROSITE; PDOC00519; DR P94427, GABT_BACSU; Q9BGI0, GABT_BOVIN; Q21217, GABT_CAEEL; DR P22256, GABT_ECOLI; P80404, GABT_HUMAN; P40829, GABT_MYCLE; DR Q50632, GABT_MYCTU; P80147, GABT_PIG ; P50554, GABT_RAT ; DR P14010, GATA_EMENI; O13837, GATA_SCHPO; P49604, GATA_USTMA; DR P17649, GATA_YEAST; P50457, GOAG_ECOLI; // ID 2.6.1.20 DE Deleted entry. // ID 2.6.1.21 DE D-alanine aminotransferase. AN D-aspartate aminotransferase. AN D-amino acid aminotransferase. AN D-amino acid transaminase. CA D-alanine + 2-oxoglutarate = pyruvate + D-glutamate. CF Pyridoxal-phosphate. CC -!- Acts on the D-isomers of leucine, aspartate, glutamate, CC aminobutyrate, norvaline and asparagine. CC -!- Formerly EC 2.6.1.10. PR PROSITE; PDOC00618; DR P54692, DAAA_BACLI; P54693, DAAA_BACSH; P19938, DAAA_BACSP; DR O07597, DAAA_BACSU; Q92B90, DAAA_LISIN; O85046, DAAA_LISMO; DR P54694, DAAA_STAHA; // ID 2.6.1.22 DE (S)-3-amino-2-methylpropionate aminotransferase. AN L-3-aminoisobutyrate aminotransferase. CA (S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3- CA oxopropanoate + L-glutamate. CC -!- Also acts on beta-alanine and other omega-amino acids having carbon CC chains between 2 and 5. CC -!- Not identical with EC 2.6.1.61. // ID 2.6.1.23 DE 4-hydroxyglutamate aminotransferase. CA 4-hydroxy-L-glutamate + 2-oxoglutarate = 4-hydroxy-2-oxoglutarate + CA L-glutamate. CC -!- Oxaloacetate can replace 2-oxoglutarate. CC -!- May be identical with EC 2.6.1.1. // ID 2.6.1.24 DE Diiodotyrosine aminotransferase. CA 3,5-diiodo-L-tyrosine + 2-oxoglutarate = 3,5-diiodo-4- CA hydroxyphenylpyruvate + L-glutamate. CF Pyridoxal-phosphate. CC -!- Also acts on 3,5-dichloro-, 3,5-dibromo- and 3-iodo-L-tyrosine, CC thyroxine and triiodothyronine. CC -!- Formerly EC 2.6.1.25. // ID 2.6.1.25 DE Transferred entry: 2.6.1.24. // ID 2.6.1.26 DE Thyroid-hormone aminotransferase. AN 3,5-dinitrotyrosine aminotransferase. CA L-3,5,3'-triiodothyronine + 2-oxoglutarate = 3,5,3'- CA triiodophenylpyruvate + L-glutamate. CF Pyridoxal-phosphate. CC -!- Acts on monoiodotyrosine, diiodotyrosine, triiodothyronine, thyroxine CC and dinitrotyrosine (unlike EC 2.6.1.24, which does not act on CC dinitrotyrosine). CC -!- Pyruvate or oxaloacetate can act as acceptor. // ID 2.6.1.27 DE Tryptophan aminotransferase. CA L-tryptophan + 2-oxoglutarate = indole-3-pyruvate + L-glutamate. CF Pyridoxal-phosphate. CC -!- Also acts on 5-hydroxytryptophan and, to a lesser extent on the CC phenyl amino acids. // ID 2.6.1.28 DE Tryptophan--phenylpyruvate aminotransferase. CA L-tryptophan + phenylpyruvate = indole-3-pyruvate + L-phenylalanine. CC -!- Valine, leucine and isoleucine can replace tryptophan as amino donor. // ID 2.6.1.29 DE Diamine aminotransferase. CA An alpha,omega-diamine + 2-oxoglutarate = an omega-aminoaldehyde + CA L-glutamate. // ID 2.6.1.30 DE Pyridoxamine--pyruvate aminotransferase. AN Pyridoxamine-pyruvic transaminase. CA Pyridoxamine + pyruvate = pyridoxal + L-alanine. CF Pyridoxal-phosphate. // ID 2.6.1.31 DE Pyridoxamine--oxaloacetate aminotransferase. CA Pyridoxamine + oxaloacetate = pyridoxal + L-aspartate. // ID 2.6.1.32 DE Valine--3-methyl-2-oxovalerate aminotransferase. AN Valine--isoleucine transaminase. AN Valine--isoleucine aminotransferase. CA L-valine + (S)-3-methyl-2-oxopentanoate = 3-methyl-2-butanoate + CA L-isoleucine. DI Valinemia; MIM:277100. // ID 2.6.1.33 DE dTDP-4-amino-4,6-dideoxy-D-glucose aminotransferase. AN Thymidine diphospho-4-keto-6-deoxy-D-glucose transaminase. AN Thymidine diphospho-4-keto-6-deoxy-D-glucose-glutamic transaminase. AN TDP-4-keto-6-deoxy-D-glucose transaminase. CA dTDP-4-amino-4,6-dideoxy-D-glucose + 2-oxoglutarate = CA dTDP-4-dehydro-6-deoxy-D-glucose + L-glutamate. CF Pyridoxal-phosphate. // ID 2.6.1.34 DE UDP-4-amino-2-acetamido-2,4,6-trideoxyglucose aminotransferase. CA UDP-2-acetamido-4-amino-2,4,6-trideoxyglucose + 2-oxoglutarate = CA UDP-2-acetamido-4-dehydro-2,6-dideoxyglucose + L-glutamate. CF Pyridoxal-phosphate. // ID 2.6.1.35 DE Glycine--oxaloacetate aminotransferase. CA Glycine + oxaloacetate = glyoxylate + L-aspartate. CF Pyridoxal-phosphate. // ID 2.6.1.36 DE L-lysine aminotransferase. AN Lysine-epsilon aminotransferase. CA L-lysine + 2-oxoglutarate = 2-aminoadipate 6-semialdehyde + L-glutamate. CF Pyridoxal-phosphate. CC -!- The product (allysine) is converted into the intramolecularly CC dehydrated form, 1-piperideine 6-carboxylate. DR P96895, LAT_MYCTU ; Q05174, LAT_NOCLA ; Q01767, LAT_STRCL ; // ID 2.6.1.37 DE 2-aminoethylphosphonate--pyruvate transaminase. AN (2-aminoethyl)phosphonate transaminase. AN (2-aminoethyl)phosphonate--pyruvate aminotransferase. AN (2-aminoethyl)phosphonic acid aminotransferase. AN 2-aminoethylphosphonate--pyruvate aminotransferase. AN 2-aminoethylphosphonate aminotransferase. CA (2-aminoethyl)phosphonate + pyruvate = 2-phosphonoacetaldehyde + CA L-alanine. CF Pyridoxal-phosphate. CC -!- 2-Aminoethylarsonate can replace 2-aminoethylphosphonate as a CC substrate. // ID 2.6.1.38 DE Histidine aminotransferase. CA L-histidine + 2-oxoglutarate = imidazol-5-yl-pyruvate + L-glutamate. // ID 2.6.1.39 DE 2-aminoadipate aminotransferase. CA L-2-aminoadipate + 2-oxoglutarate = 2-oxoadipate + L-glutamate. CF Pyridoxal-phosphate. // ID 2.6.1.40 DE (R)-3-amino-2-methylpropionate--pyruvate aminotransferase. AN D-3-aminoisobutyrate--pyruvate aminotransferase. AN Beta-aminoisobutyrate--pyruvate transaminase. CA (R)-3-amino-2-methylpropanoate + pyruvate = 2-methyl-3-oxopropanoate + CA L-alanine. DI Hyper-beta-aminoisobutyricaciduria; MIM:210100. // ID 2.6.1.41 DE D-methionine--pyruvate aminotransferase. AN D-methionine aminotransferase. CA D-methionine + pyruvate = 4-methylthio-2-oxobutanoate + L-alanine. CC -!- Oxaloacetate can replace pyruvate. // ID 2.6.1.42 DE Branched-chain amino acid aminotransferase. AN Transaminase B. CA L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate. CF Pyridoxal-phosphate. CC -!- Also acts on L-isoleucine and L-valine. CC -!- Different from EC 2.6.1.66. PR PROSITE; PDOC00618; DR Q93Y32, BCA1_ARATH; O14370, BCA1_SCHPO; P38891, BCA1_YEAST; DR Q9M439, BCA2_ARATH; P47176, BCA2_YEAST; Q9M401, BCA3_ARATH; DR Q9FYA6, BCA5_ARATH; Q9LPM9, BCA6_ARATH; O15382, BCAM_HUMAN; DR O35855, BCAM_MOUSE; O19098, BCAM_PIG ; O35854, BCAM_RAT ; DR P54688, BCAT_CAEEL; P54687, BCAT_HUMAN; P24288, BCAT_MOUSE; DR P54690, BCAT_RAT ; O67733, ILVE_AQUAE; O29329, ILVE_ARCFU; DR P39576, ILVE_BACSU; P00510, ILVE_ECOLI; P54689, ILVE_HAEIN; DR Q9ZJF1, ILVE_HELPJ; O26004, ILVE_HELPY; Q58414, ILVE_METJA; DR O27481, ILVE_METTH; O32954, ILVE_MYCLE; Q10399, ILVE_MYCTU; DR O86428, ILVE_PSEAE; Q92I26, ILVE_RICCN; O05970, ILVE_RICPR; DR P15168, ILVE_SALTY; O86505, ILVE_STRCO; P54691, ILVE_SYNY3; DR P74921, ILVE_THEMA; Q9Y885, TOXF_COCCA; O31461, YBGE_BACSU; // ID 2.6.1.43 DE Aminolevulinate aminotransferase. CA 5-aminolevulinate + pyruvate = 4,5-dioxopentanoate + L-alanine. CF Pyridoxal-phosphate. // ID 2.6.1.44 DE Alanine--glyoxylate aminotransferase. AN AGT. CA L-alanine + glyoxylate = pyruvate + glycine. CF Pyridoxal-phosphate. CC -!- With one component of the animal enzyme, 2-oxobutanoate can replace CC glyoxylate. A second component also catalyzes the reaction of CC EC 2.6.1.51. DI Oxalosis I (glycolicaciduria); MIM:259900. PR PROSITE; PDOC00514; DR Q9BYV1, AGT2_HUMAN; Q64565, AGT2_RAT ; P31029, SPYA_CALJA; DR P41689, SPYA_FELCA; P21549, SPYA_HUMAN; O35423, SPYA_MOUSE; DR P31030, SPYA_RABIT; P09139, SPYA_RAT ; // ID 2.6.1.45 DE Serine--glyoxylate aminotransferase. AN SGAT. CA L-serine + glyoxylate = 3-hydroxypyruvate + glycine. CF Pyridoxal-phosphate. PR PROSITE; PDOC00514; DR O08374, SGAA_HYPME; P55819, SGAA_METEX; // ID 2.6.1.46 DE Diaminobutyrate--pyruvate aminotransferase. AN L-diaminobutyric acid transaminase. CA L-2,4-diaminobutanoate + pyruvate = L-aspartate 4-semialdehyde + CA L-alanine. CF Pyridoxal-phosphate. DR Q9ZEU7, ECB1_HALEL; O52250, ECB2_HALEL; O06060, ECTB_MARHA; // ID 2.6.1.47 DE Alanine--oxomalonate aminotransferase. AN L-alanine-ketomalonate transaminase. CA L-alanine + oxomalonate = pyruvate + aminomalonate. CF Pyridoxal-phosphate. // ID 2.6.1.48 DE 5-aminovalerate aminotransferase. AN Delta-aminovalerate aminotransferase. AN Delta-aminovalerate transaminase. CA 5-aminopentanoate + 2-oxoglutarate = 5-oxopentanoate + L-glutamate. CF Pyridoxal-phosphate. // ID 2.6.1.49 DE Dihydroxyphenylalanine aminotransferase. AN DOPA aminotransferase. CA 3,4-dihydroxy-L-phenylalanine + 2-oxoglutarate = CA 3,4-dihydroxyphenylpyruvate + L-glutamate. CF Pyridoxal-phosphate. // ID 2.6.1.50 DE Glutamine--scyllo-inosose aminotransferase. CA L-glutamine + 2,4,6/3,5-pentahydroxycyclohexanone = 2-oxoglutaramate + CA 1-amino-1-deoxy-scyllo-inositol. CF Pyridoxal-phosphate. // ID 2.6.1.51 DE Serine--pyruvate aminotransferase. CA L-serine + pyruvate = 3-hydroxypyruvate + L-alanine. CF Pyridoxal-phosphate. CC -!- The liver enzyme may be identical with EC 2.6.1.44. PR PROSITE; PDOC00514; DR P31029, SPYA_CALJA; P41689, SPYA_FELCA; P21549, SPYA_HUMAN; DR O35423, SPYA_MOUSE; P31030, SPYA_RABIT; P09139, SPYA_RAT ; // ID 2.6.1.52 DE Phosphoserine aminotransferase. CA O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + CA L-glutamate. CF Pyridoxal-phosphate. PR PROSITE; PDOC00514; DR Q96255, SERC_ARATH; Q59196, SERC_BACCI; Q9KDM4, SERC_BACHD; DR P80862, SERC_BACSU; P57397, SERC_BUCAI; P81435, SERC_BUCAP; DR P59492, SERC_BUCBP; P91856, SERC_CAEEL; Q9VAN0, SERC_DROME; DR Q8XEA7, SERC_ECO57; Q8FJB7, SERC_ECOL6; P23721, SERC_ECOLI; DR Q9X4H1, SERC_EDWIC; P44336, SERC_HAEIN; Q9Y617, SERC_HUMAN; DR Q9CHW5, SERC_LACLA; Q926T3, SERC_LISIN; Q8Y3L0, SERC_LISMO; DR Q8TNI1, SERC_METAC; P52878, SERC_METBA; Q8PT12, SERC_METMA; DR Q99K85, SERC_MOUSE; O33062, SERC_MYCLE; Q10534, SERC_MYCTU; DR O34370, SERC_NEIMA; P57007, SERC_NEIMB; P57881, SERC_PASMU; DR Q9HZ66, SERC_PSEAE; P10658, SERC_RABIT; Q8Y0Z0, SERC_RALSO; DR P17902, SERC_SALTI; P55900, SERC_SALTY; Q10349, SERC_SCHPO; DR Q8EEH2, SERC_SHEON; P52877, SERC_SPIOL; Q8DSV3, SERC_STRMU; DR Q9KSU7, SERC_VIBCH; Q87QA3, SERC_VIBPA; Q8D900, SERC_VIBVU; DR Q8D268, SERC_WIGBR; Q8PLY7, SERC_XANAC; Q8PA97, SERC_XANCP; DR Q8RLW0, SERC_XENNE; Q9PB19, SERC_XYLFA; Q87BU0, SERC_XYLFT; DR P33330, SERC_YEAST; P19689, SERC_YEREN; Q8ZGB4, SERC_YERPE; // ID 2.6.1.53 DE Transferred entry: 1.4.1.13. // ID 2.6.1.54 DE Pyridoxamine-phosphate aminotransferase. CA Pyridoxamine 5'-phosphate + 2-oxoglutarate = pyridoxal 5'-phosphate + CA D-glutamate. CC -!- Also acts, more slowly, on pyridoxamine. // ID 2.6.1.55 DE Taurine aminotransferase. CA Taurine + 2-oxoglutarate = sulfoacetaldehyde + L-glutamate. CF Pyridoxal-phosphate. CC -!- Also acts on D L-3-aminoisobutanoate, beta-alanine and CC 3-aminopropanesulfonate. // ID 2.6.1.56 DE 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol aminotransferase. CA 1D-1-guanidino-3-amino-1,3-dideoxy-scyllo-inositol + pyruvate = CA 1D-1-guanidino-1-deoxy-3-dehydro-scyllo-inositol + L-alanine. CC -!- L-glutamate and L-glutamine can also act as amino donors. // ID 2.6.1.57 DE Aromatic amino acid transferase. CA An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + CA L-glutamate. CF Pyridoxal-phosphate. CC -!- L-methionine can also act as donor, more slowly. CC -!- Oxaloacetate can act as acceptor. CC -!- Controlled proteolysis converts the enzyme to EC 2.6.1.1. PR PROSITE; PDOC00098; DR P43336, PHHC_PSEAE; P04693, TYRB_ECOLI; P95468, TYRB_PARDE; DR P74861, TYRB_SALTY; // ID 2.6.1.58 DE Phenylalanine(histidine) aminotransferase. CA L-phenylalanine + pyruvate = phenylpyruvate + L-alanine. CC -!- L-histidine and L-tyrosine can act instead of L-phenylalanine, in CC the reverse reaction, L-methionine, l-serine and L-glutamine can CC replace L-alanine. // ID 2.6.1.59 DE dTDP-4-amino-4,6-dideoxygalactose aminotransferase. CA dTDP-4-amino-4,6-dideoxy-D-galactose + 2-oxoglutarate = dTDP-4-dehydro- CA 6-deoxy-D-galactose + L-glutamate. CF Pyridoxal-phosphate. // ID 2.6.1.60 DE Aromatic-amino-acid--glyoxylate aminotransferase. CA An aromatic amino acid + glyoxylate = an aromatic oxo acid + glycine. CC -!- Phenylalanine, kynurenine, tyrosine and histidine can act as amino CC donors. CC -!- Glyoxylate, pyruvate and hydroxypyruvate can act as amino acceptors. // ID 2.6.1.61 DE (R)-3-amino-2-methylpropanoate aminotransferase. CA (R)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3- CA oxopropanoate + L-glutamate. CC -!- Not identical with EC 2.6.1.22. // ID 2.6.1.62 DE Adenosylmethionine--8-amino-7-oxononanoate aminotransferase. AN 7,8-diamino-pelargonic acid aminotransferase. AN 7,8-diaminononanoate aminotransferase. AN DAPA aminotransferase. CA S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4- CA methylthio-2-oxobutanoate + 7,8-diaminononanoate. CF Pyridoxal-phosphate. CC -!- S-adenosylhomocysteine can also act as donor. PR PROSITE; PDOC00519; DR O66557, BIOA_AQUAE; P22805, BIOA_BACSH; P53555, BIOA_BACSU; DR P57379, BIOA_BUCAI; Q8K9P0, BIOA_BUCAP; Q89AK4, BIOA_BUCBP; DR P13071, BIOA_CITFR; P46395, BIOA_CORGL; P12995, BIOA_ECOLI; DR P53656, BIOA_ERWHE; P44426, BIOA_HAEIN; Q9ZKM5, BIOA_HELPJ; DR O25627, BIOA_HELPY; Q58696, BIOA_METJA; P45488, BIOA_MYCLE; DR O06622, BIOA_MYCTU; P12677, BIOA_SALTY; P36568, BIOA_SERMA; DR P50277, BIOA_YEAST; // ID 2.6.1.63 DE Kynurenine--glyoxylate aminotransferase. CA L-kynurenine + glyoxylate = 4-(2-aminophenyl)-2,4-dioxobutanoate + CA glycine. CC -!- Acts, more slowly, on L-phenylalanine, L-histidine and L-tyrosine. // ID 2.6.1.64 DE Glutamine--phenylpyruvate aminotransferase. AN Glutamine transaminase K. CA L-glutamine + phenylpyruvate = 2-oxoglutaramate + L-phenylalanine. CF Pyridoxal-phosphate. CC -!- L-methionine, L-histidine and L-tyrosine can act as donors. CC -!- Has little activity on pyruvate and glyoxylate (cf. EC 2.6.1.15). // ID 2.6.1.65 DE N(6)-acetyl-beta-lysine aminotransferase. CA 3-amino-6-acetamidohexanoate + 2-oxoglutarate = 3-oxo-6- CA acetamidohexanoate + L-glutamate. CF Pyridoxal-phosphate. // ID 2.6.1.66 DE Valine--pyruvate aminotransferase. AN Transaminase C. AN Alanine--valine transaminase. CA L-valine + pyruvate = 3-methyl-2-oxobutanoate + L-alanine. CF Pyridoxal-phosphate. CC -!- Different from EC 2.6.1.42. DR P09053, AVTA_ECOLI; // ID 2.6.1.67 DE 2-aminohexanoate aminotransferase. AN Norleucine aminotransferase. AN Norleucine transaminase. CA L-2-aminohexanoate + 2-oxoglutarate = 2-oxohexanoate + L-glutamate. CF Pyridoxal-phosphate. CC -!- Also acts on L-leucine and, more slowly, on L-isoleucine, CC L-2-aminopentanoate and L-aspartate. // ID 2.6.1.68 DE Ornithine(lysine) aminotransferase. CA L-ornithine + 2-oxoglutarate = 3,4-dihydro-2H-pyrrole-2-carboxylate + CA L-glutamate. CC -!- Acts on L-lysine, producing 2,3,4,5-tetrahydropyridine-2- CC carboxylate. CC -!- From Trichomonas vaginalis. // ID 2.6.1.69 DE N(2)-acetylornithine 5-aminotransferase. CA N(2)-acetyl-L-ornithine + 2-oxoglutarate = 2-acetamido-5-oxopentanoate CA + L-glutamate. CC -!- Also acts on L-ornithine and N(2)-succinyl-L-ornithine. // ID 2.6.1.70 DE Aspartate--phenylpyruvate aminotransferase. CA L-aspartate + phenylpyruvate = oxaloacetate + L-phenylalanine. CC -!- The enzyme from P.putida also acts on 4-hydroxyphenylpyruvate and, CC more slowly, on L-glutamate and L-histidine. // ID 2.6.1.71 DE Lysine--pyruvate 6-aminotransferase. CA L-lysine + pyruvate = 2-aminoadipate 6-semialdehyde + L-alanine. // ID 2.6.1.72 DE D-4-hydroxyphenylglycine aminotransferase. CA D-4-hydroxyphenylglycine + 2-oxoglutarate = 4-hydroxyphenylglyoxylate + CA L-glutamate. CF Pyridoxal-phosphate. // ID 2.6.1.73 DE Methionine--glyoxylate transaminase. AN MGAT. CA L-methionine + glyoxylate = 4-methylthio-2-oxobutanoate + glycine. CC -!- L-glutamate can also act as donor. // ID 2.6.1.74 DE Cephalosporin-C transaminase. CA Cephalosporin C + pyruvate = 7-(5-carboxyl-5-oxopentanyl)- CA aminocephalosporinate + L-alanine. CC -!- A number of D-amino acids can also act as acceptors. // ID 2.6.1.75 DE Cysteine-conjugate transaminase. CA S-(4-bromophenyl)-L-cysteine + 2-oxoglutarate = S-(4-bromophenyl)- CA mercaptopyruvate + L-glutamate. CC -!- A number of cysteine conjugates can also act. // ID 2.6.1.76 DE Diaminobutyrate-2-oxoglutarate transaminase. AN Diaminobutyrate--2-oxoglutarate aminotransferase. AN L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase. AN 2,4-diaminobutyrate 4-aminotransferase. AN Diaminobutyrate transaminase. AN DABA aminotransferase. CA L-2,4-diaminobutyrate + 2-oxoglutarate = L-glutamate + L-aspartic CA 4-semialdehyde. CF Pyridoxal-phosphate. CC -!- Involved in the formation of 1,3-diaminopropane in Haemophilus CC influenzae and Acinetobacter baumannii. CC -!- A product of the ddc gene that also encodes L-2,4-diaminobutyrate CC decarboxylase in Acinetobacter baumannii. CC -!- Differs from EC 2.6.1.46, which has pyruvate as the amino-group CC acceptor. PR PROSITE; PDOC00519; DR P56744, DAT_ACIBA ; P44951, DAT_HAEIN ; Q9Z3R2, RHBA_RHIME; // ID 2.6.2.1 DE Transferred entry: 2.1.4.1. // ID 2.6.3.1 DE Oximinotransferase. AN Transoximinase. AN Oximase. AN Pyruvate-acetone oximinotransferase. CA Pyruvate oxime + acetone = pyruvate + acetone oxime. CC -!- Acetaldehyde can act instead of acetone; D-glucose oxime can act CC instead of pyruvate oxime. // ID 2.6.99.1 DE dATP(dGTP)--DNA purine transferase. CA dATP + depurinated DNA = ribose triphosphate + DNA. CC -!- The purine residue is transferred on to the apurinic site forming a CC normal glycosylic bond. CC -!- dGTP can also act as a purine donor. // ID 2.7.1.1 DE Hexokinase. AN Glucokinase. AN Hexokinase type IV. CA ATP + D-hexose = ADP + D-hexose 6-phosphate. CC -!- D-glucose, D-mannose, D-fructose, sorbitol and D-glucosamine can act CC as acceptors. CC -!- ITP and dATP can act as donors. CC -!- The liver isoenzyme has sometimes been called glucokinase. DI Hemolytic anemia due to hexokinase deficiency; MIM:235700. PR PROSITE; PDOC00370; DR Q42525, HXK1_ARATH; P27595, HXK1_BOVIN; Q9NFT9, HXK1_DROME; DR P19367, HXK1_HUMAN; P17710, HXK1_MOUSE; P05708, HXK1_RAT ; DR Q09756, HXK1_SCHPO; O64390, HXK1_SOLTU; Q9SEK3, HXK1_SPIOL; DR Q9SEK2, HXK1_TOBAC; P93834, HXK2_ARATH; Q9NFT7, HXK2_DROME; DR P52789, HXK2_HUMAN; O08528, HXK2_MOUSE; P27881, HXK2_RAT ; DR P50521, HXK2_SCHPO; Q9SQ76, HXK2_SOLTU; P52790, HXK3_HUMAN; DR P27926, HXK3_RAT ; P35557, HXK4_HUMAN; P52792, HXK4_MOUSE; DR P17712, HXK4_RAT ; P04806, HXKA_YEAST; P04807, HXKB_YEAST; DR Q9T071, HXKL_ARATH; P50506, HXK_DEBOC ; P80581, HXK_EMENI ; DR P33284, HXK_KLULA ; Q02155, HXK_PLAFA ; Q26609, HXK_SCHMA ; // ID 2.7.1.2 DE Glucokinase. AN Glucose kinase. CA ATP + D-glucose = ADP + D-glucose 6-phosphate. CC -!- A group of enzymes found in invertebrates and microorganisms highly CC specific for glucose. PR PROSITE; PDOC00370; PR PROSITE; PDOC00866; DR Q9GTW9, GLK1_TRIVA; Q9GTW8, GLK2_TRIVA; Q8UIV7, GLK_AGRT5 ; DR P58616, GLK_ANASP ; Q9KCZ4, GLK_BACHD ; P54495, GLK_BACSU ; DR Q59171, GLK_BRUAB ; Q8YDC6, GLK_BRUME ; Q9A6N3, GLK_CAUCR ; DR P46880, GLK_ECOLI ; Q9ZKB0, GLK_HELPJ ; O25731, GLK_HELPY ; DR Q9JQX3, GLK_NEIMA ; Q9HZ46, GLK_PSEAE ; P58617, GLK_RALSO ; DR Q98DM2, GLK_RHILO ; Q92T27, GLK_RHIME ; P58618, GLK_SALTI ; DR Q93IM5, GLK_SALTY ; Q56198, GLK_STAXY ; P40184, GLK_STRCO ; DR Q55855, GLK_SYNY3 ; Q8PKU2, GLK_XANAC ; Q8P8U7, GLK_XANCP ; DR Q9PEG4, GLK_XYLFA ; Q87EG6, GLK_XYLFT ; P58619, GLK_YERPE ; DR P21908, GLK_ZYMMO ; P82680, GLMK_PREBR; Q92407, HXKG_ASPNG; DR P17709, HXKG_YEAST; // ID 2.7.1.3 DE Ketohexokinase. AN Hepatic fructokinase. CA ATP + D-fructose = ADP + D-fructose 1-phosphate. CC -!- D-sorbose, D-agatose and 5-dehydro-D-fructose also act as acceptors. DI Fructosuria; MIM:229800. DR P50053, KHK_HUMAN ; P97328, KHK_MOUSE ; Q02974, KHK_RAT ; // ID 2.7.1.4 DE Fructokinase. AN D-fructokinase. CA ATP + D-fructose = ADP + D-fructose 6-phosphate. PR PROSITE; PDOC00504; PR PROSITE; PDOC00866; DR O05510, SCRK_BACSU; P40713, SCRK_ECOLI; P26420, SCRK_KLEPN; DR Q09124, SCRK_LACLA; P82371, SCRK_LACLC; P43468, SCRK_PEDPE; DR P42720, SCRK_RHILT; P24261, SCRK_SALTH; P26984, SCRK_SALTY; DR P37829, SCRK_SOLTU; Q07211, SCRK_STRMU; P22824, SCRK_VIBAL; DR Q03417, SCRK_ZYMMO; // ID 2.7.1.5 DE Rhamnulokinase. CA ATP + L-rhamnulose = ADP + L-rhamnulose 1-phosphate. DR P32171, RHAB_ECOLI; P27030, RHAB_SALTY; // ID 2.7.1.6 DE Galactokinase. CA ATP + D-galactose = ADP + D-galactose 1-phosphate. CC -!- D-galactosamine can also act as acceptor. DI Galactokinase deficiency; MIM:230200. PR PROSITE; PDOC00099; PR PROSITE; PDOC00545; DR P94169, GAL1_ACTPL; Q9SEE5, GAL1_ARATH; Q9KDV4, GAL1_BACHD; DR P39574, GAL1_BACSU; P56091, GAL1_CANAL; P56599, GAL1_CANMA; DR O42821, GAL1_CANPA; Q97EZ6, GAL1_CLOAB; Q8XKP9, GAL1_CLOPE; DR P06976, GAL1_ECOLI; Q8RHD0, GAL1_FUSNN; P31767, GAL1_HAEIN; DR P51570, GAL1_HUMAN; P09608, GAL1_KLULA; O84902, GAL1_LACCA; DR Q00052, GAL1_LACHE; Q9R7D7, GAL1_LACLA; Q9S6S2, GAL1_LACLC; DR Q9R0N0, GAL1_MOUSE; P96910, GAL1_MYCTU; P57899, GAL1_PASMU; DR Q9HHB6, GAL1_PYRFU; O58107, GAL1_PYRHO; Q8Z8B0, GAL1_SALTI; DR P22713, GAL1_SALTY; Q9HDU2, GAL1_SCHPO; Q9RGS1, GAL1_STACA; DR Q9K3S8, GAL1_STRCO; P13227, GAL1_STRLI; P96993, GAL1_STRMU; DR Q97NZ6, GAL1_STRPN; Q9ZB10, GAL1_STRTR; P56838, GAL1_THEMA; DR O85253, GAL1_THENE; Q8R8R7, GAL1_THETN; O83433, GAL1_TREPA; DR Q9KRP1, GAL1_VIBCH; P04385, GAL1_YEAST; Q8ZGY3, GAL1_YERPE; // ID 2.7.1.7 DE Mannokinase. CA ATP + D-mannose = ADP + D-mannose 6-phosphate. DR P82680, GLMK_PREBR; // ID 2.7.1.8 DE Glucosamine kinase. CA ATP + glucosamine = ADP + glucosamine phosphate. // ID 2.7.1.9 DE Deleted entry. // ID 2.7.1.10 DE Phosphoglucokinase. AN Glucose-phosphate kinase. CA ATP + D-fructose 1-phosphate = ADP + D-fructose 1,6-bisphosphate. // ID 2.7.1.11 DE 6-phosphofructokinase. AN Phosphohexokinase. AN Phosphofructokinase I. CA ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. CC -!- D-tagatose 6-phosphate and sedoheptulose 7-phosphate can act as CC acceptors. CC -!- UTP, CTP and ITP can act as donors. CC -!- Not identical with EC 2.7.1.105. DI Glycogen storage disease VII; MIM:232800. PR PROSITE; PDOC00336; PR PROSITE; PDOC00504; DR Q8YKG3, K6P1_ANASP; Q9HGZ1, K6P1_ASPOR; Q8A8R5, K6P1_BACTN; DR O94201, K6P1_CANAL; Q8XNH2, K6P1_CLOPE; P06998, K6P1_ECOLI; DR Q03215, K6P1_KLULA; Q92448, K6P1_PICPA; O08333, K6P1_STRCO; DR P72830, K6P1_SYNY3; P21777, K6P1_THETH; P59680, K6P1_YARLI; DR P16861, K6P1_YEAST; Q8YVR1, K6P2_ANASP; Q9HGZ0, K6P2_ASPOR; DR Q8A624, K6P2_BACTN; O94200, K6P2_CANAL; Q8XL57, K6P2_CLOPE; DR P06999, K6P2_ECOLI; Q03216, K6P2_KLULA; Q9L1L8, K6P2_STRCO; DR Q55988, K6P2_SYNY3; P21778, K6P2_THETH; P16862, K6P2_YEAST; DR Q8A2E9, K6P3_BACTN; Q9FC99, K6P3_STRCO; O67605, K6PF_AQUAE; DR P78985, K6PF_ASPNG; Q9K843, K6PF_BACHD; Q59214, K6PF_BACMC; DR Q93LR4, K6PF_BACSH; P00512, K6PF_BACST; O34529, K6PF_BACSU; DR P57391, K6PF_BUCAI; Q8K9N0, K6PF_BUCAP; P59563, K6PF_BUCBP; DR Q27483, K6PF_CAEEL; Q27543, K6PF_CALFI; P52784, K6PF_CANFA; DR O08308, K6PF_CLOAB; Q890Z2, K6PF_CLOTE; Q8RQN5, K6PF_COREF; DR Q8NR14, K6PF_CORGL; Q9RWN1, K6PF_DEIRA; P90521, K6PF_DICDI; DR P52034, K6PF_DROME; Q8FBD0, K6PF_ECOL6; Q9Z6C3, K6PF_ENTCL; DR Q8RG98, K6PF_FUSNN; Q27665, K6PF_HAECO; P43863, K6PF_HAEIN; DR P08237, K6PF_HUMAN; P80019, K6PF_LACDE; Q07636, K6PF_LACLA; DR Q88VY1, K6PF_LACPL; Q92BE4, K6PF_LISIN; Q8Y6W0, K6PF_LISMO; DR P47857, K6PF_MOUSE; P47457, K6PF_MYCGE; O33106, K6PF_MYCLE; DR Q8EVH2, K6PF_MYCPE; P75476, K6PF_MYCPN; Q98PW8, K6PF_MYCPU; DR O53257, K6PF_MYCTU; Q8EPD6, K6PF_OCEIH; Q9CPH2, K6PF_PASMU; DR P00511, K6PF_RABIT; P47858, K6PF_RAT ; Q8XG19, K6PF_SALTY; DR Q27778, K6PF_SCHMA; O42938, K6PF_SCHPO; P20275, K6PF_SPICI; DR Q99TG4, K6PF_STAAM; Q8CS68, K6PF_STAEP; Q8E5Q1, K6PF_STRA3; DR Q8DTX6, K6PF_STRMU; Q8K7A2, K6PF_STRP3; Q8P0S6, K6PF_STRP8; DR Q97RC6, K6PF_STRPN; Q99ZD0, K6PF_STRPY; Q8DQ85, K6PF_STRR6; DR Q9L9E3, K6PF_STRTR; Q8DJB1, K6PF_SYNEL; Q9WY52, K6PF_THEMA; DR Q8R914, K6PF_THETN; Q9PQV8, K6PF_UREPA; Q9KNP2, K6PF_VIBCH; DR Q87KX0, K6PF_VIBPA; Q8DCY1, K6PF_VIBVU; Q8ZJL6, K6PF_YERPE; DR P17858, K6PL_HUMAN; P12382, K6PL_MOUSE; P30835, K6PL_RAT ; DR Q01813, K6PP_HUMAN; Q9WUA3, K6PP_MOUSE; P47859, K6PP_RABIT; DR P47860, K6PP_RAT ; // ID 2.7.1.12 DE Gluconokinase. AN Gluconate kinase. CA ATP + D-gluconate = ADP + 6-phospho-D-gluconate. PR PROSITE; PDOC00408; DR P46834, GNTK_BACLI; P12011, GNTK_BACSU; P46859, GNTK_ECOLI; DR Q10242, GNTK_SCHPO; P39208, IDNK_ECOLI; // ID 2.7.1.13 DE Dehydogluconokinase. AN Ketogluconokinase. CA ATP + 2-dehydro-D-gluconate = ADP + 6-phospho-2-dehydro-D-gluconate. // ID 2.7.1.14 DE Sedoheptulokinase. AN Heptulokinase. CA ATP + sedoheptulose = ADP + sedoheptulose 7-phosphate. // ID 2.7.1.15 DE Ribokinase. CA ATP + D-ribose = ADP + D-ribose 5-phosphate. CC -!- 2-deoxy-D-ribose can also act as acceptor. PR PROSITE; PDOC00504; DR Q9K6K1, RBSK_BACHD; P36945, RBSK_BACSU; P05054, RBSK_ECOLI; DR P44331, RBSK_HAEIN; Q9H477, RBSK_HUMAN; Q9CF42, RBSK_LACLA; DR O60116, RBSK_SCHPO; P25332, RBSK_YEAST; // ID 2.7.1.16 DE L-ribulokinase. CA ATP + L-ribulose = ADP + L-ribulose 5-phosphate. CC -!- Ribitol and L-arabinitol can also act as acceptors. DR Q9KBQ3, ARAB_BACHD; Q9S468, ARAB_BACST; P94524, ARAB_BACSU; DR P58541, ARAB_ECO57; Q8FL88, ARAB_ECOL6; P08204, ARAB_ECOLI; DR Q9LBQ3, ARAB_MYCSM; P58542, ARAB_SALTI; P06188, ARAB_SALTY; DR Q99W57, ARAB_STAAM; Q8NXY1, ARAB_STAAW; Q8CRC6, ARAB_STAEP; DR Q87FK5, ARAB_VIBPA; P58543, ARAB_YERPE; // ID 2.7.1.17 DE Xylulokinase. AN Xylulose kinase. CA ATP + D-xylulose = ADP + D-xylulose 5-phosphate. PR PROSITE; PDOC00408; DR P42826, XKS1_YEAST; P12867, XYLB_ACTMI; P54271, XYLB_AMPSP; DR P26909, XYLB_ARTS7; P39211, XYLB_BACSU; P09099, XYLB_ECOLI; DR P44401, XYLB_HAEIN; P29444, XYLB_KLEPN; P35850, XYLB_LACBR; DR Q9CFG8, XYLB_LACLA; P21939, XYLB_LACPE; P27155, XYLB_STAXY; DR Q9RK00, XYLB_STRCO; P27156, XYLB_STRRU; // ID 2.7.1.18 DE Phosphoribokinase. CA ATP + D-ribose 5-phosphate = ADP + D-ribose 1,5-bisphosphate. // ID 2.7.1.19 DE Phosphoribulokinase. AN Phosphopentokinase. CA ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-bisphosphate. PR PROSITE; PDOC00490; DR P58347, KPP1_RHIME; P12033, KPP1_RHOSH; P25933, KPP1_SELMI; DR P56887, KPP2_RHIME; P23010, KPP2_RHOSH; P25934, KPP2_SELMI; DR P19924, KPPP_ALCEU; P19923, KPPR_ALCEU; P25697, KPPR_ARATH; DR P19824, KPPR_CHLRE; P37307, KPPR_ECOLI; P27774, KPPR_MESCR; DR P37100, KPPR_NITVU; P81664, KPPR_PINPS; P09559, KPPR_SPIOL; DR P37101, KPPR_SYNY3; P26302, KPPR_WHEAT; P23015, KPPR_XANFL; // ID 2.7.1.20 DE Adenosine kinase. CA ATP + adenosine = ADP + AMP. CC -!- 2-aminoadenosine can also act as acceptor. PR PROSITE; PDOC00504; DR Q9SF85, ADK1_ARATH; Q9LZG0, ADK2_ARATH; P55262, ADK_CRIGR ; DR P55263, ADK_HUMAN ; P55264, ADK_MOUSE ; O49923, ADK_PHYPA ; DR Q64640, ADK_RAT ; Q9TVW2, ADK_TOXGO ; P47143, ADK_YEAST ; // ID 2.7.1.21 DE Thymidine kinase. CA ATP + thymidine = ADP + thymidine 5'-phosphate. CC -!- Deoxyuridine can also act as acceptor. CC -!- dGTP can also act as donor. CC -!- The deoxypyrimidine kinase complex induced by herpes simplex virus CC catalyzes this reaction as well as those of EC 2.7.1.114, CC EC 2.7.1.118, and EC 2.7.4.9. CC -!- Formerly EC 2.7.1.75. PR PROSITE; PDOC00524; DR P28852, KITH_AMEPV; P18555, KITH_ASFB7; Q9K6F0, KITH_BACHD; DR O52951, KITH_BACNA; Q03221, KITH_BACSU; P13300, KITH_BPT4 ; DR P16600, KITH_CAPVK; Q05879, KITH_CBEPV; Q05880, KITH_CFEPV; DR P04047, KITH_CHICK; P09768, KITH_CRIGR; P03177, KITH_EBV ; DR Q9S5G7, KITH_ECO57; P23331, KITH_ECOLI; O96720, KITH_ENCCU; DR P10052, KITH_FOWPV; P44309, KITH_HAEIN; P03176, KITH_HSV11; DR P06478, KITH_HSV1C; P08333, KITH_HSV1E; P17402, KITH_HSV1K; DR P06479, KITH_HSV1S; P04407, KITH_HSV23; P36226, KITH_HSVB5; DR P24096, KITH_HSVB6; P22649, KITH_HSVBH; P33802, KITH_HSVBM; DR P24424, KITH_HSVBQ; P24425, KITH_HSVE4; P09100, KITH_HSVEB; DR P13159, KITH_HSVF ; P28855, KITH_HSVI1; P17653, KITH_HSVMD; DR P21293, KITH_HSVSA; P04408, KITH_HSVSM; P13157, KITH_HSVTF; DR P25987, KITH_HSVTU; P04183, KITH_HUMAN; P23983, KITH_ILTVT; DR P04363, KITH_MONPV; P04184, KITH_MOUSE; Q8RLE0, KITH_MYCGA; DR P47280, KITH_MYCGE; P75070, KITH_MYCPN; P28851, KITH_MYXVA; DR Q9Q8N6, KITH_MYXVL; O81263, KITH_ORYSA; P57926, KITH_PASMU; DR P27363, KITH_PRVN3; Q90029, KITH_RACVI; P27158, KITH_RAT ; DR Q9ZIG2, KITH_RHOSI; P07605, KITH_SFVKA; P23335, KITH_SPVKA; DR O50519, KITH_STRCO; P47848, KITH_STRGC; Q9WYN2, KITH_THEMA; DR O57203, KITH_VACCA; Q9JFB7, KITH_VACCT; P03297, KITH_VACCV; DR P04364, KITH_VARV ; P14341, KITH_VZV4 ; P14342, KITH_VZV7 ; DR P09250, KITH_VZVD ; P14343, KITH_VZVG ; P14344, KITH_VZVW ; DR Q90033, KITH_YABAM; O00142, KITM_HUMAN; Q9N0C5, KITM_MACFA; DR Q9R088, KITM_MOUSE; // ID 2.7.1.22 DE Ribosylnicotinamide kinase. CA ATP + N-ribosylnicotinamide = ADP + nicotinamide ribonucleotide. // ID 2.7.1.23 DE NAD(+) kinase. AN DPN kinase. CA ATP + NAD(+) = ADP + NADP(+). DR Q8YN19, PPN1_ANASP; Q9K904, PPN1_BACHD; O31612, PPN1_BACSU; DR Q92D53, PPN1_LISIN; Q8Y8D7, PPN1_LISMO; P74430, PPN1_SYNY3; DR Q8Z074, PPN2_ANASP; Q9K808, PPN2_BACHD; O34934, PPN2_BACSU; DR Q92BC2, PPN2_LISMO; P73955, PPN2_SYNY3; Q9YD08, PPNK_AERPE; DR O67055, PPNK_AQUAE; O30297, PPNK_ARCFU; P58055, PPNK_BACST; DR O51291, PPNK_BORBU; Q8YGW9, PPNK_BRUME; P57282, PPNK_BUCAI; DR Q8K9V8, PPNK_BUCAP; Q89AR9, PPNK_BUCBP; Q9PHM6, PPNK_CAMJE; DR P58056, PPNK_CAUCR; Q97HD7, PPNK_CLOAB; Q8XJE3, PPNK_CLOPE; DR P58057, PPNK_ECO57; P37768, PPNK_ECOLI; Q8RGM4, PPNK_FUSNN; DR P44497, PPNK_HAEIN; Q9HNX7, PPNK_HALN1; Q9ZJ81, PPNK_HELPJ; DR O25944, PPNK_HELPY; O95544, PPNK_HUMAN; Q9CIJ4, PPNK_LACLA; DR Q8TKQ5, PPNK_METAC; Q58327, PPNK_METJA; Q8TXD2, PPNK_METKA; DR Q8PTD1, PPNK_METMA; O26958, PPNK_METTH; P58058, PPNK_MOUSE; DR P47374, PPNK_MYCGE; Q49897, PPNK_MYCLE; P75508, PPNK_MYCPN; DR O33196, PPNK_MYCTU; Q9JQL9, PPNK_NEIMA; Q9CNU2, PPNK_PASMU; DR Q51841, PPNK_PORGI; Q9HZC0, PPNK_PSEAE; Q9V081, PPNK_PYRAB; DR Q8U1V2, PPNK_PYRFU; O58801, PPNK_PYRHO; Q8XW25, PPNK_RALSO; DR Q98NA6, PPNK_RHILO; Q92QJ0, PPNK_RHIME; Q92I08, PPNK_RICCN; DR Q9ZDA2, PPNK_RICPR; Q8XFN1, PPNK_SALTY; Q99V84, PPNK_STAAM; DR Q9S219, PPNK_STRCO; Q97QV0, PPNK_STRPN; Q99ZQ7, PPNK_STRPY; DR Q97WJ8, PPNK_SULSO; Q96YN6, PPNK_SULTO; Q9HKH7, PPNK_THEAC; DR Q9X255, PPNK_THEMA; Q8RAC3, PPNK_THETN; Q979U7, PPNK_THEVO; DR O83455, PPNK_TREPA; Q9PQW6, PPNK_UREPA; Q9KTP8, PPNK_VIBCH; DR Q87RX6, PPNK_VIBPA; Q8DF58, PPNK_VIBVU; Q8D391, PPNK_WIGBR; DR Q8PM39, PPNK_XANAC; Q8PAD9, PPNK_XANCP; Q9PBQ0, PPNK_XYLFA; DR Q87DA0, PPNK_XYLFT; Q8ZH09, PPNK_YERPE; // ID 2.7.1.24 DE Dephospho-CoA kinase. AN Dephosphocoenzyme A kinase. CA ATP + dephospho-CoA = ADP + CoA. DR Q9JRM6, COAE_ACTAC; P56186, COAE_AERHY; Q8UJC4, COAE_AGRT5; DR Q8YW62, COAE_ANASP; O67792, COAE_AQUAE; Q9K857, COAE_BACHD; DR Q46526, COAE_BACNO; O34932, COAE_BACSU; O51497, COAE_BORBU; DR Q8YE21, COAE_BRUME; P57299, COAE_BUCAI; Q8K9U1, COAE_BUCAP; DR Q9ZF69, COAE_BURPS; Q9PMD9, COAE_CAMJE; P58100, COAE_CAUCR; DR Q9PJP9, COAE_CHLMU; Q9Z7U3, COAE_CHLPN; Q8KD46, COAE_CHLTE; DR O84499, COAE_CHLTR; Q97K22, COAE_CLOAB; Q8XIX0, COAE_CLOPE; DR P58101, COAE_CORAM; Q9RT73, COAE_DEIRA; P36679, COAE_ECOLI; DR Q8RHR7, COAE_FUSNN; P44920, COAE_HAEIN; Q9ZL12, COAE_HELPJ; DR O25502, COAE_HELPY; Q9CHQ8, COAE_LACLA; Q92BF2, COAE_LISIN; DR Q8Y6W8, COAE_LISMO; P47506, COAE_MYCGE; Q50178, COAE_MYCLE; DR P75400, COAE_MYCPN; O06148, COAE_MYCTU; Q50962, COAE_NEIGO; DR Q9JSS4, COAE_NEIMA; Q9CPF5, COAE_PASMU; Q9HVP8, COAE_PSEAE; DR O69082, COAE_PSEPG; P36644, COAE_PSEPU; Q9ZEL7, COAE_PSEST; DR Q8XVK2, COAE_RALSO; Q98DY2, COAE_RHILO; Q92TE9, COAE_RHIME; DR Q92GL2, COAE_RICCN; Q9ZCK0, COAE_RICPR; Q8XGF5, COAE_SALTY; DR Q99TH4, COAE_STAAM; Q9S2K7, COAE_STRCO; Q8P249, COAE_STRP3; DR Q97R60, COAE_STRPN; P58102, COAE_STRPY; Q55515, COAE_SYNY3; DR Q9X1A7, COAE_THEMA; Q56416, COAE_THETH; Q8RBE5, COAE_THETN; DR O83319, COAE_TREPA; Q9KPE3, COAE_VIBCH; Q87LT4, COAE_VIBPA; DR Q56741, COAE_VIBVU; Q8D308, COAE_WIGBR; Q8PHK7, COAE_XANAC; DR Q56764, COAE_XANCP; Q9PAI2, COAE_XYLFA; Q87AA7, COAE_XYLFT; DR Q8ZBI0, COAE_YERPE; P58897, COE1_CORGL; P56187, COE2_CORGL; // ID 2.7.1.25 DE Adenylylsulfate kinase. AN APS kinase. AN Adenosine-5'phosphosulfate kinase. CA ATP + adenylylsulfate = ADP + 3'-phosphoadenylylsulfate. CC -!- The human phosphoadenosine-phosphosulfate synthase (PAPS) system CC is a bifunctional enzyme: ATP sulfurylase, which catalyzes the CC formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic CC sulfate and the second step is catalyzed by the APS kinase portion of CC 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which CC involves the formation of PAPS from enzyme bound APS and ATP. CC -!- This is in contrast to what is found in bacteria, yeast, fungi CC and plants, where the formation of PAPS is carried out by two CC individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25. DR Q9KCT0, CYC1_BACHD; O34577, CYC1_BACSU; P57702, CYC1_PSEAE; DR Q9K7H6, CYC2_BACHD; O06735, CYC2_BACSU; P29811, CYC2_PSEAE; DR Q9YCR6, CYSC_AERPE; O29953, CYSC_ARCFU; P57497, CYSC_BUCAI; DR Q8K9D4, CYSC_BUCAP; Q97MT8, CYSC_CLOAB; P56861, CYSC_DEIRA; DR Q8FEJ2, CYSC_ECOL6; P23846, CYSC_ECOLI; P56858, CYSC_PYRAB; DR Q8XF34, CYSC_SALTY; Q8EB13, CYSC_SHEON; Q8DJ87, CYSC_SYNEL; DR P72940, CYSC_SYNY3; Q9KP21, CYSC_VIBCH; Q87SX6, CYSC_VIBPA; DR Q8DE75, CYSC_VIBVU; Q8ZBP3, CYSC_YERPE; Q10600, CYSN_MYCTU; DR O50274, CYSN_PSEAE; Q9PD78, CYSN_XYLFA; Q87DG7, CYSN_XYLFT; DR Q43295, KAP1_ARATH; O49196, KAP2_ARATH; O49204, KAPS_CATRO; DR Q92203, KAPS_EMENI; Q12657, KAPS_PENCH; Q02196, KAPS_YEAST; DR P28604, NODQ_AZOBR; P13442, NODQ_RHIME; P72339, NODQ_RHIS3; DR O07309, NODQ_RHISB; P52978, NODQ_RHITR; O54820, PPS1_CAVPO; DR O43252, PPS1_HUMAN; Q60967, PPS1_MOUSE; O95340, PPS2_HUMAN; DR O88428, PPS2_MOUSE; Q27128, PPS_URECA ; O67174, SATC_AQUAE; // ID 2.7.1.26 DE Riboflavin kinase. AN Flavokinase. CA ATP + riboflavin = ADP + FMN. DR P54575, RIBC_BACSU; P57250, RIBF_BUCAI; Q8K9Z1, RIBF_BUCAP; DR Q59263, RIBF_CORAM; P08391, RIBF_ECOLI; P44957, RIBF_HAEIN; DR P47391, RIBF_MYCGE; P75587, RIBF_MYCPN; P22990, RIBF_PSEFL; DR O84990, RIBF_RHOOP; P73651, RIBF_SYNY3; // ID 2.7.1.27 DE Erythritol kinase. CA ATP + erythritol = ADP + D-erythritol 4-phosphate. DR Q05512, MRK2_MOUSE; P27448, MRK3_HUMAN; Q03141, MRK3_MOUSE; DR Q96L34, MRK4_HUMAN; // ID 2.7.1.28 DE Triokinase. AN Triose kinase. CA ATP + D-glyceraldehyde = ADP + D-glyceraldehyde 3-phosphate. // ID 2.7.1.29 DE Glycerone kinase. AN Dihydroxyacetone kinase. CA ATP + glycerone = ADP + glycerone phosphate. DR O13902, DAK1_SCHPO; P54838, DAK1_YEAST; O74215, DAK2_SCHPO; DR P43550, DAK2_YEAST; P45510, DAK_CITFR ; O60017, DAK_PICAN ; DR O74192, DAK_PICPA ; // ID 2.7.1.30 DE Glycerol kinase. AN Glycerokinase. AN ATP:glycerol 3-phosphotransferase. CA ATP + glycerol = ADP + glycerol 3-phosphate. CC -!- Glycerone and L-glyceraldehyde can act as acceptors. CC -!- UTP (and, in the case of the yeast enzyme, ITP and GTP) can act as CC donors. DI Hyperglycerolemia; MIM:307030. PR PROSITE; PDOC00408; DR Q14410, GKP2_HUMAN; Q14409, GKP3_HUMAN; Q9ADA7, GLK1_STRCO; DR Q9X049, GLK1_THEMA; Q9RJM2, GLK2_STRCO; Q9X1E4, GLK2_THEMA; DR Q8U940, GLPK_AGRT5; Q8YW05, GLPK_ANASP; O66746, GLPK_AQUAE; DR Q9KDW8, GLPK_BACHD; P18157, GLPK_BACSU; O51257, GLPK_BORBU; DR Q21944, GLPK_CAEEL; Q97JG4, GLPK_CLOAB; Q8XHD3, GLPK_CLOPE; DR Q9RT38, GLPK_DEIRA; P08859, GLPK_ECOLI; O34153, GLPK_ENTCA; DR O34154, GLPK_ENTFA; Q8RHZ9, GLPK_FUSNN; P44400, GLPK_HAEIN; DR Q9HNS5, GLPK_HALN1; P32189, GLPK_HUMAN; Q9CG64, GLPK_LACLA; DR Q92BH6, GLPK_LISIN; Q8Y6Z2, GLPK_LISMO; Q64516, GLPK_MOUSE; DR P47284, GLPK_MYCGE; Q9CB81, GLPK_MYCLE; P75064, GLPK_MYCPN; DR Q98QY9, GLPK_MYCPU; O69664, GLPK_MYCTU; P57944, GLPK_PASMU; DR Q51390, GLPK_PSEAE; O87924, GLPK_PSETO; Q9V207, GLPK_PYRAB; DR Q8TZI8, GLPK_PYRFU; O93623, GLPK_PYRKO; Q8XUY1, GLPK_RALSO; DR Q63060, GLPK_RAT ; Q98M73, GLPK_RHILO; O86033, GLPK_RHIME; DR Q8Z2Y6, GLPK_SALTI; Q8ZKP3, GLPK_SALTY; Q99UH3, GLPK_STAAM; DR Q8NWX7, GLPK_STAAW; P25013, GLPK_STRGR; Q8K665, GLPK_STRP3; DR Q8NZW9, GLPK_STRP8; Q97N78, GLPK_STRPN; Q99YI7, GLPK_STRPY; DR P95907, GLPK_SULSO; P74260, GLPK_SYNY3; Q9WX53, GLPK_THEAQ; DR Q9X6C9, GLPK_THEBO; O66131, GLPK_THETH; Q8R8J4, GLPK_THETN; DR Q9KLJ9, GLPK_VIBCH; Q87M72, GLPK_VIBPA; Q8DBM6, GLPK_VIBVU; DR Q8PQG7, GLPK_XANAC; Q8PDI0, GLPK_XANCP; Q9PB76, GLPK_XYLFA; DR Q87BZ2, GLPK_XYLFT; P32190, GLPK_YEAST; // ID 2.7.1.31 DE Glycerate kinase. CA ATP + (R)-glycerate = ADP + 3-phospho-(R)-glycerate. DR P77364, GRK1_ECOLI; P23524, GRK2_ECOLI; Q9XBL1, GRK_BACCE ; DR Q9Z9P2, GRK_BACHD ; P42100, GRK_BACSU ; P44507, GRK_HAEIN ; DR P57098, GRK_NEIMA ; P57099, GRK_NEIMB ; // ID 2.7.1.32 DE Choline kinase. CA ATP + choline = ADP + O-phosphocholine. CC -!- Ethanolamine and its methyl and ethyl derivatives can also act as CC acceptors. DR Q9Y259, KICE_HUMAN; O55229, KICE_MOUSE; O54783, KICE_RAT ; DR P35790, KICH_HUMAN; O54804, KICH_MOUSE; Q01134, KICH_RAT ; DR Q10276, KICH_SCHPO; P20485, KICH_YEAST; // ID 2.7.1.33 DE Pantothenate kinase. AN Pantothenic acid kinase. CA ATP + pantothenate = ADP + D-4'-phosphopantothenate. DR Q8UJ92, COAA_AGRT5; Q9K8X7, COAA_BACHD; P54556, COAA_BACSU; DR Q8YE39, COAA_BRUME; Q8NRQ2, COAA_CORGL; P15044, COAA_ECOLI; DR P44793, COAA_HAEIN; Q9CFM3, COAA_LACLA; Q92D94, COAA_LISIN; DR Q8Y8I0, COAA_LISMO; Q9X795, COAA_MYCLE; O53440, COAA_MYCTU; DR P57967, COAA_PASMU; Q98CS9, COAA_RHILO; Q92TB5, COAA_RHIME; DR Q8Z318, COAA_SALTI; Q9L9K3, COAA_SALTY; O86779, COAA_STRCO; DR Q8K7C7, COAA_STRP3; Q8P0V9, COAA_STRP8; Q97RH6, COAA_STRPN; DR Q99ZH1, COAA_STRPY; Q9KV38, COAA_VIBCH; Q8ZAN6, COAA_YERPE; DR Q8L5Y9, PNK1_ARATH; Q8TE04, PNK1_HUMAN; Q8K4K6, PNK1_MOUSE; DR O80765, PNK2_ARATH; Q9BZ23, PNK2_HUMAN; Q9H999, PNK3_HUMAN; DR Q8R2W9, PNK3_MOUSE; Q9NVE7, PNK4_HUMAN; Q923S8, PNK4_RAT ; // ID 2.7.1.34 DE Pantetheine kinase. CA ATP + pantetheine = ADP + pantetheine 4'-phosphate. // ID 2.7.1.35 DE Pyridoxal kinase. AN Pyridoxine kinase. AN Pyridoxamine kinase. AN Vitamin B6 kinase. CA ATP + pyridoxal = ADP + pyridoxal 5'-phosphate. CC -!- Pyridoxine, pyridoxamine and various derivatives can also act as CC acceptor. DR Q8W1X2, PDXK_ARATH; O01824, PDXK_CAEEL; P40191, PDXK_ECOLI; DR O00764, PDXK_HUMAN; Q8Z4W1, PDXK_SALTI; P40192, PDXK_SALTY; DR P82197, PDXK_SHEEP; P77150, PDXY_ECOLI; P44690, PDXY_HAEIN; DR Q51892, PDXY_PROMI; // ID 2.7.1.36 DE Mevalonate kinase. CA ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate. CC -!- CTP, GTP or UTP can also act as donors. DI Mevalonicaciduria; MIM:251170. PR PROSITE; PDOC00545; DR Q9Y946, KIME_AERPE; P46086, KIME_ARATH; O27995, KIME_ARCFU; DR Q03426, KIME_HUMAN; Q58487, KIME_METJA; Q50559, KIME_METTH; DR Q9R008, KIME_MOUSE; Q9V187, KIME_PYRAB; Q8U0F3, KIME_PYRFU; DR O59291, KIME_PYRHO; P17256, KIME_RAT ; Q09780, KIME_SCHPO; DR P07277, KIME_YEAST; // ID 2.7.1.37 DE Protein kinase. AN Phosphorylase B kinase kinase. AN Glycogen synthase A kinase. AN Hydroxyalkyl-protein kinase. AN Serine(threonine) protein kinase. CA ATP + a protein = ADP + a phosphoprotein. PR PROSITE; PDOC00100; DR P54741, AFSK_STRCO; P54742, AFSK_STRGR; Q16671, AMH2_HUMAN; DR Q62893, AMH2_RAT ; O59790, ARK1_SCHPO; Q13315, ATM_HUMAN ; DR Q62388, ATM_MOUSE ; Q28041, AVR1_BOVIN; Q04771, AVR1_HUMAN; DR P37172, AVR1_MOUSE; P80201, AVR1_RAT ; Q28043, AVR2_BOVIN; DR P27037, AVR2_HUMAN; P27038, AVR2_MOUSE; P38444, AVR2_RAT ; DR Q28560, AVR2_SHEEP; P27039, AVR2_XENLA; Q95126, AVRB_BOVIN; DR Q13705, AVRB_HUMAN; P27040, AVRB_MOUSE; P38445, AVRB_RAT ; DR P27041, AVRB_XENLA; Q94F62, BAK1_ARATH; Q13873, BMR2_HUMAN; DR O35607, BMR2_MOUSE; P36894, BMRA_HUMAN; P36895, BMRA_MOUSE; DR Q05438, BMRB_CHICK; O00238, BMRB_HUMAN; P36898, BMRB_MOUSE; DR O22476, BRI1_ARATH; Q8GUQ5, BRI1_LYCES; Q8L899, BRI1_LYCPE; DR Q9GKI7, C43B_BOVIN; Q9Y5P4, C43B_HUMAN; Q9EQG9, C43B_MOUSE; DR P32562, CDC5_YEAST; P06243, CDC7_YEAST; Q00534, CDK6_HUMAN; DR Q64261, CDK6_MOUSE; Q9H4B4, CNK_HUMAN ; Q60806, CNK_MOUSE ; DR Q9R011, CNK_RAT ; P38679, COT1_NEUCR; Q8NK05, CPK1_CRYNE; DR Q12126, CRK1_SCHPO; Q05609, CTR1_ARATH; P20792, DAF1_CAEEL; DR P50488, DAF4_CAEEL; Q9BQI3, E2K1_HUMAN; Q9Z2R9, E2K1_MOUSE; DR P33279, E2K1_RABIT; Q63185, E2K1_RAT ; P28869, ERK1_CANAL; DR P42525, ERK1_DICDI; P40417, ERKA_DROME; Q9LYN8, EXS_ARATH ; DR P16892, FUS3_YEAST; Q92207, HOG1_CANAL; Q9UV50, HOG1_DEBHA; DR P32485, HOG1_YEAST; P38991, IPL1_YEAST; Q9U6D2, JNK1_ANCCA; DR Q8WQG9, JNK1_CAEEL; P92208, JNK_DROME ; Q966Y3, JNK_SUBDO ; DR Q15418, K6A1_HUMAN; P18653, K6A1_MOUSE; Q63531, K6A1_RAT ; DR Q15349, K6A2_HUMAN; Q9WUT3, K6A2_MOUSE; P51812, K6A3_HUMAN; DR P18654, K6A3_MOUSE; Q9UK32, K6A6_HUMAN; P18652, K6AA_CHICK; DR P10665, K6AA_XENLA; P00517, KAPA_BOVIN; P25321, KAPA_CRIGR; DR P17612, KAPA_HUMAN; P05132, KAPA_MOUSE; P36887, KAPA_PIG ; DR P27791, KAPA_RAT ; P06244, KAPA_YEAST; P05131, KAPB_BOVIN; DR P22694, KAPB_HUMAN; P05206, KAPB_MOUSE; P05383, KAPB_PIG ; DR P40376, KAPB_SCHPO; P06245, KAPB_YEAST; P49673, KAPC_ASCSU; DR P21137, KAPC_CAEEL; P34099, KAPC_DICDI; P12370, KAPC_DROME; DR P05986, KAPC_YEAST; P22612, KAPG_HUMAN; O62846, KAPG_MACMU; DR P24256, KAPI_BOVIN; Q08467, KC21_ARATH; P21868, KC21_CHICK; DR P19138, KC21_HUMAN; Q60737, KC21_MOUSE; P33674, KC21_RABIT; DR P19139, KC21_RAT ; P40231, KC21_SCHPO; P15790, KC21_YEAST; DR Q08466, KC22_ARATH; P20427, KC22_BOVIN; P21869, KC22_CHICK; DR P19784, KC22_HUMAN; O54833, KC22_MOUSE; P28020, KC22_XENLA; DR P19454, KC22_YEAST; O64817, KC23_ARATH; P18334, KC2A_CAEEL; DR Q02720, KC2A_DICDI; P08181, KC2A_DROME; P28523, KC2A_MAIZE; DR Q8TG13, KC2A_NEUCR; O76484, KC2A_SPOFR; P28547, KC2A_THEPA; DR P16911, KDC1_DROME; P49840, KG3A_HUMAN; P18265, KG3A_RAT ; DR P49841, KG3B_HUMAN; Q9WV60, KG3B_MOUSE; P18266, KG3B_RAT ; DR P83101, KG3H_DROME; Q03042, KGP1_DROME; Q03043, KGP2_DROME; DR Q13237, KGP2_HUMAN; Q61410, KGP2_MOUSE; Q64595, KGP2_RAT ; DR P32023, KGP3_DROME; P00516, KGPA_BOVIN; Q13976, KGPA_HUMAN; DR O77676, KGPA_RABIT; P21136, KGPB_BOVIN; P14619, KGPB_HUMAN; DR Q9Z0Z0, KGPB_MOUSE; P13186, KIN2_YEAST; P00513, KIPA_BPT7 ; DR P36896, KIR2_HUMAN; P80202, KIR2_RAT ; P37023, KIR3_HUMAN; DR Q61288, KIR3_MOUSE; P80203, KIR3_RAT ; Q8TAS1, KIST_HUMAN; DR P97343, KIST_MOUSE; Q63285, KIST_RAT ; P00531, KMIL_AVIMH; DR P05625, KMIL_CHICK; P87347, KMOS_APTAU; P10650, KMOS_CERAE; DR P10741, KMOS_CHICK; P00540, KMOS_HUMAN; P00536, KMOS_MOUSE; DR P07331, KMOS_MSVMH; P00537, KMOS_MSVMM; P00538, KMOS_MSVMO; DR P32593, KMOS_MSVMT; P10421, KMOS_MSVTS; P50118, KMOS_PIG ; DR P00539, KMOS_RAT ; P12965, KMOS_XENLA; P32350, KNS1_YEAST; DR Q9VPC0, KP58_DROME; P83099, KPC4_DROME; P04409, KPCA_BOVIN; DR P17252, KPCA_HUMAN; P20444, KPCA_MOUSE; P10102, KPCA_RABIT; DR P05696, KPCA_RAT ; P05126, KPCB_BOVIN; P05771, KPCB_HUMAN; DR P04410, KPCB_MOUSE; P05772, KPCB_RABIT; P05128, KPCG_BOVIN; DR P05129, KPCG_HUMAN; P05697, KPCG_MOUSE; P10829, KPCG_RABIT; DR P41743, KPCI_HUMAN; Q62074, KPCI_MOUSE; Q05513, KPCZ_HUMAN; DR Q02956, KPCZ_MOUSE; O19111, KPCZ_RABIT; P09217, KPCZ_RAT ; DR Q05652, KPEL_DROME; P17801, KPRO_MAIZE; P11801, KPSH_HUMAN; DR P14681, KSS1_YEAST; P53667, LIK1_HUMAN; P53668, LIK1_MOUSE; DR P53669, LIK1_RAT ; Q10156, LKH1_SCHPO; Q9DGE2, M14A_BRARE; DR Q90336, M14A_CYPCA; O62618, M14A_DROME; Q9DGE1, M14B_BRARE; DR Q9I958, M14B_CYPCA; O61443, M14B_DROME; P83100, M14C_DROME; DR Q02779, M3KA_HUMAN; Q12852, M3KC_HUMAN; Q60700, M3KC_MOUSE; DR Q63796, M3KC_RAT ; Q99558, M3KE_HUMAN; Q9WUL6, M3KE_MOUSE; DR Q92918, M4K1_HUMAN; P70218, M4K1_MOUSE; Q12851, M4K2_HUMAN; DR Q61161, M4K2_MOUSE; Q8IVH8, M4K3_HUMAN; Q99JP0, M4K3_MOUSE; DR Q924I2, M4K3_RAT ; O95819, M4K4_HUMAN; P97820, M4K4_MOUSE; DR Q9Y4K4, M4K5_HUMAN; Q8BPM2, M4K5_MOUSE; Q8N4C8, M4K6_HUMAN; DR Q9JM52, M4K6_MOUSE; Q06060, MAPK_PEA ; Q40884, MAPK_PETHY; DR Q10292, MEK1_SCHPO; P24719, MEK1_YEAST; P46196, MK01_BOVIN; DR P28482, MK01_HUMAN; P27703, MK01_MOUSE; P26696, MK01_XENLA; DR P27361, MK03_HUMAN; Q63844, MK03_MOUSE; P21708, MK03_RAT ; DR P31152, MK04_HUMAN; Q63454, MK04_RAT ; Q16659, MK06_HUMAN; DR Q61532, MK06_MOUSE; P27704, MK06_RAT ; Q13164, MK07_HUMAN; DR Q9WVS8, MK07_MOUSE; Q9DGD9, MK08_BRARE; P45983, MK08_HUMAN; DR Q91Y86, MK08_MOUSE; P49185, MK08_RAT ; Q8QHK8, MK08_XENLA; DR P79996, MK09_CHICK; P45984, MK09_HUMAN; Q9WTU6, MK09_MOUSE; DR P49186, MK09_RAT ; P53779, MK10_HUMAN; Q61831, MK10_MOUSE; DR P49187, MK10_RAT ; Q15759, MK11_HUMAN; Q9WUI1, MK11_MOUSE; DR O42376, MK12_BRARE; P53778, MK12_HUMAN; O08911, MK12_MOUSE; DR Q63538, MK12_RAT ; O15264, MK13_HUMAN; Q9Z1B7, MK13_MOUSE; DR Q9N272, MK13_PANTR; Q9WTY9, MK13_RAT ; O02812, MK14_CANFA; DR Q16539, MK14_HUMAN; P47811, MK14_MOUSE; Q95NE7, MK14_PANTR; DR P70618, MK14_RAT ; P47812, MK14_XENLA; Q90327, MK8A_CYPCA; DR O42099, MK8B_CYPCA; P43068, MKC1_CANAL; Q07176, MMK1_MEDSA; DR Q40353, MMK2_MEDSA; Q9BUB5, MNK1_HUMAN; O08605, MNK1_MOUSE; DR Q9HBH9, MNK2_HUMAN; Q8CDB0, MNK2_MOUSE; O94235, MPH1_SCHPO; DR Q39021, MPK1_ARATH; Q39022, MPK2_ARATH; Q39023, MPK3_ARATH; DR Q39024, MPK4_ARATH; Q39025, MPK5_ARATH; Q39026, MPK6_ARATH; DR Q39027, MPK7_ARATH; O75011, NAK1_SCHPO; Q96PY6, NEK1_HUMAN; DR P51954, NEK1_MOUSE; P51955, NEK2_HUMAN; O35942, NEK2_MOUSE; DR P51956, NEK3_HUMAN; Q9R0A5, NEK3_MOUSE; P51957, NEK4_HUMAN; DR Q9Z1J2, NEK4_MOUSE; P48479, NIM1_NEUCR; P10676, NINC_DROME; DR O48963, NPH1_ARATH; O42626, NRC2_NEUCR; P38692, NRK1_YEAST; DR Q08942, NRKA_TRYBB; Q03428, NRKB_TRYBB; Q40517, NTF3_TOBAC; DR Q40532, NTF4_TOBAC; Q40531, NTF6_TOBAC; O13310, ORB6_SCHPO; DR O15530, PDPK_HUMAN; Q9Z2A0, PDPK_MOUSE; O55173, PDPK_RAT ; DR O74456, PEF1_SCHPO; O94921, PFT1_HUMAN; O35495, PFT1_MOUSE; DR Q9N0P9, PIM1_BOVIN; Q9YHZ5, PIM1_BRARE; Q95LJ0, PIM1_FELCA; DR P11309, PIM1_HUMAN; P06803, PIM1_MOUSE; P26794, PIM1_RAT ; DR Q9P1W9, PIM2_HUMAN; Q62070, PIM2_MOUSE; Q9PU85, PIM3_COTJA; DR P58750, PIM3_MOUSE; O70444, PIM3_RAT ; Q91822, PIM3_XENLA; DR Q9KIG4, PK1_STRTO ; Q9W0V1, PK61_DROME; P54739, PKAA_STRCO; DR P54740, PKAB_STRCO; P37562, PKN1_BACSU; Q9PK92, PKN1_CHLMU; DR Q9Z986, PKN1_CHLPN; O84303, PKN1_CHLTR; Q8FUI5, PKN1_COREF; DR Q8NU98, PKN1_CORGL; P33973, PKN1_MYXXA; Q8R9T6, PKN1_THETN; DR O34507, PKN2_BACSU; Q97IC2, PKN2_CLOAB; Q8XJL8, PKN2_CLOPE; DR Q8FUI4, PKN2_COREF; Q8NU97, PKN2_CORGL; P54736, PKN2_MYXXA; DR Q9XBQ0, PKN3_MYXXA; P54737, PKN5_MYXXA; P54738, PKN6_MYXXA; DR P54734, PKNA_ANASP; Q8G4G1, PKNA_BIFLO; P54743, PKNA_MYCLE; DR P71585, PKNA_MYCTU; Q8G6P9, PKNB_BIFLO; Q9CEF5, PKNB_LACLA; DR P54744, PKNB_MYCLE; P71584, PKNB_MYCTU; O05871, PKND_MYCTU; DR P72001, PKNE_MYCTU; P72003, PKNF_MYCTU; P57993, PKNG_MYCLE; DR P96256, PKNG_MYCTU; Q11053, PKNH_MYCTU; Q10964, PKNI_MYCTU; DR Q10697, PKNJ_MYCTU; P95078, PKNK_MYCTU; O53510, PKNL_MYCTU; DR P47355, PKNS_MYCGE; P75524, PKNS_MYCPN; Q9XA16, PKNX_STRCO; DR Q9S2C0, PKSC_STRCO; P49695, PKWA_THECU; P50528, PLO1_SCHPO; DR Q17446, PMK1_CAEEL; Q8MXI4, PMK2_CAEEL; O44514, PMK3_CAEEL; DR Q13523, PR4B_HUMAN; Q61136, PR4B_MOUSE; P78527, PRKD_HUMAN; DR P97313, PRKD_MOUSE; Q9ZVR7, PSKR_ARATH; Q8LPB4, PSKR_DAUCA; DR P38623, RCK2_YEAST; Q13546, RIK1_HUMAN; Q60855, RIK1_MOUSE; DR O43353, RIK2_HUMAN; P58801, RIK2_MOUSE; Q9Y572, RIK3_HUMAN; DR Q9QZL0, RIK3_MOUSE; Q9Z2P5, RIK3_RAT ; P47735, RLK5_ARATH; DR P27966, RMIL_AVEVR; P10533, RMIL_AVII1; Q04982, RMIL_CHICK; DR P34908, RMIL_COTJA; P42411, RSBT_BACSU; Q9K5J7, RSBW_BACAA; DR Q9KFF1, RSBW_BACHD; O50231, RSBW_BACLI; P17904, RSBW_BACSU; DR Q92DC2, RSBW_LISIN; Q8Y8K6, RSBW_LISMO; Q8CXL7, RSBW_OCEIH; DR P95843, RSBW_STAAM; Q8NVI5, RSBW_STAAW; Q9F7V2, RSBW_STAEP; DR Q9UEE5, S17A_HUMAN; Q9GM70, S17A_RABIT; O94768, S17B_HUMAN; DR P11792, SCH9_YEAST; P50530, SCK1_SCHPO; P18431, SGG_DROME ; DR O00141, SGK1_HUMAN; Q9WVC6, SGK1_MOUSE; Q9XT18, SGK1_RABIT; DR Q06226, SGK1_RAT ; Q9HBY8, SGK2_HUMAN; Q8R4U9, SGK2_RAT ; DR Q96BR1, SGK3_HUMAN; Q9ERE3, SGK3_MOUSE; P23293, SGV1_YEAST; DR O14305, SID1_SCHPO; Q00772, SLT2_YEAST; Q09488, SMA6_CAEEL; DR P41808, SMK1_YEAST; P70878, SP22_BACCO; Q9KCN2, SP22_BACHD; DR P26778, SP22_BACLI; P35148, SP22_BACME; O32724, SP22_BACSH; DR O32727, SP22_BACST; P10728, SP22_BACSU; Q97GQ9, SP22_CLOAB; DR Q8XIR5, SP22_CLOPE; P59623, SP22_CLOTE; Q8EQ73, SP22_OCEIH; DR O32721, SP22_PAEPO; P59624, SP22_PASPE; Q8RAA8, SP22_THETN; DR P27638, SPK1_SCHPO; Q9FAB3, SPKA_SYNY3; P74297, SPKB_SYNY3; DR P74745, SPKC_SYNY3; P54735, SPKD_SYNY3; P73515, SPKE_SYNY3; DR P73469, SPKF_SYNY3; Q92398, SPM1_SCHPO; O94547, SRK1_SCHPO; DR Q09092, SRK6_BRAOL; P23561, ST11_YEAST; P49842, ST19_HUMAN; DR Q9JHN8, ST19_MOUSE; Q9UPE1, ST23_HUMAN; Q9Z0G2, ST23_MOUSE; DR Q9Y6E0, ST24_HUMAN; O00506, ST25_HUMAN; Q9Z2W1, ST25_MOUSE; DR Q9BXA7, ST2A_HUMAN; Q61241, ST2A_MOUSE; Q96PF2, ST2B_HUMAN; DR O54863, ST2B_MOUSE; Q96PN8, ST2C_HUMAN; Q9D2E1, ST2C_MOUSE; DR Q9BXU1, ST31_HUMAN; Q99MW1, ST31_MOUSE; Q8TDR2, ST35_HUMAN; DR Q91819, ST6L_XENLA; Q13188, STK3_HUMAN; Q13043, STK4_HUMAN; DR O14965, STK6_HUMAN; P97477, STK6_MOUSE; P59241, STK6_RAT ; DR Q91820, STK6_XENLA; O76039, STK9_HUMAN; O94804, STKA_HUMAN; DR O55098, STKA_MOUSE; Q15831, STKB_HUMAN; Q91604, STKB_XENLA; DR Q96GD4, STKC_HUMAN; O70126, STKC_MOUSE; Q9N0X0, STKC_PIG ; DR O55099, STKC_RAT ; Q9UQB9, STKD_HUMAN; O88445, STKD_MOUSE; DR O75716, STKG_HUMAN; O88697, STKG_MOUSE; P57760, STKG_RAT ; DR Q09892, STY1_SCHPO; P39745, SUR1_CAEEL; P36897, TGR1_HUMAN; DR Q64729, TGR1_MOUSE; P80204, TGR1_RAT ; P37173, TGR2_HUMAN; DR Q62312, TGR2_MOUSE; P38551, TGR2_PIG ; P38438, TGR2_RAT ; DR Q9UKE5, TNIK_HUMAN; P83510, TNIK_MOUSE; Q11179, YPC2_CAEEL; DR Q9RI12, YPKA_YERPE; Q05608, YPKA_YERPS; // ID 2.7.1.38 DE Phosphorylase kinase. AN Dephosphophosphorylase kinase. CA 4 ATP + 2 phosphorylase B = 4 ADP + phosphorylase A. DI Glycogen storage disease VIII; MIM:306000. DI Phosphorylase kinase deficiency of liver and muscle; MIM:261750. PR PROSITE; PDOC00100; DR Q16816, KPBG_HUMAN; P07934, KPBG_MOUSE; P00518, KPBG_RABIT; DR P13286, KPBG_RAT ; P15735, KPBH_HUMAN; Q9DB30, KPBH_MOUSE; DR P31325, KPBH_RAT ; // ID 2.7.1.39 DE Homoserine kinase. CA ATP + L-homoserine = ADP + O-phospho-L-homoserine. PR PROSITE; PDOC00545; DR Q9YA72, KHSE_AERPE; Q8UHA8, KHSE_AGRT5; Q8YZV9, KHSE_ANASP; DR O67332, KHSE_AQUAE; Q9K7E4, KHSE_BACHD; P04948, KHSE_BACSU; DR Q8YFR2, KHSE_BRUME; O66132, KHSE_BUCAI; Q8K9V0, KHSE_BUCAP; DR P59568, KHSE_BUCBP; Q9PIZ3, KHSE_CAMJE; Q92209, KHSE_CANAL; DR Q9A342, KHSE_CAUCR; Q97JN8, KHSE_CLOAB; P07128, KHSE_CORGL; DR Q9RRU5, KHSE_DEIRA; Q8XA82, KHSE_ECO57; P00547, KHSE_ECOLI; DR P04947, KHSE_FREDI; P44504, KHSE_HAEIN; Q9HP55, KHSE_HALN1; DR Q9ZM48, KHSE_HELPJ; O25690, KHSE_HELPY; Q9CGD7, KHSE_LACLA; DR P52991, KHSE_LACLC; Q927U8, KHSE_LISIN; Q8Y4A6, KHSE_LISMO; DR Q9RAM6, KHSE_METFL; O32378, KHSE_METGL; Q58504, KHSE_METJA; DR Q8TYG6, KHSE_METKA; P45836, KHSE_MYCLE; Q10603, KHSE_MYCTU; DR Q9JWE5, KHSE_NEIMA; Q9CPD3, KHSE_PASMU; P29364, KHSE_PSEAE; DR Q9UZV7, KHSE_PYRAB; Q8ZZX3, KHSE_PYRAE; Q8U1Z9, KHSE_PYRFU; DR O58814, KHSE_PYRHO; Q8XX83, KHSE_RALSO; Q985W2, KHSE_RHILO; DR Q92RG1, KHSE_RHIME; Q8XGP5, KHSE_SALTY; O43056, KHSE_SCHPO; DR P27722, KHSE_SERMA; Q99UE6, KHSE_STAAM; Q8NWV8, KHSE_STAAW; DR Q9ADB2, KHSE_STRCO; P72535, KHSE_STRPN; Q97W70, KHSE_SULSO; DR Q975A7, KHSE_SULTO; P73646, KHSE_SYNY3; Q9HKR6, KHSE_THEAC; DR Q9WZ15, KHSE_THEMA; Q8R711, KHSE_THETN; Q979X5, KHSE_THEVO; DR Q9KPK4, KHSE_VIBCH; Q87SC9, KHSE_VIBPA; Q8DEP3, KHSE_VIBVU; DR Q8P9Q0, KHSE_XANCP; Q9PBC0, KHSE_XYLFA; Q87C24, KHSE_XYLFT; DR P17423, KHSE_YEAST; Q8ZIN5, KHSE_YERPE; O69015, KHSE_ZYMMO; // ID 2.7.1.40 DE Pyruvate kinase. AN Phosphoenolpyruvate kinase. AN Phosphoenol transphosphorylase. CA ATP + pyruvate = ADP + phosphoenolpyruvate. CC -!- UTP, GTP, CTP, ITP and dATP can also act as donors. CC -!- Also phosphorylates hydroxylamine and fluoride in the presence of CC CO(2). DI Hemolytic anemia due to pyruvate kinase deficiency; MIM:266200. PR PROSITE; PDOC00101; DR P14178, KPY1_ECOLI; P11979, KPY1_FELCA; P14618, KPY1_HUMAN; DR O30853, KPY1_PHOLE; P11974, KPY1_RABIT; P11980, KPY1_RAT ; DR Q8Z6K2, KPY1_SALTI; P77983, KPY1_SALTY; P19680, KPY1_SPICI; DR Q55863, KPY1_SYNY3; P30615, KPY1_TRYBB; P00549, KPY1_YEAST; DR P21599, KPY2_ECOLI; P14786, KPY2_HUMAN; P52480, KPY2_MOUSE; DR O18919, KPY2_RABIT; P11981, KPY2_RAT ; P73534, KPY2_SYNY3; DR P30616, KPY2_TRYBB; P52489, KPY2_YEAST; P70789, KPY3_AGRVI; DR Q44473, KPY4_AGRVI; Q43117, KPYA_RICCO; Q40545, KPYA_TOBAC; DR O65595, KPYC_ARATH; P22200, KPYC_SOLTU; Q42806, KPYC_SOYBN; DR Q42954, KPYC_TOBAC; P55964, KPYG_RICCO; Q40546, KPYG_TOBAC; DR O94122, KPYK_AGABI; Q12669, KPYK_ASPNG; P51181, KPYK_BACLI; DR P51182, KPYK_BACPY; Q02499, KPYK_BACST; P80885, KPYK_BACSU; DR O51323, KPYK_BORBU; P57404, KPYK_BUCAI; Q8K9M3, KPYK_BUCAP; DR P46614, KPYK_CANAL; P00548, KPYK_CHICK; Q9PK61, KPYK_CHLMU; DR Q9Z984, KPYK_CHLPN; P94685, KPYK_CHLTR; O08309, KPYK_CLOAB; DR P81344, KPYK_CLOPA; Q46289, KPYK_CLOPE; Q46078, KPYK_CORGL; DR O62619, KPYK_DROME; O44006, KPYK_EIMTE; P22360, KPYK_EMENI; DR P43924, KPYK_HAEIN; P34038, KPYK_LACDE; Q07637, KPYK_LACLA; DR Q04668, KPYK_LEIBR; Q27686, KPYK_LEIME; O05118, KPYK_METEX; DR Q57572, KPYK_METJA; P47458, KPYK_MYCGE; P94939, KPYK_MYCIT; DR P78031, KPYK_MYCPN; O06134, KPYK_MYCTU; Q10208, KPYK_SCHPO; DR P32044, KPYK_THEAC; Q56301, KPYK_THELI; P31865, KPYK_TRIRE; DR Q27788, KPYK_TRYBO; Q92122, KPYK_XENLA; P30614, KPYK_YARLI; DR Q29536, KPYR_CANFA; P30613, KPYR_HUMAN; P53657, KPYR_MOUSE; DR P12928, KPYR_RAT ; // ID 2.7.1.41 DE Glucose-1-phosphate phosphodismutase. CA 2 D-glucose 1-phosphate = D-glucose + D-glucose 1,6-bisphosphate. // ID 2.7.1.42 DE Riboflavin phosphotransferase. CA D-glucose 1-phosphate + riboflavin = D-glucose + FMN. // ID 2.7.1.43 DE Glucuronokinase. CA ATP + D-glucuronate = ADP + 1-phospho-alpha-D-glucuronate. // ID 2.7.1.44 DE Galacturonokinase. CA ATP + D-galacturonate = ADP + 1-phospho-alpha-D-galacturonate. // ID 2.7.1.45 DE 2-dehydro-3-deoxygluconokinase. AN 2-keto-3-deoxygluconokinase. AN 3-deoxy-2-oxo-D-gluconate kinase. AN KDG kinase. CA ATP + 2-dehydro-3-deoxy-D-gluconate = ADP + 6-phospho-2-dehydro-3-deoxy- CA D-gluconate. PR PROSITE; PDOC00504; DR P50845, KDGK_BACSU; P37647, KDGK_ECOLI; P45416, KDGK_ERWCH; DR P44482, KDGK_HAEIN; // ID 2.7.1.46 DE L-arabinokinase. CA ATP + L-arabinose = ADP + L-arabinose 1-phosphate. // ID 2.7.1.47 DE D-ribulokinase. CA ATP + D-ribulose = ADP + D-ribulose 5-phosphate. // ID 2.7.1.48 DE Uridine kinase. AN Uridine monophosphokinase. CA ATP + uridine = ADP + UMP. CC -!- Cytidine can act as acceptor. CC -!- GTP or ITP can act as donors. DI Immunodeficiency disease; MIM:191710. DR Q9HA47, UCK1_HUMAN; P52623, UCK1_MOUSE; Q9BZX2, UCK2_HUMAN; DR Q99PM9, UCK2_MOUSE; Q17413, UCK_CAEEL ; Q9VC99, UCK_DROME ; DR P27515, URK1_YEAST; Q9KDD8, URK_BACHD ; O32033, URK_BACSU ; DR Q59190, URK_BORBU ; Q9Z7H0, URK_CHLPN ; Q8XJI6, URK_CLOPE ; DR Q9RXZ5, URK_DEIRA ; P31218, URK_ECOLI ; P44533, URK_HAEIN ; DR Q9HQC9, URK_HALN1 ; Q9CF21, URK_LACLA ; Q92BL6, URK_LISIN ; DR Q8Y727, URK_LISMO ; P47622, URK_MYCGE ; P75217, URK_MYCPN ; DR Q9CM85, URK_PASMU ; Q8XEY2, URK_SALTY ; Q99TN8, URK_STAAM ; DR Q8P0F8, URK_STRP8 ; Q97QJ7, URK_STRPN ; Q99Z70, URK_STRPY ; DR Q9PQF9, URK_UREPA ; Q9KT67, URK_VIBCH ; Q8ZFZ9, URK_YERPE ; // ID 2.7.1.49 DE Hydroxymethylpyrimidine kinase. CA ATP + 4-amino-2-methyl-5-hydroxymethylpyrimidine = ADP + 4-amino-2- CA methyl-5-phosphomethylpyrimidine. CC -!- CTP, UTP and GTP can act as donors. // ID 2.7.1.50 DE Hydroxyethylthiazole kinase. CA ATP + 4-methyl-5-(2-hydroxyethyl)-thiazole = ADP + 4-methyl-5-(2- CA phosphoethyl)-thiazole. DR P40386, THI4_SCHPO; P41835, THI6_YEAST; Q8UAS9, THIM_AGRT5; DR O28204, THIM_ARCFU; Q9K7L2, THIM_BACHD; P39593, THIM_BACSU; DR Q8XKQ7, THIM_CLOPE; Q8NQH0, THIM_CORGL; Q8X7G3, THIM_ECO57; DR P76423, THIM_ECOLI; Q57233, THIM_HAEIN; Q9ZKZ9, THIM_HELPJ; DR O25516, THIM_HELPY; Q9CG46, THIM_LACLA; Q92EW7, THIM_LISIN; DR Q8YA46, THIM_LISMO; Q8TMD5, THIM_METAC; Q8PS50, THIM_METMA; DR P57931, THIM_PASMU; Q9UZQ4, THIM_PYRAB; Q8U191, THIM_PYRFU; DR O58877, THIM_PYRHO; Q8Z5C8, THIM_SALTI; P55883, THIM_SALTY; DR Q99SG5, THIM_STAAM; Q8NVH4, THIM_STAAW; Q9RGS6, THIM_STACA; DR Q97RS6, THIM_STRPN; Q8R807, THIM_THETN; Q87JW7, THIM_VIBPA; // ID 2.7.1.51 DE L-fuculokinase. CA ATP + L-fuculose = ADP + L-fuculose 1-phosphate. PR PROSITE; PDOC00408; DR Q8X6R3, FUCK_ECO57; P11553, FUCK_ECOLI; P44399, FUCK_HAEIN; DR Q8Z428, FUCK_SALTI; Q8ZMC5, FUCK_SALTY; // ID 2.7.1.52 DE Fucokinase. AN L-fucose kinase. CA ATP + 6-deoxy-L-galactose = ADP + 6-deoxy-L-galactose 1-phosphate. DR Q8N0W3, FUK_HUMAN ; // ID 2.7.1.53 DE L-xylulokinase. AN L-xylulose kinase. CA ATP + L-xylulose = ADP + L-xylulose 5-phosphate. PR PROSITE; PDOC00408; DR P37677, LYXK_ECOLI; P44991, LYXK_HAEIN; P57928, LYXK_PASMU; // ID 2.7.1.54 DE D-arabinokinase. CA ATP + D-arabinose = ADP + D-arabinose 5-phosphate. // ID 2.7.1.55 DE Allose kinase. AN Allokinase. CA ATP + D-allose = ADP + D-allose 6-phosphate. DR P32718, ALSK_ECOLI; // ID 2.7.1.56 DE 1-phosphofructokinase. AN Fructose 1-phosphate kinase. CA ATP + D-fructose 1-phosphate = ADP + D-fructose 1,6-bisphosphate. CC -!- ITP, GTP or UTP can replace ATP. PR PROSITE; PDOC00504; DR Q49396, FRUK_MYCGE; P75038, FRUK_MYCPN; O31714, K1PF_BACSU; DR O51575, K1PF_BORBU; P23539, K1PF_ECOLI; P44330, K1PF_HAEIN; DR P23386, K1PF_RHOCA; P23354, K1PF_XANCP; // ID 2.7.1.57 DE Deleted entry. // ID 2.7.1.58 DE 2-dehydro-3-deoxygalactonokinase. AN 2-keto-3-deoxy-galactonokinase. AN 2-oxo-3-deoxygalactonate kinase. CA ATP + 2-dehydro-3-deoxy-D-galactonate = ADP + 2-dehydro-3-deoxy-D- CA galactonate 6-phosphate. DR P31459, DGOK_ECOLI; // ID 2.7.1.59 DE N-acetylglucosamine kinase. AN GlcNAc kinase. CA ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate. CC -!- The bacterial enzyme also acts on D-glucose. DR Q9UJ70, NAGK_HUMAN; Q9QZ08, NAGK_MOUSE; // ID 2.7.1.60 DE N-acylmannosamine kinase. CA ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate. CC -!- Acts on the acetyl and glycolyl derivatives. DR Q8YBP2, NAEK_BRUME; Q8FWN5, NAEK_BRUSU; Q8FD60, NAK1_ECOL6; DR Q8FDU8, NAK2_ECOL6; Q8X9H0, NANK_ECO57; P45425, NANK_ECOLI; DR P44541, NANK_HAEIN; Q9CKB3, NANK_PASMU; Q8Z3F1, NANK_SALTI; DR Q8ZLQ8, NANK_SALTY; P59437, NANK_SHIFL; Q9KR61, NANK_VIBCH; DR Q8D612, NANK_VIBVU; Q8ZCG9, NANK_YERPE; // ID 2.7.1.61 DE Acyl-phosphate-hexose phosphotransferase. CA Acyl phosphate + D-hexose = an acid + D-hexose phosphate. CC -!- Phosphorylates D-glucose and D-mannose on O-6, and D-fructose on O-1 CC or O-6. // ID 2.7.1.62 DE Phosphoramidate-hexose phosphotransferase. CA Phosphoramidate + hexose = NH(3) + hexose 1-phosphate. CC -!- May be identical with EC 3.1.3.9. // ID 2.7.1.63 DE Polyphosphate-glucose phosphotransferase. AN Polyphosphate glucokinase. CA {Phosphate}(N) + D-glucose = {phosphate}(N-1) + D-glucose 6-phosphate. CC -!- Requires a neutral salt, e.g. KCl, for maximum activity. CC -!- Also acts on glucosamine. DR Q49988, PPGK_MYCLE; Q59568, PPGK_MYCTU; // ID 2.7.1.64 DE Inositol 3-kinase. AN Myo-inositol 1-kinase. AN Myoinositol kinase. AN Inositol 1-kinase. CA ATP + myo-inositol = ADP + 1D-myo-inositol 3-phosphate. // ID 2.7.1.65 DE Scyllo-inosamine kinase. CA ATP + 1-amino-1-deoxy-scyllo-inositol = ADP + 1-amino-1-deoxy-scyllo- CA inositol 4-phosphate. CC -!- Also acts on streptamine, 2-deoxystreptamine and 1D-1-guanidino-3- CC amino-1,3-dideoxy-scyllo-inositol. // ID 2.7.1.66 DE Undecaprenol kinase. AN Isoprenoid-alcohol kinase. CA ATP + undecaprenol = ADP + undecaprenyl phosphate. DR P58740, UPK1_AGRT5; Q9KFL5, UPK1_BACHD; Q97LQ3, UPK1_CLOAB; DR Q98DM7, UPK1_RHILO; Q9FC36, UPK1_STRCO; P58741, UPK2_AGRT5; DR Q9KCP8, UPK2_BACHD; Q97KF6, UPK2_CLOAB; Q98NJ1, UPK2_RHILO; DR Q9K407, UPK2_STRCO; Q8YXJ9, UPK_ANASP ; O67939, UPK_AQUAE ; DR P39438, UPK_AZOBR ; P94507, UPK_BACSU ; O51273, UPK_BORBU ; DR Q8YDC0, UPK_BRUME ; P57170, UPK_BUCAI ; Q8KA52, UPK_BUCAP ; DR P59523, UPK_BUCBP ; Q9PIS4, UPK_CAMJE ; Q9A2G0, UPK_CAUCR ; DR Q8KFJ7, UPK_CHLTE ; Q8XL56, UPK_CLOPE ; Q8NQC3, UPK_CORGL ; DR Q9FB58, UPK_CORST ; Q9RB37, UPK_CYTJO ; Q9RX61, UPK_DEIRA ; DR P31054, UPK_ECOLI ; Q8RIA6, UPK_FUSNN ; Q9CDM7, UPK_LACLA ; DR Q9CC42, UPK_MYCLE ; O06239, UPK_MYCTU ; Q9JSY6, UPK_NEIMA ; DR Q9K0Z3, UPK_NEIMB ; Q9I2E5, UPK_PSEAE ; Q8ZYX0, UPK_PYRAE ; DR Q8Y1I9, UPK_RALSO ; Q92SP2, UPK_RHIME ; Q8ZLY3, UPK_SALTY ; DR Q99VT8, UPK_STAAM ; Q9KIN5, UPK_STAAU ; Q8NXQ4, UPK_STAAW ; DR Q97SC8, UPK_STRPN ; Q9A1G8, UPK_STRPY ; Q97X94, UPK_SULSO ; DR Q96ZM1, UPK_SULTO ; Q55684, UPK_SYNY3 ; Q9WZZ5, UPK_THEMA ; DR Q8RB29, UPK_THETN ; Q9KUJ4, UPK_VIBCH ; Q8PQW6, UPK_XANAC ; DR Q8PDZ9, UPK_XANCP ; Q9PCE0, UPK_XYLFA ; Q87CN8, UPK_XYLFT ; DR Q8ZI65, UPK_YERPE ; Q9RNL1, UPK_ZYMMO ; // ID 2.7.1.67 DE 1-phosphatidylinositol 4-kinase. AN Phosphatidylinositol 4-kinase. AN Phosphatidylinositol kinase (phosphorylating). AN Phosphatidylinositol kinase. AN Type II phosphatidylinositol kinase. AN PI kinase. AN PI4-kinase. AN PI4K-alpha. AN PtdIns-4-kinase. CA ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo- CA inositol 4-phosphate. PR PROSITE; PDOC00710; DR P54677, PI4K_DICDI; P42356, PI4K_HUMAN; P39104, PIK1_YEAST; DR P37297, STT4_YEAST; // ID 2.7.1.68 DE 1-phosphatidylinositol-4-phosphate 5-kinase. AN Diphosphoinositide kinase. AN PIP kinase. AN Phosphatidylinositol 4-phosphate kinase. AN Phosphatidylinositol-4-phosphate 5-kinase. AN Type I PIP kinase. AN PtdIns(4)P-5-kinase. CA ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1- CA phosphatidyl-1D-myo-inositol 4,5-bisphosphate. CC -!- This enzyme can also phosphorylate PtdIns3P in the 4-position, and CC PtdIns, PtdIns3P and PtdIns(3,4)P(2) in the 5-position in vitro, CC but to a lesser extent. CC -!- The last of these reactions occurs in vivo and is physiologically CC relevant. DR O59722, FAB1_SCHPO; Q9Y2I7, FYV1_HUMAN; Q9Z1T6, FYV1_MOUSE; DR P38994, MSS4_YEAST; // ID 2.7.1.69 DE Protein-N(pi)-phosphohistidine-sugar phosphotransferase. AN Enzyme II of the phosphotransferase system. AN PTS permease. AN PEP-sugar phosphotransferase enzyme II. CA Protein N-phosphohistidine + sugar = protein histidine + sugar CA phosphate. CC -!- Comprises a group of related enzymes. CC -!- The protein substrate is a phosphocarrier protein of low molecular CC mass (9.5 Kd). CC -!- The protein is phosphorylated in a reaction catalyzed by CC EC 2.7.3.9 and this acts as the phosphate donor for the above CC reaction. CC -!- The enzyme translocates the sugar it phosphorylates into bacteria. CC -!- Aldohexoses and their glycosides and alditols are phosphorylated CC on O-6; fructose and sorbose on O-1. CC -!- Glycerone and disaccharides are also substrates. PR PROSITE; PDOC00528; PR PROSITE; PDOC00795; DR P54745, HRSA_ECOLI; P09323, PTAA_ECOLI; P45604, PTAA_KLEPN; DR O06900, PTAB_FUSMR; Q9AGA7, PTAB_KLEPN; P40739, PTBA_BACSU; DR P08722, PTBA_ECOLI; P26207, PTBA_ERWCH; Q45402, PTCA_BACST; DR P46319, PTCA_BACSU; P17335, PTCA_ECOLI; P55901, PTCB_AERHY; DR Q45399, PTCB_BACST; P46318, PTCB_BACSU; P17409, PTCB_ECOLI; DR P24241, PTDA_ECOLI; P23388, PTF1_RHOCA; P45597, PTF1_XANCP; DR P26379, PTFA_BACSU; P24217, PTFA_ECOLI; P44715, PTFA_HAEIN; DR P47308, PTFA_MYCGE; P75039, PTFA_MYCPN; Q8Z591, PTFA_SALTI; DR P17127, PTFA_SALTY; P41029, PTFB_BACAM; P26380, PTFB_BACSU; DR P20966, PTFB_ECOLI; P44714, PTFB_HAEIN; P23387, PTFB_RHOCA; DR P23355, PTFB_XANCP; P42015, PTGA_BACST; P20166, PTGA_BACSU; DR Q44840, PTGA_BORBU; Q9WXI7, PTGA_BUCAI; Q8KA51, PTGA_BUCAP; DR Q89B05, PTGA_BUCBP; Q45298, PTGA_CORGL; P08837, PTGA_ECOLI; DR P45338, PTGA_HAEIN; P45618, PTGA_MYCCA; P47315, PTGA_MYCGE; DR P75569, PTGA_MYCPN; P02908, PTGA_SALTY; P35595, PTGA_STRPN; DR P57437, PTGB_BUCAI; Q8K9J0, PTGB_BUCAP; P05053, PTGB_ECOLI; DR P37439, PTGB_SALTY; P05706, PTHA_ECOLI; O32333, PTHB_CLOBE; DR P56580, PTHB_ECOLI; O32522, PTHB_ERWAM; P54715, PTIB_BACSU; DR P31451, PTIB_ECOLI; P37187, PTKA_ECOLI; Q8X7H5, PTKB_ECOL6; DR P37188, PTKB_ECOLI; P11502, PTLA_LACCA; P23532, PTLA_LACLA; DR P02909, PTLA_STAAM; P26426, PTLA_STRMU; P24400, PTLB_LACCA; DR P23531, PTLB_LACLA; P11162, PTLB_STAAU; P50976, PTLB_STRMU; DR Q9K680, PTMA_BACHD; Q45420, PTMA_BACST; P42956, PTMA_BACSU; DR P57635, PTMA_BUCAI; Q8K911, PTMA_BUCAP; P00550, PTMA_ECOLI; DR P27547, PTMA_ENTFA; Q9XBM7, PTMA_KLEPN; P75145, PTMA_MYCPN; DR Q9CLY8, PTMA_PASMU; P17875, PTMA_STAAM; P17876, PTMA_STACA; DR Q02420, PTMA_STRMU; Q9KKQ7, PTMA_VIBCH; Q9K678, PTMB_BACHD; DR P50852, PTMB_BACST; O65989, PTMB_CLOAB; P75146, PTMB_MYCPN; DR P28008, PTMB_STACA; Q46072, PTNA_CORGL; P08186, PTNA_ECOLI; DR P19642, PTOA_ECOLI; P42909, PTPB_ECOLI; P42904, PTPV_ECOLI; DR P37080, PTRA_KLEPN; P37081, PTRB_KLEPN; Q04938, PTSA_LACLA; DR P43470, PTSA_PEDPE; P12655, PTSA_STRMU; P05306, PTSB_BACSU; DR P27219, PTSB_KLEPN; Q9CJZ2, PTSB_PASMU; P08470, PTSB_SALTY; DR P51184, PTSB_STAXY; P22825, PTSB_VIBAL; Q9KVD9, PTSB_VIBCH; DR P30335, PTSN_BRAJA; P31222, PTSN_ECOLI; P17162, PTSN_KLEPN; DR P33670, PTSN_PSEPU; P39794, PTTB_BACSU; P36672, PTTB_ECOLI; DR P32155, PTVA_ECOLI; P32154, PTVB_ECOLI; P32673, PTWB_ECOLI; DR P32676, PTWX_ECOLI; P39303, PTXA_ECOLI; P75292, PTXA_MYCPN; DR P39302, PTXB_ECOLI; Q9EXD8, PTXB_MYCPN; P32058, PTYA_ECOLI; DR P32059, PTYC_ECOLI; P39363, SGCA_ECOLI; P58035, SGCB_ECOLI; DR P36881, YADI_ECOLI; P39816, YBFS_BACSU; P77272, YFEV_ECOLI; DR P77579, YPDG_ECOLI; P76525, YPDH_ECOLI; P50829, YPQE_BACSU; DR P39584, YWBA_BACSU; // ID 2.7.1.70 DE Protamine kinase. AN Histone kinase. CA ATP + [protamine] = ADP + [protamine] O-phospho-L-serine. CC -!- Phosphorylates protamines and histones. CC -!- Requires cyclic AMP. // ID 2.7.1.71 DE Shikimate kinase. CA ATP + shikimate = ADP + shikimate 3-phosphate. PR PROSITE; PDOC00868; DR Q9WYI3, ARKB_THEMA; P07547, ARO1_EMENI; Q12659, ARO1_PNECA; DR Q9P7R0, ARO1_SCHPO; P08566, ARO1_YEAST; Q9YEK6, AROK_AERPE; DR O67925, AROK_AQUAE; Q9SJ05, AROK_ARATH; O29730, AROK_ARCFU; DR Q9KFH9, AROK_BACHD; P37944, AROK_BACSU; P57605, AROK_BUCAI; DR Q8K938, AROK_BUCAP; P59488, AROK_BUCBP; Q9PK27, AROK_CHLMU; DR Q9Z6M1, AROK_CHLPN; O84372, AROK_CHLTR; Q9X5D1, AROK_CORGL; DR P24167, AROK_ECOLI; P43880, AROK_HAEIN; Q9HQB0, AROK_HALN1; DR Q9ZMS3, AROK_HELPJ; P56073, AROK_HELPY; Q9CEU1, AROK_LACLA; DR P43906, AROK_LACLC; Q00497, AROK_LYCES; Q8TR06, AROK_METAC; DR Q58835, AROK_METJA; Q8PUH2, AROK_METMA; O26896, AROK_METTH; DR Q9CCS5, AROK_MYCLE; P95014, AROK_MYCTU; O50467, AROK_NEIGO; DR Q9JQV1, AROK_NEIMA; P57925, AROK_PASMU; P34003, AROK_PSEAE; DR Q9V1H6, AROK_PYRAB; Q8U0A5, AROK_PYRFU; Q8XFE9, AROK_SALTY; DR P72796, AROK_SYNY3; Q9HLE5, AROK_THEAC; Q9KNV1, AROK_VIBCH; DR Q87L67, AROK_VIBPA; Q8DCM1, AROK_VIBVU; Q8D1X8, AROK_WIGBR; DR Q9PDP4, AROK_XYLFA; Q87DU8, AROK_XYLFT; Q8ZJF7, AROK_YERPE; DR P08329, AROL_ECOLI; P10880, AROL_ERWCH; Q8XEP9, AROL_SALTY; DR Q8ZC15, AROL_YERPE; // ID 2.7.1.72 DE Streptomycin 6-kinase. AN Streptidine kinase. AN Streptomycin 6-phosphotransferase. AN APH(6). CA ATP + streptomycin = ADP + streptomycin 6-phosphate. CC -!- dATP can replace ATP. CC -!- Dihydrostreptomycin, streptidine and 2-deoxystreptidine can act as CC acceptors. DR P18622, STRA_STRGA; P08077, STRA_STRGR; // ID 2.7.1.73 DE Inosine kinase. AN Inosine-guanosine kinase. CA ATP + inosine = ADP + IMP. PR PROSITE; PDOC00504; DR P22937, INGK_ECOLI; // ID 2.7.1.74 DE Deoxycytidine kinase. CA NTP + deoxycytidine = NDP + CMP. CC -!- Cytosine arabinoside can act as acceptors. CC -!- All natural nucleoside triphosphates (except dCTP) can act as donors. DR P21974, DCK1_FOWPV; Q9J579, DCK2_FOWPV; P27707, DCK_HUMAN ; DR P43346, DCK_MOUSE ; P48769, DCK_RAT ; // ID 2.7.1.75 DE Transferred entry: 2.7.1.21. // ID 2.7.1.76 DE Deoxyadenosine kinase. CA ATP + deoxyadenosine = ADP + dAMP. CC -!- Deoxyguanosine can also act as acceptor. CC -!- Possibly identical with EC 2.7.1.74. DR Q59483, DGK1_LACAC; // ID 2.7.1.77 DE Nucleoside phosphotransferase. CA A nucleotide + 2'-deoxynucleoside = a nucleoside + 2'-deoxynucleoside CA 5'-monophosphate. CC -!- Phenyl phosphate and nucleoside 3'-phosphates can act as donors, CC although not so well as nucleoside 5'-phosphates. // ID 2.7.1.78 DE Polynucleotide 5'-hydroxyl-kinase. CA ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA. CC -!- Also acts on 5'-dephospho-RNA 3'-mononucleotides. DR P06855, KIPN_BPT4 ; O13911, PNK1_SCHPO; P41476, PNKL_NPVAC; // ID 2.7.1.79 DE Diphosphate--glycerol phosphotransferase. AN Pyrophosphate--glycerol phosphotransferase. CA Diphosphate + glycerol = phosphate + glycerol 1-phosphate. CC -!- May be identical with EC 3.1.3.9. // ID 2.7.1.80 DE Diphosphate--serine phosphotransferase. AN Pyrophosphate--serine phosphotransferase. CA Diphosphate + L-serine = phosphate + O-phospho-L-serine. // ID 2.7.1.81 DE Hydroxylysine kinase. CA GTP + 5-hydroxy-L-lysine = GDP + 5-phosphonooxy-L-lysine. CC -!- Both the natural 5-hydroxy-L-lysine and its 5-epimer act as CC acceptors. // ID 2.7.1.82 DE Ethanolamine kinase. CA ATP + ethanolamine = ADP + O-phosphoethanolamine. DI Ethanolaminosis; MIM:227150. DR P54352, EAS_DROME ; Q9HBU6, EKI1_HUMAN; Q9D4V0, EKI1_MOUSE; DR Q03764, EKI1_YEAST; Q9Y259, KICE_HUMAN; O55229, KICE_MOUSE; DR O54783, KICE_RAT ; // ID 2.7.1.83 DE Pseudouridine kinase. CA ATP + pseudouridine = ADP + pseudouridine 5'-phosphate. // ID 2.7.1.84 DE Alkylglycerone kinase. CA ATP + O-alkylglycerone = ADP + O-alkylglycerone phosphate. // ID 2.7.1.85 DE Beta-glucoside kinase. CA ATP + cellobiose = ADP + 6-phospho-beta-D-glucosyl-(1,4)-D-glucose. CC -!- Phosphorylates a number of beta-D-glucosides. CC -!- GTP, CTP, ITP and UTP can also act as donors. // ID 2.7.1.86 DE NADH kinase. CA ATP + NADH = ADP + NADPH. CC -!- CTP, ITP, UTP and GTP can also act as phosphate donors (in decreasing CC order of activity). CC -!- Specific for NADH. CC -!- Activated by acetate. CC -!- Formerly EC 2.7.1.96. // ID 2.7.1.87 DE Streptomycin 3''-kinase. AN Streptomycin 3''-phosphotransferase. CA ATP + streptomycin = ADP + streptomycin 3''-phosphate. CC -!- Also phosphorylates dihydrostreptomycin, 3'-deoxydihydrostreptomycin CC and their 6-phosphates. DR P18150, APHE_STRGR; P13082, STR_KLEPN ; // ID 2.7.1.88 DE Dihydrostreptomycin-6-phosphate 3'-alpha-kinase. CA ATP + dihydrostreptomycin 6-phosphate = ADP + dihydrostreptomycin CA 3'-alpha-6-bisphosphate. CC -!- 3'-deoxydihydrostreptomycin 6-phosphate can also act as acceptor. // ID 2.7.1.89 DE Thiamine kinase. CA ATP + thiamine = ADP + thiamine phosphate. CC -!- Formerly EC 2.7.1.96. // ID 2.7.1.90 DE Diphosphate--fructose-6-phosphate 1-phosphotransferase. AN Pyrophosphate--fructose-6-phosphate 1-phosphotransferase. AN 6-phosphofructokinase (pyrophosphate). AN 6-phosphofructokinase (diphosphate). AN Pyrophosphate-dependent 6-phosphofructose-1-kinase. AN Diphosphate-dependent 6-phosphofructose-1-kinase. CA Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose CA 1,6-bisphosphate. DR Q41140, PFPA_RICCO; P21342, PFPA_SOLTU; Q41141, PFPB_RICCO; DR P21343, PFPB_SOLTU; Q9AGC0, PFP_AMYMD ; Q59126, PFP_AMYME ; DR Q9KH71, PFP_DICTH ; P29495, PFP_PROFR ; // ID 2.7.1.91 DE Sphinganine kinase. AN Dihydrosphingosine kinase. CA ATP + sphinganine = ADP + sphinganine 1-phosphate. // ID 2.7.1.92 DE 5-dehydro-2-deoxygluconokinase. AN 5-keto-2-deoxygluconokinase. CA ATP + 5-dehydro-2-deoxy-D-gluconate = ADP + 6-phospho-5-dehydro-2- CA deoxy-D-gluconate. // ID 2.7.1.93 DE Alkylglycerol kinase. CA ATP + 1-O-alkyl-sn-glycerol = ADP + 1-O-alkyl-sn-glycerol 3-phosphate. // ID 2.7.1.94 DE Acylglycerol kinase. AN Monoacylglycerol kinase. CA ATP + acylglycerol = ADP + acyl-sn-glycerol 3-phosphate. CC -!- Acts on both 1- and 2-acylglycerols. // ID 2.7.1.95 DE Kanamycin kinase. AN Aminoglycoside 3'-phosphotransferase. AN Neomycin-kanamycin phosphotransferase. AN APH(3'). CA ATP + kanamycin = ADP + kanamycin 3'-phosphate. CC -!- Also acts on the antibiotics neomycin, paromomycin, neamine, CC paromamine, vistamycin and gentamicin A. An enzyme from Pseudomonas CC aeruginosa also acts on butirosin. DR P00551, KKA1_ECOLI; Q03447, KKA1_SALTY; P00552, KKA2_KLEPN; DR P00554, KKA3_ENTFA; P00553, KKA4_BACCI; P00555, KKA5_STRFR; DR P09885, KKA6_ACIBA; P14508, KKA7_CAMJE; P14509, KKA8_ECOLI; DR P13250, KKA9_STRRI; Q02149, KKIH_LACLA; // ID 2.7.1.96 DE Transferred entry: 2.7.1.86. // ID 2.7.1.97 DE Transferred entry: 2.7.1.125. // ID 2.7.1.98 DE Deleted entry. // ID 2.7.1.99 DE [Pyruvate dehydrogenase(lipoamide)] kinase. CA ATP + [pyruvate dehydrogenase (lipoamide)] = ADP + [pyruvate CA dehydrogenase (lipoamide)] phosphate. CC -!- A mitochondrial enzyme associated with the pyruvate dehydrogenase CC complex. CC -!- Phosphorylation inactivates EC 1.2.4.1. DR Q15118, PDK1_HUMAN; Q63065, PDK1_RAT ; Q15119, PDK2_HUMAN; DR Q9JK42, PDK2_MOUSE; Q64536, PDK2_RAT ; Q15120, PDK3_HUMAN; DR Q16654, PDK4_HUMAN; O70571, PDK4_MOUSE; O54937, PDK4_RAT ; DR O88345, PDK4_SPETR; O02623, PDK_ASCSU ; Q02332, PDK_CAEEL ; DR P91622, PDK_DROME ; // ID 2.7.1.100 DE 5-methylthioribose kinase. CA ATP + S(5)-methyl-5-thio-D-ribose = ADP + S(5)-methyl-5-thio-D-ribose CA 1-phosphate. CC -!- Also acts, more slowly, on CTP. // ID 2.7.1.101 DE Tagatose kinase. AN D-tagatose 6-phosphate kinase. CA ATP + D-tagatose = ADP + D-tagatose 6-phosphate. // ID 2.7.1.102 DE Hamamelose kinase. CA ATP + D-hamamelose = ADP + D-hamamelose 2'-phosphate. CC -!- Also acts, more slowly, on D-hamamelitol. // ID 2.7.1.103 DE Viomycin kinase. AN Viomycin phosphotransferase. AN Capreomycin phosphotransferase. CA ATP + viomycin = ADP + O-phosphoviomycin. CC -!- Also acts on capreomycins. CC -!- A serine residue in the peptide antibiotics acts as phosphate- CC acceptor. DR P18623, VPH_STRVI ; // ID 2.7.1.104 DE Diphosphate-protein phosphotransferase. AN Pyrophosphate-protein phosphotransferase. CA Diphosphate + [microsomal-membrane protein] = phosphate + CA [microsomal-membrane protein] phosphate. // ID 2.7.1.105 DE 6-phosphofructo-2-kinase. AN Phosphofructokinase 2. CA ATP + D-fructose 6-phosphate = ADP + D-fructose 2,6-bisphosphate. CC -!- Not identical with EC 2.7.1.11. CC -!- The enzyme co-purifies with EC 3.1.3.46. PR PROSITE; PDOC00158; DR P40433, 6P21_YEAST; Q12471, 6P22_YEAST; P49872, F261_BOVIN; DR P16118, F261_HUMAN; P70266, F261_MOUSE; P07953, F261_RAT ; DR P26285, F262_BOVIN; O60825, F262_HUMAN; P70265, F262_MOUSE; DR Q9JJH5, F262_RAT ; Q28901, F263_BOVIN; Q16875, F263_HUMAN; DR O35552, F263_RAT ; Q16877, F264_HUMAN; P25114, F264_RAT ; DR Q91348, F26L_CHICK; Q21122, F26_CAEEL ; Q91309, F26_RANCA ; // ID 2.7.1.106 DE Glucose-1,6-bisphosphate synthase. CA 3-phospho-D-glyceroyl phosphate + D-glucose 1-phosphate = 3-phospho-D- CA glycerate + D-glucose 1,6-bisphosphate. CC -!- D-glucose 6-phosphate can act as acceptor, forming D-glucose CC 1,6-bisphosphate. // ID 2.7.1.107 DE Diacylglycerol kinase. AN Diglyceride kinase. AN DGK. CA ATP + 1,2-diacylglycerol = ADP + 1,2-diacylglycerol 3-phosphate. PR PROSITE; PDOC00820; DR Q39017, KDG1_ARATH; P23743, KDGA_HUMAN; O88673, KDGA_MOUSE; DR P20192, KDGA_PIG ; P51556, KDGA_RAT ; Q9Y6T7, KDGB_HUMAN; DR P49621, KDGB_RAT ; Q16760, KDGD_HUMAN; Q64398, KDGD_MESAU; DR Q09103, KDGE_DROME; P52429, KDGE_HUMAN; Q9R1C6, KDGE_MOUSE; DR P49619, KDGG_HUMAN; Q91WG7, KDGG_MOUSE; P49620, KDGG_RAT ; DR O75912, KDGI_HUMAN; P19638, KDGL_BACSU; Q03603, KDGL_CAEEL; DR Q01583, KDGL_DROME; P00556, KDGL_ECOLI; P44424, KDGL_HAEIN; DR Q9ZLE0, KDGL_HELPJ; P56411, KDGL_HELPY; P29945, KDGL_PSEDE; DR Q06119, KDGL_RHIME; Q05888, KDGL_STRMU; Q55143, KDGL_SYNY3; DR P52824, KDGT_HUMAN; Q13574, KDGZ_HUMAN; O08560, KDGZ_RAT ; // ID 2.7.1.108 DE Dolichol kinase. CA CTP + dolichol = CDP + dolichyl phosphate. DR P20048, SC59_YEAST; // ID 2.7.1.109 DE [Hydroxymethylglutaryl-CoA reductase(NADPH)] kinase. AN Reductase kinase. CA ATP + [3-hydroxy-3-methylglutaryl-CoA reductase (NADPH)] = ADP + CA [3-hydroxy-3-methylglutaryl-CoA reductase (NADPH)] phosphate. CC -!- EC 1.1.1.34 is inactivated by the phosphorylation of the enzyme CC protein. CC -!- Histones can also act as acceptors. // ID 2.7.1.110 DE Dephospho-[reductase kinase] kinase. AN Reductase kinase kinase. CA ATP + dephospho[[3-hydroxy-3-methylglutaryl-CoA reductase (NADPH)] CA kinase] = ADP + [[3-hydroxy-3-methylglutaryl-CoA reductase (NADPH)] CA kinase]. CC -!- Phosphorylates and activates EC 2.7.1.109 which has been inactivated CC by EC 3.1.3.16. // ID 2.7.1.111 DE Transferred entry: 2.7.1.128. // ID 2.7.1.112 DE Protein-tyrosine kinase. AN Tyrosylprotein kinase. AN Tyrosine-protein kinase. AN Protein kinase (tyrosine). AN Hydroxyaryl-protein kinase. CA ATP + a protein tyrosine = ADP + protein tyrosine phosphate. PR PROSITE; PDOC00100; DR P13368, 7LES_DROME; P20806, 7LES_DROVI; P03949, ABL1_CAEEL; DR P00519, ABL1_HUMAN; P00520, ABL1_MOUSE; P42684, ABL2_HUMAN; DR P11681, ABL_CALVI ; P00522, ABL_DROME ; P10447, ABL_FSVHY ; DR P00521, ABL_MLVAB ; Q9UM73, ALK_HUMAN ; P97793, ALK_MOUSE ; DR Q46631, AMSA_ERWAM; Q01742, BFR2_HUMAN; P51451, BLK_HUMAN ; DR P16277, BLK_MOUSE ; P51813, BMX_HUMAN ; P08630, BTKL_DROME; DR Q06187, BTK_HUMAN ; P35991, BTK_MOUSE ; P39851, CAPB_STAAU; DR Q9VBW3, CD96_DROME; P18460, CEK2_CHICK; P18461, CEK3_CHICK; DR Q9AHD2, CPD1_STRPN; Q54520, CPD2_STRPN; Q04663, CPSD_STRA3; DR Q9AFI1, CPSD_STRA5; Q9S0S7, CPSD_STRAG; P41239, CSK_CHICK ; DR P41240, CSK_HUMAN ; P41241, CSK_MOUSE ; P32577, CSK_RAT ; DR Q08345, DDR1_HUMAN; Q03146, DDR1_MOUSE; Q63474, DDR1_RAT ; DR Q16832, DDR2_HUMAN; Q62371, DDR2_MOUSE; Q10656, EG15_CAEEL; DR P13387, EGFR_CHICK; P04412, EGFR_DROME; P00533, EGFR_HUMAN; DR P55245, EGFR_MACMU; Q01279, EGFR_MOUSE; Q91845, EP4A_XENLA; DR Q91694, EP4B_XENLA; P21709, EPA1_HUMAN; Q60750, EPA1_MOUSE; DR P29317, EPA2_HUMAN; Q03145, EPA2_MOUSE; O13146, EPA3_BRARE; DR P29318, EPA3_CHICK; P29320, EPA3_HUMAN; P29319, EPA3_MOUSE; DR O08680, EPA3_RAT ; O13148, EPA4_BRARE; Q07496, EPA4_CHICK; DR P54764, EPA4_HUMAN; Q03137, EPA4_MOUSE; P54755, EPA5_CHICK; DR P54756, EPA5_HUMAN; Q60629, EPA5_MOUSE; P54757, EPA5_RAT ; DR Q62413, EPA6_MOUSE; P54758, EPA6_RAT ; O42422, EPA7_CHICK; DR Q15375, EPA7_HUMAN; Q61772, EPA7_MOUSE; P54759, EPA7_RAT ; DR P29322, EPA8_HUMAN; O09127, EPA8_MOUSE; P29321, EPA8_RAT ; DR Q07494, EPB1_CHICK; P54762, EPB1_HUMAN; P58593, EPB1_RALSO; DR P09759, EPB1_RAT ; P28693, EPB2_CHICK; Q90344, EPB2_COTJA; DR P29323, EPB2_HUMAN; P54763, EPB2_MOUSE; Q45409, EPB2_RALSO; DR O13147, EPB3_BRARE; Q07498, EPB3_CHICK; P54753, EPB3_HUMAN; DR P54754, EPB3_MOUSE; Q91735, EPB3_XENLA; P54760, EPB4_HUMAN; DR P54761, EPB4_MOUSE; Q07497, EPB5_CHICK; Q91571, EPBA_XENLA; DR Q91736, EPBB_XENLA; P04626, ERB2_HUMAN; Q60553, ERB2_MESAU; DR P70424, ERB2_MOUSE; P06494, ERB2_RAT ; P21860, ERB3_HUMAN; DR Q61526, ERB3_MOUSE; Q62799, ERB3_RAT ; Q15303, ERB4_HUMAN; DR Q61527, ERB4_MOUSE; Q62956, ERB4_RAT ; P00534, ERBB_ALV ; DR P00535, ERBB_AVIER; P11273, ERBB_AVIEU; P58764, ETK_ECO27 ; DR Q8XC28, ETK_ECO57 ; P38134, ETK_ECOLI ; Q00944, FAK1_CHICK; DR Q05397, FAK1_HUMAN; P34152, FAK1_MOUSE; O35346, FAK1_RAT ; DR Q91738, FAK1_XENLA; Q14289, FAK2_HUMAN; Q9QVP9, FAK2_MOUSE; DR P70600, FAK2_RAT ; P16591, FER_HUMAN ; P14238, FES_FELCA ; DR P00542, FES_FSVGA ; P00543, FES_FSVST ; P07332, FES_HUMAN ; DR P16879, FES_MOUSE ; P21804, FGR1_CHICK; Q07407, FGR1_DROME; DR P11362, FGR1_HUMAN; P16092, FGR1_MOUSE; Q04589, FGR1_RAT ; DR P22182, FGR1_XENLA; Q09147, FGR2_DROME; P21802, FGR2_HUMAN; DR P21803, FGR2_MOUSE; Q03364, FGR2_XENLA; P22607, FGR3_HUMAN; DR Q61851, FGR3_MOUSE; P22455, FGR4_HUMAN; Q03142, FGR4_MOUSE; DR P00544, FGR_FSVGR ; P09769, FGR_HUMAN ; P14234, FGR_MOUSE ; DR P09760, FLK_RAT ; P36888, FLT3_HUMAN; Q00342, FLT3_MOUSE; DR P00541, FPS_AVISP ; P18106, FPS_DROME ; P00530, FPS_FUJSV ; DR P42685, FRK_HUMAN ; Q05876, FYN_CHICK ; P06241, FYN_HUMAN ; DR P39688, FYN_MOUSE ; P13406, FYN_XENLA ; P27446, FYN_XIPHE ; DR P08631, HCK_HUMAN ; Q95M30, HCK_MACFA ; P08103, HCK_MOUSE ; DR P50545, HCK_RAT ; P53356, HT16_HYDAT; Q25197, HTK7_HYDAT; DR Q05688, IG1R_BOVIN; P08069, IG1R_HUMAN; Q60751, IG1R_MOUSE; DR Q29000, IG1R_PIG ; P24062, IG1R_RAT ; O02466, ILPR_BRALA; DR Q93105, INSR_AEDAE; P09208, INSR_DROME; P06213, INSR_HUMAN; DR Q28516, INSR_MACMU; P15208, INSR_MOUSE; P15127, INSR_RAT ; DR P14617, IRR_CAVPO ; P14616, IRR_HUMAN ; Q9WTL4, IRR_MOUSE ; DR Q64716, IRR_RAT ; Q08881, ITK_HUMAN ; Q03526, ITK_MOUSE ; DR O12990, JAK1_BRARE; Q09178, JAK1_CYPCA; P23458, JAK1_HUMAN; DR P52332, JAK1_MOUSE; O60674, JAK2_HUMAN; Q62120, JAK2_MOUSE; DR Q62689, JAK2_RAT ; P52333, JAK3_HUMAN; Q62137, JAK3_MOUSE; DR Q63272, JAK3_RAT ; Q24592, JAK_DROME ; P13369, KFMS_FELCA; DR P00545, KFMS_FSVMD; P07333, KFMS_HUMAN; P09581, KFMS_MOUSE; DR Q00495, KFMS_RAT ; P34891, KI15_CAEEL; P34892, KI16_CAEEL; DR Q10925, KI25_CAEEL; P34265, KI28_CAEEL; P43481, KIT_BOVIN ; DR O97799, KIT_CANFA ; Q28317, KIT_CAPHI ; Q08156, KIT_CHICK ; DR Q28889, KIT_FELCA ; P04048, KIT_FSVHZ ; P10721, KIT_HUMAN ; DR P05532, KIT_MOUSE ; P29376, KLTK_HUMAN; P08923, KLTK_MOUSE; DR P32350, KNS1_YEAST; P00529, KROS_AVISU; P08941, KROS_CHICK; DR P08922, KROS_HUMAN; P43405, KSYK_HUMAN; P48025, KSYK_MOUSE; DR Q00655, KSYK_PIG ; Q64725, KSYK_RAT ; P18160, KYK1_DICDI; DR P18161, KYK2_DICDI; P42683, LCK_CHICK ; P06239, LCK_HUMAN ; DR P06240, LCK_MOUSE ; Q01621, LCK_RAT ; Q10156, LKH1_SCHPO; DR P24348, LT23_CAEEL; P07948, LYN_HUMAN ; P25911, LYN_MOUSE ; DR Q07014, LYN_RAT ; P42679, MATK_HUMAN; P41242, MATK_MOUSE; DR P41243, MATK_RAT ; Q12866, MERK_HUMAN; Q60805, MERK_MOUSE; DR P57097, MERK_RAT ; P08581, MET_HUMAN ; P16056, MET_MOUSE ; DR P97523, MET_RAT ; Q25410, MIPR_LYMST; P09619, PGDR_HUMAN; DR P05622, PGDR_MOUSE; Q05030, PGDR_RAT ; P16234, PGDS_HUMAN; DR P26618, PGDS_MOUSE; P20786, PGDS_RAT ; P26619, PGDS_XENLA; DR Q9I7F7, PR2_DROME ; Q13882, PTK6_HUMAN; Q64434, PTK6_MOUSE; DR O52788, PTK_ACIJO ; P07949, RET_HUMAN ; P35546, RET_MOUSE ; DR Q04912, RON_HUMAN ; Q62190, RON_MOUSE ; Q24488, ROR1_DROME; DR Q01973, ROR1_HUMAN; Q9Z139, ROR1_MOUSE; Q9V6K3, ROR2_DROME; DR Q01974, ROR2_HUMAN; Q9Z138, ROR2_MOUSE; P42159, RTK2_GEOCY; DR Q27324, RYK1_DROME; Q9V422, RYK2_DROME; P33497, RYK_AVIR3 ; DR P34925, RYK_HUMAN ; Q01887, RYK_MOUSE ; P23049, SEA_AVIET ; DR P42687, SPK1_DUGTI; P00528, SRC1_DROME; P13115, SRC1_XENLA; DR P13116, SRC2_XENLA; P15054, SRC_AVIS2 ; P00525, SRC_AVISR ; DR P14084, SRC_AVISS ; P14085, SRC_AVIST ; P00523, SRC_CHICK ; DR P12931, SRC_HUMAN ; P05480, SRC_MOUSE ; Q9WUD9, SRC_RAT ; DR P25020, SRC_RSVH1 ; P00526, SRC_RSVP ; P31693, SRC_RSVPA ; DR P00524, SRC_RSVSR ; P42686, SRK1_SPOLA; P42688, SRK2_SPOLA; DR P42689, SRK3_SPOLA; P42690, SRK4_SPOLA; Q9H3Y6, SRMS_HUMAN; DR Q62270, SRMS_MOUSE; P17713, STK_HYDAT ; P42680, TEC_HUMAN ; DR P24604, TEC_MOUSE ; Q06805, TIE1_BOVIN; P35590, TIE1_HUMAN; DR Q06806, TIE1_MOUSE; Q06807, TIE2_BOVIN; Q02763, TIE2_HUMAN; DR Q02858, TIE2_MOUSE; P18475, TOR_DROME ; O76997, TRK1_LYMST; DR Q91009, TRKA_CHICK; P04629, TRKA_HUMAN; P35739, TRKA_RAT ; DR Q91987, TRKB_CHICK; Q16620, TRKB_HUMAN; P15209, TRKB_MOUSE; DR Q63604, TRKB_RAT ; Q91044, TRKC_CHICK; Q16288, TRKC_HUMAN; DR P24786, TRKC_PIG ; Q03351, TRKC_RAT ; P42681, TXK_HUMAN ; DR P42682, TXK_MOUSE ; P29597, TYK2_HUMAN; Q9R117, TYK2_MOUSE; DR Q06418, TYO3_HUMAN; P55144, TYO3_MOUSE; P55146, TYO3_RAT ; DR P30530, UFO_HUMAN ; Q00993, UFO_MOUSE ; P17948, VGR1_HUMAN; DR P35969, VGR1_MOUSE; P53767, VGR1_RAT ; P52583, VGR2_COTJA; DR P35968, VGR2_HUMAN; P35918, VGR2_MOUSE; O08775, VGR2_RAT ; DR P35916, VGR3_HUMAN; P35917, VGR3_MOUSE; P54350, WEE1_DROME; DR P30291, WEE1_HUMAN; P47810, WEE1_MOUSE; Q63802, WEE1_RAT ; DR P47817, WEE1_XENLA; P83097, WSCK_DROME; Q8X7L9, WZC_ECO57 ; DR P76387, WZC_ECOLI ; Q8Z5G6, WZC_SALTI ; Q9F7B1, WZC_SALTY ; DR P13388, XMRK_XIPMA; Q48452, YC06_KLEPN; P00527, YES_AVISY ; DR Q28923, YES_CANFA ; P09324, YES_CHICK ; P07947, YES_HUMAN ; DR Q04736, YES_MOUSE ; P10936, YES_XENLA ; P27447, YES_XIPHE ; DR Q02977, YRK_CHICK ; Q19238, YS3J_CAEEL; P71051, YVEL_BACSU; DR P96716, YWQD_BACSU; P43403, ZA70_HUMAN; P43404, ZA70_MOUSE; // ID 2.7.1.113 DE Deoxyguanosine kinase. CA ATP + deoxyguanosine = ADP + dGMP. CC -!- Deoxyinosine can also act as acceptor. DR Q59484, DGK2_LACAC; Q16854, DGK_HUMAN ; Q9QX60, DGK_MOUSE ; // ID 2.7.1.114 DE AMP--thymidine kinase. AN Adenylate-nucleoside phosphotransferase. CA AMP + thymidine = adenosine + thymidine 5'-phosphate. CC -!- The deoxypyrimidine kinase complex induced by herpes simplex virus CC catalyzes this reaction as well as those of EC 2.7.1.21, CC EC 2.7.1.128, and EC 2.7.4.9. // ID 2.7.1.115 DE [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] kinase. AN Branched-chain alpha-ketoacid dehydrogenase kinase. CA ATP + [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] = ADP + CA [3-methyl-2-oxobutanoate dehydrogenase (lipoamide)] phosphate. CC -!- A mitochondrial enzyme associated with the branched-chain 2-oxoacid CC dehydrogenase complex. CC -!- Phosphorylation inactivates EC 1.2.4.4. DR O14874, BCKD_HUMAN; O55028, BCKD_MOUSE; Q00972, BCKD_RAT ; // ID 2.7.1.116 DE [Isocitrate dehydrogenase (NADP+)] kinase. AN Isocitrate dehydrogenase kinase. AN Isocitrate dehydrogenase kinase/phosphatase. AN IDH kinase/phosphatase. CA ATP + [isocitrate dehydrogenase (NADP+)] = ADP + [isocitrate CA dehydrogenase (NADP+)] phosphate. CC -!- Phosphorylates and inactivates EC 1.1.1.42. DR P11071, ACEK_ECOLI; P51067, ACEK_SALTY; // ID 2.7.1.117 DE [Myosin light-chain] kinase. AN Myosin light-chain kinase. AN Myosin kinase. AN Smooth-muscle-myosin-light-chain kinase. CA ATP + [myosin light-chain] = ADP + [myosin light-chain] phosphate. CF Calcium. CC -!- Requires calmodulin. CC -!- The 20 Kd light chain from smooth muscle myosin is phosphorylated CC more rapidly than any other acceptor, but light chains from other CC myosins and myosin itself can act as acceptors, more slowly. PR PROSITE; PDOC00100; DR Q9H1R3, KML2_HUMAN; Q8VCR8, KML2_MOUSE; P07313, KML2_RABIT; DR P20689, KML2_RAT ; P25323, KMLC_DICDI; Q28824, KMLS_BOVIN; DR P11799, KMLS_CHICK; Q15746, KMLS_HUMAN; P79280, KMLS_PIG ; DR P29294, KMLS_RABIT; O02827, KMLS_SHEEP; // ID 2.7.1.118 DE ADP--thymidine kinase. CA ADP + thymidine = AMP + thymidine 5'-phosphate. CC -!- The deoxypyrimidine kinase complex induced by herpes simplex virus CC catalyzes this reaction as well as those of EC 2.7.1.21, EC 2.7.1.114 CC and EC 2.7.4.9. // ID 2.7.1.119 DE Hygromycin-B kinase. AN Hygromycin B phosphotransferase. AN APH(7''). CA ATP + hygromycin B = ADP + 7''-O-phosphohygromycin B. CC -!- Phosphorylates the antibiotics hygromycin B, 1-N-hygromycin B and CC destomycin, but not hydromycin B2, at the 7''-hydroxyl group in the CC destomic acid ring. DR P00557, KHYB_ECOLI; P09979, KHYB_STRHY; // ID 2.7.1.120 DE Caldesmon kinase. CA ATP + [caldesmon] = ADP + [caldesmon] phosphate. CF Calcium. CC -!- Requires calmodulin. CC -!- Phosphorylation abolishes the ability of the protein caldesmon to CC bind actin and inhibit ATPase. CC -!- The enzyme appears to be identical with caldesmon; the reaction is CC an autophosphorylation. // ID 2.7.1.121 DE Phosphoenolpyruvate--glycerone phosphotransferase. CA Phosphoenolpyruvate + glycerone = pyruvate + glycerone phosphate. // ID 2.7.1.122 DE Xylitol kinase. AN Xylitol phosphotransferase. CA ATP + xylitol = ADP + xylitol 5-phosphate. // ID 2.7.1.123 DE Calcium/calmodulin-dependent protein kinase. AN Calcium/calmodulin-dependent protein kinase type II. AN Microtubule-associated protein 2 kinase. CA ATP + protein = ADP + O-phosphoprotein. CF Calcium. CC -!- Requires calmodulin. CC -!- A wide range of proteins can act as acceptor, including vimentin, CC synapsin, glycogen synthase and myosin light-chains and the CC microtubule-associated tau protein. CC -!- Not identical with EC 2.7.1.117, EC 2.7.1.120 or EC 2.7.1.135. PR PROSITE; PDOC00100; DR Q24210, CAKI_DROME; Q00771, KCC1_EMENI; Q14012, KCC1_HUMAN; DR O14408, KCC1_METAN; Q91YS8, KCC1_MOUSE; Q63450, KCC1_RAT ; DR Q9P7I2, KCC1_SCHPO; P27466, KCC1_YEAST; O42844, KCC2_SCHPO; DR P22517, KCC2_YEAST; Q16566, KCC4_HUMAN; P08414, KCC4_MOUSE; DR P13234, KCC4_RAT ; Q9UQM7, KCCA_HUMAN; P11798, KCCA_MOUSE; DR P11275, KCCA_RAT ; Q13554, KCCB_HUMAN; P28652, KCCB_MOUSE; DR P08413, KCCB_RAT ; Q13557, KCCD_HUMAN; P15791, KCCD_RAT ; DR Q13555, KCCG_HUMAN; Q923T9, KCCG_MOUSE; P11730, KCCG_RAT ; DR Q07250, KCCS_MALDO; // ID 2.7.1.124 DE Tyrosine 3-monooxygenase kinase. CA ATP + [tyrosine-3-monooxygenase] = ADP + [tyrosine-3-monooxygenase] CA phosphate. CC -!- Activates EC 1.14.16.2 by phosphorylation. CC -!- Specific for this substrate, with which it co-purifies. // ID 2.7.1.125 DE Rhodopsin kinase. CA ATP + [rhodopsin] = ADP + [rhodopsin] phosphate. CC -!- Acts on the bleached or activated form of rhodopsin. CC -!- Also phosphorylates the beta-adrenergic receptor, but more slowly. CC -!- Does not act on casein, histones or phosphovitin. CC -!- Inhibited by Zn(2+) and digitonin. CC -!- Cf. EC 2.7.1.126. CC -!- Formerly EC 2.7.1.97. PR PROSITE; PDOC00100; DR P28327, RK_BOVIN ; Q15835, RK_HUMAN ; Q9WVL4, RK_MOUSE ; DR Q63651, RK_RAT ; // ID 2.7.1.126 DE [Beta-adrenergic-receptor] kinase. AN Beta-adrenergic receptor kinase. CA ATP + [beta-adrenergic receptor] = ADP + [beta-adrenergic receptor] CA phosphate. CC -!- Acts on the agonist-occupied form of the receptor. CC -!- Also phosphorylates rhodopsin, but more slowly. CC -!- Does not act on casein or histones. CC -!- Inhibited by NH(3+) and digitonin; unaffected by cyclic-AMP. CC -!- Cf. EC 2.7.1.125. PR PROSITE; PDOC00100; DR P21146, ARK1_BOVIN; P25098, ARK1_HUMAN; Q64682, ARK1_MESAU; DR P26817, ARK1_RAT ; P26818, ARK2_BOVIN; P35626, ARK2_HUMAN; DR P26819, ARK2_RAT ; // ID 2.7.1.127 DE Inositol-trisphosphate 3-kinase. AN 1D-myo-inositol-trisphosphate 3-kinase. AN Inositol 1,4,5-trisphosphate 3-kinase. AN IP3K. AN IP3 3-kinase. CA ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol CA 1,3,4,5-tetrakisphosphate. CF Calcium. DR P23677, IP3K_HUMAN; P17105, IP3K_RAT ; P27987, IP3L_HUMAN; DR P42335, IP3L_RAT ; // ID 2.7.1.128 DE [Acetyl-CoA carboxylase] kinase. CA ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] CA phosphate. CC -!- Phosphorylates and inactivates EC 6.4.1.2. CC -!- Formerly EC 2.7.1.111. // ID 2.7.1.129 DE [Myosin heavy-chain] kinase. AN Myosin heavy-chain kinase. CA ATP + [myosin heavy-chain] = ADP + [myosin heavy-chain] phosphate. CC -!- The enzyme from Dictyostelium sp. brings about phosphorylation of CC the heavy chains of Dictyostelium myosin, inhibiting the actin- CC activated ATPase activity of the myosin. CC -!- One threonine residue in each heavy chain acts as acceptor. PR PROSITE; PDOC00100; DR P42527, KMHA_DICDI; P90648, KMHB_DICDI; P34125, KMHC_DICDI; // ID 2.7.1.130 DE Tetraacyldisaccharide 4'-kinase. AN Lipid-A 4'-kinase. CA ATP + 2,3-bis(3-hydroxytetradecanoyl)-D-glucosaminyl-(beta-D-1,6)-2,3- CA bis(3-hydroxytetradecanoyl)-D-glucosaminyl beta-phosphate = ADP + CA 2,3,2',3'-tetrakis(3-hydroxytetradecanoyl)-D-glucosaminyl-1,6-beta-D- CA glucosamine 1,4'-bisphosphate. CC -!- Involved with EC 2.3.1.129 and 2.4.1.182 in the biosynthesis of CC the phosphorylated glycolipid, lipid A, in the outer membrane of CC E.coli. DR Q8UHI5, LPXK_AGRT5; O67572, LPXK_AQUAE; Q8YB72, LPXK_BRUME; DR Q9PPA9, LPXK_CAMJE; P58184, LPXK_CAUCR; Q9PJZ4, LPXK_CHLMU; DR Q9Z823, LPXK_CHLPN; O84407, LPXK_CHLTR; Q8XDH0, LPXK_ECO57; DR P27300, LPXK_ECOLI; Q47909, LPXK_FRANO; P44491, LPXK_HAEIN; DR Q9ZMB1, LPXK_HELPJ; O25095, LPXK_HELPY; Q9JVE4, LPXK_NEIMA; DR Q9K0D7, LPXK_NEIMB; Q9CMG8, LPXK_PASMU; Q9HZM3, LPXK_PSEAE; DR Q8XWE4, LPXK_RALSO; P58185, LPXK_RHILO; Q92RP7, LPXK_RHIME; DR Q92GN1, LPXK_RICCN; P58186, LPXK_RICMO; Q9ZCL0, LPXK_RICPR; DR P58187, LPXK_RICRI; P58188, LPXK_RICTY; Q8Z801, LPXK_SALTI; DR Q8ZQC2, LPXK_SALTY; Q9KQX0, LPXK_VIBCH; Q87R15, LPXK_VIBPA; DR Q8DAV1, LPXK_VIBVU; Q8D2U9, LPXK_WIGBR; Q8PKS4, LPXK_XANAC; DR Q8P8W5, LPXK_XANCP; Q9PEE6, LPXK_XYLFA; Q87EE9, LPXK_XYLFT; DR Q8ZGA8, LPXK_YERPE; // ID 2.7.1.131 DE [Low-density lipoprotein receptor] kinase. AN Low-density lipoprotein receptor kinase. AN LDL receptor kinase. CA ATP + [low-density lipoprotein receptor] L-serine = ADP + [low-density CA lipoprotein receptor] O-phospho-L-serine. CC -!- Phosphorylates the serine-833 in the cytoplasmic domain of the CC low-density lipoprotein receptor. CC -!- GTP can act instead of ATP. // ID 2.7.1.132 DE Tropomyosin kinase. CA ATP + [tropomyosin] = ADP + [tropomyosin] O-phospho-L-serine. CC -!- Also phosphorylates casein. // ID 2.7.1.133 DE Transferred entry: 2.7.1.134. // ID 2.7.1.134 DE Inositol-tetrakisphosphate 1-kinase. AN 1D-myo-inositol-tetrakisphosphate 1-kinase. AN Inositol-trisphosphate 6-kinase. AN 1D-myo-inositol-trisphosphate 6-kinase. AN ATP:1D-myo-inositol-1,3,4-trisphosphate 6-phosphotransferase. AN Inositol-trisphosphate 5-kinase. AN 1D-myo-inositol-trisphosphate 5-kinase. AN ATP:1D-myo-inositol-1,3,4-trisphosphate 5-phosphotransferase. CA ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol CA 1,3,4,5,6-pentakisphosphate. CC -!- This enzyme also phosphorylates Ins(1,3,4)P(3) on O-5 and O-6. CC -!- The phosphotransfer from ATP to either inositol 1,3,4-trisphosphate CC or inositol 3,4,5,6-tetrakisphosphate appears to be freely CC reversible to the extent that the enzyme can act like an inositol CC polyphosphate phosphatase in the presence of ADP. CC -!- It can also catalyze an isomerization between Ins(1,3,4,5)P(4) and CC Ins(1,3,4,6)P(4) in the presence of ADP. CC -!- Formerly EC 2.7.1.133 and EC 2.7.1.139. // ID 2.7.1.135 DE [Tau protein] kinase. CA ATP + [tau protein] = ADP + [tau protein] O-phospho-L-serine. CC -!- Activated by tubulin. CC -!- Different from EC 2.7.1.123: not activated by calmodulin, cyclic CC nucleotides or calcium. CC -!- Involved in the formation of paired helical filaments in brain. // ID 2.7.1.136 DE Macrolide 2'-kinase. CA ATP + oleandomycin = ADP + oleandomycin 2'-O-phosphate. CC -!- Erythromycin, spiramycin and some other macrolide antibiotics can CC also act as acceptors. // ID 2.7.1.137 DE Phosphatidylinositol 3-kinase. AN 1-phosphatidylinositol 3-kinase. AN PI3-kinase. AN PtdIns-3-kinase. AN Type III phosphoinositide 3-kinase. AN Type I phosphatidylinositol kinase. CA ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo- CA inositol 3-phosphate. PR PROSITE; PDOC00710; DR Q94125, AGE1_CAEEL; P54673, P3K1_DICDI; P42347, P3K1_SOYBN; DR P54674, P3K2_DICDI; P42348, P3K2_SOYBN; P54675, P3K3_DICDI; DR P54676, P3K4_DICDI; P42339, PI3K_ARATH; O14356, TOR1_SCHPO; DR P35169, TOR1_YEAST; Q9Y7K2, TOR2_SCHPO; P32600, TOR2_YEAST; DR Q92213, VP34_CANAL; P50520, VP34_SCHPO; P22543, VP34_YEAST; // ID 2.7.1.138 DE Ceramide kinase. AN Acylsphingosine kinase. CA ATP + ceramide = ADP + ceramide 1-phosphate. DR Q8TCT0, CEK1_HUMAN; Q8K4Q7, CEK1_MOUSE; // ID 2.7.1.139 DE Transferred entry: 2.7.1.134. // ID 2.7.1.140 DE 1D-myo-inositol-tetrakisphosphate 5-kinase. CA ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate = ADP + 1D-myo-inositol CA 1,3,4,5,6-pentakisphosphate. // ID 2.7.1.141 DE [RNA-polymerase]-subunit kinase. AN CTD kinase. CA ATP + [DNA-directed RNA polymerase] = ADP + phospho-[DNA-directed RNA CA polymerase]. CC -!- The enzyme appears to be distinct from other protein phosphokinases. CC -!- Brings about multiple phosphorylation of the unique C-terminal CC repeat domain of the largest subunit of eukaryotic EC 2.7.7.6. PR PROSITE; PDOC00100; // ID 2.7.1.142 DE Glycerol-3-phosphate-glucose phosphotransferase. CA Sn-glycerol 3-phosphate + D-glucose = glycerol + D-glucose 6-phosphate. CC -!- Involved in the anaerobic metabolism of sugars in the bloodstream CC of trypanosomes. // ID 2.7.1.143 DE Diphosphate-purine nucleoside kinase. AN Pyrophosphate-purine nucleoside kinase. AN Pyrophosphate-dependent nucleoside kinase. AN Diphosphate-dependent nucleoside kinase. CA Diphosphate + a purine nucleoside = phosphate + a purine mononucleotide. CC -!- The enzyme from the Acholeplasma class of Mollicutes catalyzes the CC conversion of adenosine, guanosine and inosine to AMP, GMP and IMP. CC -!- ATP cannot substitute for diphosphate as a substrate. // ID 2.7.1.144 DE Tagatose-6-phosphate kinase. AN Phosphotagatokinase. CA ATP + D-tagatose 6-phosphate = ADP + D-tagatose 1,6-bisphosphate. PR PROSITE; PDOC00504; DR P42903, AGAZ_ECOLI; P37191, GATZ_ECOLI; P23391, LACC_LACLA; DR P11099, LACC_STAAW; P26421, LACC_STRMU; // ID 2.7.1.145 DE Deoxynucleoside kinase. AN Multispecific deoxynucleoside kinase. AN ms-dNK. AN Multisubstrate deoxyribonucleoside kinase. AN Multifunctional deoxynucleoside kinase. CA ATP + 2'-deoxynucleoside = ADP + 2'-deoxynucleoside 5'-phosphate. CC -!- The enzyme from embryonic cells of Drosophila melanogaster differs CC from other deoxynucleoside kinases (EC 2.7.1.76 and EC 2.7.1.113) CC in its broad specificity for all four common deoxynucleosides. DR Q9XZT6, DNK_DROME ; // ID 2.7.1.146 DE ADP-specific phosphofructokinase. AN ADP-6-phosphofructokinase. AN ADP-dependent phosphofructokinase. AN ADP-Pfk. CA ADP + D-fructose 6-phosphate = AMP + D-fructose 1,6-bisphosphate. CF Magnesium or Cobalt. CC -!- ADP can be replaced by GDP, ATP and GTP, to a limited extent. DR P58847, K6PF_METAC; Q58999, K6PF_METJA; Q9V1A6, K6PF_PYRAB; DR Q9V2Z7, K6PF_PYRFU; O59355, K6PF_PYRHO; Q977Q3, K6PF_THELI; DR Q9HH12, K6PF_THEZI; // ID 2.7.1.147 DE ADP-specific glucokinase. AN ADP-dependent glucokinase. CA ADP + D-glucose = AMP + D-glucose 6-phosphate. CF Magnesium. CC -!- The enzyme from Pyrococcus furiosus is highly specific for CC D-glucose; there is some activity with 2-deoxy-D-glucose, but no CC activity with D-fructose, D-mannose or D-galactose as the CC substrate. CC -!- No activity is detected when ADP is replaced by ATP, GDP, CC phosphoenolpyruvate, diphosphate or polyphosphate. // ID 2.7.1.148 DE 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol kinase. AN 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase. AN CDP-ME kinase. AN CMK. CA ATP + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = CA ADP + 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. CF Magnesium or Manganese. CC -!- Forms part of an alternative nonmevalonate pathway for terpenoid CC biosynthesis. DR Q8UHP8, ISPE_AGRT5; Q8YS61, ISPE_ANASP; O67060, ISPE_AQUAE; DR O81014, ISPE_ARATH; Q9KGK0, ISPE_BACHD; P37550, ISPE_BACSU; DR Q8G6I4, ISPE_BIFLO; Q8YFI3, ISPE_BRUME; Q8G2D0, ISPE_BRUSU; DR P57267, ISPE_BUCAI; Q8K9X1, ISPE_BUCAP; Q9PNJ0, ISPE_CAMJE; DR Q9A8L7, ISPE_CAUCR; Q9PLC0, ISPE_CHLMU; Q8KCC7, ISPE_CHLTE; DR O84810, ISPE_CHLTR; Q97F51, ISPE_CLOAB; Q8XIA9, ISPE_CLOPE; DR Q8FQZ4, ISPE_COREF; Q8NRY0, ISPE_CORGL; Q9RR89, ISPE_DEIRA; DR Q8FI04, ISPE_ECOL6; P24209, ISPE_ECOLI; Q8R6C8, ISPE_FUSNN; DR P45271, ISPE_HAEIN; Q9ZJH3, ISPE_HELPJ; O25984, ISPE_HELPY; DR Q8EZM8, ISPE_LEPIN; Q92F77, ISPE_LISIN; Q8YAE1, ISPE_LISMO; DR P93841, ISPE_LYCES; P56848, ISPE_MENPI; Q9CD51, ISPE_MYCLE; DR O05596, ISPE_MYCTU; Q9JUX8, ISPE_NEIMA; Q9JZW4, ISPE_NEIMB; DR Q8EU37, ISPE_OCEIH; P57833, ISPE_PASMU; P42805, ISPE_PSEAE; DR Q8Y2E0, ISPE_RALSO; Q986C6, ISPE_RHILO; Q92RM1, ISPE_RHIME; DR Q8Z699, ISPE_SALTI; P30753, ISPE_SALTY; Q8EAR0, ISPE_SHEON; DR Q99WA8, ISPE_STAAM; Q8CQU6, ISPE_STAEP; Q8E7K5, ISPE_STRA3; DR Q8E245, ISPE_STRA5; Q9K3R6, ISPE_STRCO; Q8DS40, ISPE_STRMU; DR Q8DLJ1, ISPE_SYNEL; P72663, ISPE_SYNY3; Q9X1A3, ISPE_THEMA; DR Q8R765, ISPE_THETN; O83386, ISPE_TREPA; Q9KQ23, ISPE_VIBCH; DR Q87RN7, ISPE_VIBPA; Q8DFF6, ISPE_VIBVU; Q8D2K6, ISPE_WIGBR; DR Q8PNU1, ISPE_XANAC; Q8PC64, ISPE_XANCP; Q9PA75, ISPE_XYLFA; DR Q87A21, ISPE_XYLFT; Q8ZEY1, ISPE_YERPE; Q9X3W5, ISPE_ZYMMO; // ID 2.7.1.149 DE 1-phosphatidylinositol-5-phosphate 4-kinase. AN Type II PIP kinase. CA ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + CA 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate. DR P48426, PI52_HUMAN; O70172, PI52_MOUSE; P53807, PI53_HUMAN; // ID 2.7.1.150 DE 1-phosphatidylinositol-3-phosphate 5-kinase. AN Phosphatidylinositol 3-phosphate 5-kinase. AN Type III PIP kinase. CA ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + CA 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate. DR P34756, FAB1_YEAST; // ID 2.7.1.151 DE Inositol-polyphosphate multikinase. CA ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol CA 1,4,5,6-tetrakisphosphate. CA ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol CA 1,3,4,5,6-pentakisphosphate. CC -!- This enzyme also phosphorylates Ins(1,4,5)P(3) to Ins(1,3,4,5)P(4), CC Ins(1,3,4,5)P(4) to Ins(1,3,4,5,6)P(5), and Ins(1,3,4,5,6)P(4) to CC Ins(PP)P(4), isomer unknown. // ID 2.7.1.152 DE Inositol-hexakisphosphate kinase. CA ATP + myo-inositol hexakisphosphate = ADP + diphospho-myo-inositol CA pentakisphosphate (isomeric configuration unknown). CC -!- This enzyme also phosphorylates Ins(1,3,4,5,6)P(5) to Ins(PP)P(4), CC isomer unknown. // ID 2.7.1.153 DE Phosphatidylinositol-4,5-bisphosphate 3-kinase. AN Type I phosphoinositide 3-kinase. CA ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + CA 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate. CC -!- This enzyme also catalyzes the phosphorylation of PtdIns4P to CC PtdIns(3,4)P(2), and of PtdIns to PtdIns3P. DR O02696, P101_PIG ; P32871, P11A_BOVIN; P42336, P11A_HUMAN; DR P42337, P11A_MOUSE; P42338, P11B_HUMAN; Q9Z1L0, P11B_RAT ; DR O00329, P11D_HUMAN; O35904, P11D_MOUSE; P48736, P11G_HUMAN; DR Q9JHG7, P11G_MOUSE; O02697, P11G_PIG ; // ID 2.7.1.154 DE Phosphatidylinositol-4-phosphate 3-kinase. AN Type II phosphoinositide 3-kinase. AN C2-domain-containing phosphoinositide 3-kinase. AN Phosphoinositide 3-kinase. CA ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1- CA phosphatidyl-1D-myo-inositol 3,4-bisphosphate. CC -!- This enzyme also phosphorylates PtdIns to PtdIns3P. DR O00750, PK3B_HUMAN; O75747, PK3G_HUMAN; O70167, PK3G_MOUSE; DR O70173, PK3G_RAT ; // ID 2.7.2.1 DE Acetate kinase. AN Acetokinase. CA ATP + acetate = ADP + acetyl phosphate. CC -!- Propanoate also acts as acceptor, but more slowly. PR PROSITE; PDOC00826; DR Q8XNW5, ACK1_CLOPE; Q9CE35, ACK1_LACLA; Q92BD4, ACK1_LISIN; DR Q8Y6V0, ACK1_LISMO; P58382, ACK1_RHIME; Q9KT07, ACK1_VIBCH; DR Q87MZ4, ACK1_VIBPA; Q8DAH8, ACK1_VIBVU; Q8XJN2, ACK2_CLOPE; DR Q9CE36, ACK2_LACLA; Q92CN9, ACK2_LISIN; Q8Y7V1, ACK2_LISMO; DR Q9X449, ACK2_RHIME; Q9KMT5, ACK2_VIBCH; Q87IJ5, ACK2_VIBPA; DR Q8D7K4, ACK2_VIBVU; Q8YU00, ACKA_ANASP; Q9K815, ACKA_BACHD; DR P37877, ACKA_BACSU; O51567, ACKA_BORBU; P57272, ACKA_BUCAI; DR Q8K9W6, ACKA_BUCAP; Q89AS8, ACKA_BUCBP; Q9PPL8, ACKA_CAMJE; DR O05278, ACKA_CHAYP; P71104, ACKA_CLOAB; O52594, ACKA_CLOTM; DR Q59331, ACKA_CLOTS; Q8FMB7, ACKA_COREF; P77845, ACKA_CORGL; DR P15046, ACKA_ECOLI; Q8RED7, ACKA_FUSNN; P44406, ACKA_HAEIN; DR Q9ZKU5, ACKA_HELPJ; Q9X4M1, ACKA_LACSK; Q9F1X7, ACKA_LACSN; DR Q8TK19, ACKA_METAC; Q8PZJ7, ACKA_METMA; P38502, ACKA_METTE; DR Q49113, ACKA_MYCCA; P47599, ACKA_MYCGE; P75245, ACKA_MYCPN; DR P96255, ACKA_MYCTU; P57866, ACKA_PASMU; Q9ZE38, ACKA_RICPR; DR Q8XF99, ACKA_SALTY; Q931P6, ACKA_STAAM; Q99TF2, ACKA_STAAN; DR Q8NW53, ACKA_STAAW; Q9L298, ACKA_STRCO; Q8P2X6, ACKA_STRP8; DR Q97NI3, ACKA_STRPN; Q9A1T1, ACKA_STRPY; P73162, ACKA_SYNY3; DR Q9WYB1, ACKA_THEMA; Q8R9V4, ACKA_THETN; O83489, ACKA_TREPA; DR Q8D320, ACKA_WIGBR; Q8ZDJ6, ACKA_YERPE; // ID 2.7.2.2 DE Carbamate kinase. CA ATP + NH(3) + CO(2) = ADP + carbamoyl phosphate. DR P35836, ARC1_ENTFA; P59625, ARC2_ENTFA; O86134, ARCC_BACLI; DR Q46171, ARCC_CLOPE; Q8XCV5, ARCC_ECO57; Q8FK51, ARCC_ECOL6; DR P37306, ARCC_ECOLI; P44769, ARCC_HAEIN; Q48295, ARCC_HALN1; DR Q8G997, ARCC_LACHI; O53090, ARCC_LACSK; Q8VW54, ARCC_OENOE; DR P13982, ARCC_PSEAE; O31019, ARCC_RHIET; Q92ZT0, ARCC_RHIME; DR P74733, ARCC_SYNY3; Q9HII9, ARCC_THEAC; Q97C45, ARCC_THEVO; DR O97438, CBK_GIALA ; O96432, CBK_TRIVA ; Q9UWF8, CPKA_PYRAB; DR P95474, CPKA_PYRFU; O59023, CPKA_PYRHO; // ID 2.7.2.3 DE Phosphoglycerate kinase. CA ATP + 3-phospho-D-glycerate = ADP + 3-phospho-D-glyceroyl phosphate. DI Hemolytic anemia due to phosphoglycerate kinase deficiency; MIM:311800. PR PROSITE; PDOC00102; DR P00558, PGK1_HUMAN; P29408, PGK1_MACEU; P09411, PGK1_MOUSE; DR P29405, PGK1_RHINI; P41760, PGK1_TRYCO; P07205, PGK2_HUMAN; DR P09041, PGK2_MOUSE; P16617, PGK2_RAT ; P29406, PGK2_RHINI; DR P25055, PGKA_CRIFA; P08891, PGKA_TRYBB; P08966, PGKB_CRIFA; DR Q27683, PGKB_LEIMA; Q27684, PGKB_LEIME; P07377, PGKB_TRYBB; DR P50319, PGKC_ALCEU; P08967, PGKC_CRIFA; P50312, PGKC_LEIMA; DR Q27685, PGKC_LEIME; P07378, PGKC_TRYBB; P08892, PGKD_TRYBB; DR P08893, PGKE_TRYBB; P41762, PGKG_TRYCO; P50318, PGKH_ARATH; DR P36232, PGKH_CHLFU; P41758, PGKH_CHLRE; P80659, PGKH_PHYPA; DR P29409, PGKH_SPIOL; Q42961, PGKH_TOBAC; Q9SBN4, PGKH_VOLCA; DR P12782, PGKH_WHEAT; P50320, PGKP_ALCEU; P36204, PGKT_THEMA; DR Q42962, PGKY_TOBAC; P12783, PGKY_WHEAT; Q9YFS7, PGK_AERPE ; DR O94123, PGK_AGABI ; Q8U9I9, PGK_AGRT5 ; Q8YPR1, PGK_ANASP ; DR O61471, PGK_APLCA ; O66519, PGK_AQUAE ; O29119, PGK_ARCFU ; DR P41756, PGK_ASPOR ; P83075, PGK_BACCE ; Q9K714, PGK_BACHD ; DR P24269, PGK_BACME ; P18912, PGK_BACST ; P40924, PGK_BACSU ; DR Q59181, PGK_BORBU ; Q8YIY0, PGK_BRUME ; Q8FYX8, PGK_BRUSU ; DR P57525, PGK_BUCAI ; Q8K9B3, PGK_BUCAP ; P59461, PGK_BUCBP ; DR P91427, PGK_CAEEL ; Q9PMQ5, PGK_CAMJE ; P46273, PGK_CANAL ; DR P41757, PGK_CANMA ; Q9A3F5, PGK_CAUCR ; P51903, PGK_CHICK ; DR Q9PLN4, PGK_CHLMU ; Q9Z7M5, PGK_CHLPN ; Q8KAE1, PGK_CHLTE ; DR P94686, PGK_CHLTR ; O52632, PGK_CLOAB ; P81346, PGK_CLOPA ; DR Q8XKU0, PGK_CLOPE ; O00940, PGK_CONMG ; Q8FT66, PGK_COREF ; DR Q01655, PGK_CORGL ; P50310, PGK_CRIGR ; Q9RUP2, PGK_DEIRA ; DR Q01604, PGK_DROME ; Q8XD03, PGK_ECO57 ; P11665, PGK_ECOLI ; DR P11977, PGK_EMENI ; O02608, PGK_EUPCR ; Q8RFN7, PGK_FUSNN ; DR O00852, PGK_GLACH ; O74233, PGK_GLOMO ; P43726, PGK_HAEIN ; DR Q9HQD1, PGK_HALN1 ; P50315, PGK_HALVA ; Q9ZJP1, PGK_HELPJ ; DR P56154, PGK_HELPY ; P00559, PGK_HORSE ; P14828, PGK_KLULA ; DR O32756, PGK_LACDE ; Q9CIW1, PGK_LACLA ; Q8F5H8, PGK_LEPIN ; DR Q928I0, PGK_LISIN ; Q8Y4I2, PGK_LISMO ; Q8TK32, PGK_METAC ; DR P20972, PGK_METBR ; P20971, PGK_METFE ; Q58058, PGK_METJA ; DR Q8TUU1, PGK_METKA ; Q8PZK7, PGK_METMA ; O27121, PGK_METTH ; DR O32848, PGK_MYCAV ; P47542, PGK_MYCGE ; P46712, PGK_MYCLE ; DR P78018, PGK_MYCPN ; O06821, PGK_MYCTU ; Q9JWS8, PGK_NEIMA ; DR Q9K1R0, PGK_NEIMB ; P38667, PGK_NEUCR ; Q8ENP3, PGK_OCEIH ; DR P50311, PGK_OPISI ; O02609, PGK_OXYNO ; O00869, PGK_PARPR ; DR P57973, PGK_PASMU ; P09188, PGK_PENCH ; P33161, PGK_PENCI ; DR Q8GF87, PGK_PHOLU ; P27362, PGK_PLAFA ; Q9I5Y4, PGK_PSEAE ; DR Q9UZW0, PGK_PYRAB ; Q8ZWK6, PGK_PYRAE ; P50316, PGK_PYRFU ; DR O58965, PGK_PYRHO ; Q8Y1W6, PGK_RALSO ; Q98FJ1, PGK_RHILO ; DR Q92M79, PGK_RHIME ; Q8XG18, PGK_SALTY ; P41759, PGK_SCHMA ; DR O60101, PGK_SCHPO ; Q8EIB1, PGK_SHEON ; Q9Z5C4, PGK_STAAM ; DR Q8CTD6, PGK_STAEP ; Q8E3F0, PGK_STRA3 ; Q8DXT0, PGK_STRA5 ; DR Q9Z519, PGK_STRCO ; Q8DVV2, PGK_STRMU ; Q8K5W7, PGK_STRP3 ; DR Q8NZG3, PGK_STRP8 ; Q97S89, PGK_STRPN ; P82487, PGK_STRPY ; DR Q8DQX8, PGK_STRR6 ; P50317, PGK_SULSO ; Q971K1, PGK_SULTO ; DR Q8DGP7, PGK_SYNEL ; P74421, PGK_SYNY3 ; O00871, PGK_TETPY ; DR P50313, PGK_TETTH ; Q9HJ95, PGK_THEAC ; P09403, PGK_THETH ; DR Q8R965, PGK_THETN ; Q97BC6, PGK_THEVO ; O83549, PGK_TREPA ; DR P14228, PGK_TRIRE ; P24590, PGK_TRIVI ; P96154, PGK_VIBCH ; DR Q87LL1, PGK_VIBPA ; Q8DCA0, PGK_VIBVU ; Q8D2P9, PGK_WIGBR ; DR Q8PHB2, PGK_XANAC ; Q8P5Z4, PGK_XANCP ; P50314, PGK_XANFL ; DR Q9PF55, PGK_XYLFA ; Q87AH8, PGK_XYLFT ; P29407, PGK_YARLI ; DR P00560, PGK_YEAST ; Q8ZHH3, PGK_YERPE ; P09404, PGK_ZYMMO ; // ID 2.7.2.4 DE Aspartate kinase. AN Aspartokinase. CA ATP + L-aspartate = ADP + 4-phospho-L-aspartate. CC -!- The enzyme from E.coli is a multifunctional protein, which also CC catalyzes the reaction of EC 1.1.1.3. PR PROSITE; PDOC00289; DR P00561, AK1H_ECOLI; P27725, AK1H_SERMA; Q04795, AK1_BACSU ; DR P00562, AK2H_ECOLI; Q59229, AK2_BACSP ; P53553, AK2_BACST ; DR P08495, AK2_BACSU ; P94417, AK3_BACSU ; P08660, AK3_ECOLI ; DR P49079, AKH1_MAIZE; P49080, AKH2_MAIZE; P57290, AKH_BUCAI ; DR Q8K9U9, AKH_BUCAP ; P37142, AKH_DAUCA ; P44505, AKH_HAEIN ; DR O67221, AK_AQUAE ; Q9PK32, AK_CHLMU ; Q9Z6L0, AK_CHLPN ; DR O84367, AK_CHLTR ; Q8RQN1, AK_COREF ; P41398, AK_CORFL ; DR P26512, AK_CORGL ; Q9ZJZ7, AK_HELPJ ; O25827, AK_HELPY ; DR Q57991, AK_METJA ; P47731, AK_MYCBO ; P41403, AK_MYCSM ; DR P97048, AK_MYCTU ; O69077, AK_PSEAE ; Q9ZCI7, AK_RICPR ; DR O60163, AK_SCHPO ; P97151, AK_THETH ; P10869, AK_YEAST ; // ID 2.7.2.5 DE Transferred entry: 6.3.4.16. // ID 2.7.2.6 DE Formate kinase. CA ATP + formate = ADP + formyl phosphate. // ID 2.7.2.7 DE Butyrate kinase. CA ATP + 2-butanoate = ADP + butanoyl phosphate. CC -!- The enzyme from Clostridium sp. also acts, more slowly on pentanoate CC and propanoate, and on some branched-chain fatty acids CC (cf. EC 2.7.1.14). PR PROSITE; PDOC00826; DR Q45829, BUK1_CLOAB; Q9X276, BUK1_THEMA; Q97II1, BUK2_CLOAB; DR Q9X278, BUK2_THEMA; P54621, BUK_BACST ; P54532, BUK_BACSU ; DR Q05619, BUK_CLOBE ; P81337, BUK_CLOPA ; Q9ZNE5, BUK_CLOPE ; DR Q9RVA9, BUK_DEIRA ; Q9RPS7, BUK_ENTFA ; Q92BY5, BUK_LISIN ; DR Q8Y7B6, BUK_LISMO ; Q8R832, BUK_THETN ; // ID 2.7.2.8 DE Acetylglutamate kinase. CA ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate. DR P78586, AR56_CANAL; P54898, AR56_NEUCR; P31318, AR56_SCHPO; DR Q01217, AR56_YEAST; Q8UIB7, ARGB_AGRT5; Q8YXG8, ARGB_ANASP; DR O67848, ARGB_AQUAE; O28988, ARGB_ARCFU; Q9K8V4, ARGB_BACHD; DR Q07905, ARGB_BACST; P36840, ARGB_BACSU; P59295, ARGB_BIFLO; DR Q8YDA5, ARGB_BRUME; P59296, ARGB_BRUSU; P57157, ARGB_BUCAI; DR P59098, ARGB_BUCAP; Q9PIR8, ARGB_CAMJE; Q9ABE5, ARGB_CAUCR; DR P59297, ARGB_CHLTE; Q97GH8, ARGB_CLOAB; Q59281, ARGB_CORGL; DR Q9TLT0, ARGB_CYACA; Q9RRP6, ARGB_DEIRA; P59298, ARGB_ECOL6; DR P11445, ARGB_ECOLI; Q9CHD2, ARGB_LACLA; O08320, ARGB_LACPL; DR P59299, ARGB_LEPIN; Q92BB9, ARGB_LISIN; Q8Y6U3, ARGB_LISMO; DR Q8THJ9, ARGB_METAC; Q60382, ARGB_METJA; Q8TUX2, ARGB_METKA; DR Q8PXJ8, ARGB_METMA; O26285, ARGB_METTH; Q9K4Z0, ARGB_MORS3; DR Q9K4Z5, ARGB_MORS4; Q9CC13, ARGB_MYCLE; P94989, ARGB_MYCTU; DR Q9JUK2, ARGB_NEIMA; Q9JZF7, ARGB_NEIMB; P57908, ARGB_PASMU; DR P31595, ARGB_PORPU; Q9HTN2, ARGB_PSEAE; P59300, ARGB_PSEPK; DR Q8Y3E7, ARGB_RALSO; Q98D76, ARGB_RHILO; Q92SG0, ARGB_RHIME; DR Q8ZKL7, ARGB_SALTY; P59301, ARGB_SHEON; P59302, ARGB_SHIFL; DR Q9LCS6, ARGB_STRCL; Q9L1A3, ARGB_STRCO; P59303, ARGB_SYNEL; DR P73326, ARGB_SYNY3; Q9X2A4, ARGB_THEMA; Q8R7C0, ARGB_THETN; DR Q9KNT7, ARGB_VIBCH; P59304, ARGB_VIBVU; Q8PK29, ARGB_XANAC; DR Q8P8J6, ARGB_XANCP; Q9PEM7, ARGB_XYLFA; Q87EL2, ARGB_XYLFT; DR Q8ZA87, ARGB_YERPE; // ID 2.7.2.9 DE Transferred entry: 6.3.5.5. // ID 2.7.2.10 DE Phosphoglycerate kinase (GTP). CA GTP + 3-phospho-D-glycerate = GDP + 3-phospho-D-glyceroyl phosphate. // ID 2.7.2.11 DE Glutamate 5-kinase. AN Gamma-glutamyl kinase. CA ATP + L-glutamate = ADP + L-glutamate 5-phosphate. CC -!- The product rapidly cyclizes to 5-oxoproline and phosphate. PR PROSITE; PDOC00701; DR P54887, P5C1_ARATH; P54888, P5C2_ARATH; O04015, P5CS_ACTCH; DR P54889, P5CS_CAEEL; P54886, P5CS_HUMAN; Q96480, P5CS_LYCES; DR O65361, P5CS_MESCR; Q9Z110, P5CS_MOUSE; O04226, P5CS_ORYSA; DR P32296, P5CS_VIGAC; Q98EZ4, PRB1_RHILO; Q92LB3, PRB1_RHIME; DR Q989S7, PRB2_RHILO; Q92LF7, PRB2_RHIME; Q8UBS0, PROB_AGRT5; DR Q8YSI2, PROB_ANASP; O67209, PROB_AQUAE; Q9KCR4, PROB_BACHD; DR P39820, PROB_BACSU; Q8G4T9, PROB_BIFLO; Q8YJ79, PROB_BRUME; DR Q9PJ29, PROB_CAMJE; Q9ABB6, PROB_CAUCR; Q8KCG4, PROB_CHLTE; DR Q97E63, PROB_CLOAB; Q8XHA6, PROB_CLOPE; Q8FN82, PROB_COREF; DR P46546, PROB_CORGL; Q9RTD8, PROB_DEIRA; P07005, PROB_ECOLI; DR P43763, PROB_HAEIN; Q9CF72, PROB_LACLA; P94871, PROB_LEPIN; DR Q92CE4, PROB_LISIN; Q93Q56, PROB_LISMO; Q9ZG98, PROB_MEIRU; DR Q9HHA0, PROB_METAC; Q8PYP3, PROB_METMA; Q9CBZ5, PROB_MYCLE; DR P71910, PROB_MYCTU; Q9JUK7, PROB_NEIMA; Q9JZG2, PROB_NEIMB; DR Q8CUQ5, PROB_OCEIH; Q9CJU5, PROB_PASMU; Q9HVL9, PROB_PSEAE; DR Q8XVL1, PROB_RALSO; Q8XF21, PROB_SALTY; O13810, PROB_SCHPO; DR P17856, PROB_SERMA; Q8EHU2, PROB_SHEON; Q8E784, PROB_STRA3; DR Q9RDJ9, PROB_STRCO; Q8DVN0, PROB_STRMU; Q8K6C1, PROB_STRP3; DR Q8NZX8, PROB_STRP8; Q97R95, PROB_STRPN; Q99YJ7, PROB_STRPY; DR Q8DQ61, PROB_STRR6; P96488, PROB_STRTR; Q8DH42, PROB_SYNEL; DR P73071, PROB_SYNY3; Q9WYD0, PROB_THEMA; Q60050, PROB_THETH; DR Q8RAE6, PROB_THETN; P74936, PROB_TREPA; Q9KPT8, PROB_VIBCH; DR Q8DF93, PROB_VIBVU; Q8PK34, PROB_XANAC; Q8P8K2, PROB_XANCP; DR Q9PEM4, PROB_XYLFA; Q87EL0, PROB_XYLFT; P32264, PROB_YEAST; DR Q8ZC08, PROB_YERPE; O07509, PROJ_BACSU; // ID 2.7.2.12 DE Acetate kinase (diphosphate). AN Acetate kinase (pyrophosphate). CA Diphosphate + acetate = phosphate + acetyl phosphate. // ID 2.7.2.13 DE Glutamate 1-kinase. CA ATP + L-glutamate = ADP + alpha-L-glutamyl phosphate. // ID 2.7.2.14 DE Branched-chain-fatty-acid kinase. AN Isobutyrate kinase. CA ATP + 2-methylpropanoate = ADP + 2-methylpropanoyl phosphate. CC -!- 3-methylbutanoate, 2-methylbutanoate, pentanoate, butanoate, and CC propanoate can also act as acceptors (cf. EC 2.7.2.7). // ID 2.7.3.1 DE Guanidoacetate kinase. AN Glycocyamine kinase. CA ATP + guanidoacetate = ADP + phosphoguanidoacetate. DR P51546, KGCY_NERDI; // ID 2.7.3.2 DE Creatine kinase. CA ATP + creatine = ADP + phosphocreatine. CC -!- N-ethylglycocyamine can also act as acceptor. PR PROSITE; PDOC00103; DR P05124, KCRB_CANFA; P05122, KCRB_CHICK; P12277, KCRB_HUMAN; DR Q04447, KCRB_MOUSE; Q29594, KCRB_PIG ; P00567, KCRB_RABIT; DR P07335, KCRB_RAT ; P26460, KCRB_SQUAC; P18294, KCRF_STRPU; DR Q9XSC6, KCRM_BOVIN; P05123, KCRM_CANFA; P00565, KCRM_CHICK; DR P06732, KCRM_HUMAN; P07310, KCRM_MOUSE; P00563, KCRM_RABIT; DR P00564, KCRM_RAT ; P04414, KCRM_TORCA; P00566, KCRM_TORMA; DR P11009, KCRS_CHICK; P17540, KCRS_HUMAN; O77814, KCRS_RABIT; DR P09605, KCRS_RAT ; P24722, KCRT_ONCMY; Q9TTK8, KCRU_BOVIN; DR P70079, KCRU_CHICK; P12532, KCRU_HUMAN; P30275, KCRU_MOUSE; DR Q29577, KCRU_PIG ; P25809, KCRU_RAT ; // ID 2.7.3.3 DE Arginine kinase. CA ATP + L-arginine = ADP + N-phospho-L-arginine. PR PROSITE; PDOC00103; DR Q10454, KAG1_CAEEL; Q27535, KAG2_CAEEL; O15992, KARG_ANTJA; DR O61367, KARG_APIME; Q95V58, KARG_ARTSF; Q9NH49, KARG_CALSI; DR Q9U9J4, KARG_CARMA; P48610, KARG_DROME; Q9NH48, KARG_ERISI; DR P14208, KARG_HOMGA; P51541, KARG_LIMPO; O15990, KARG_LIOJA; DR P51544, KARG_NORMA; Q9GYX1, KARG_PACMR; P51545, KARG_PENJP; DR Q95PM9, KARG_PLOIN; P91798, KARG_SCHAM; O15989, KARG_TURCO; // ID 2.7.3.4 DE Taurocyamine kinase. CA ATP + taurocyamine = ADP + N-phosphotaurocyamine. PR PROSITE; PDOC00103; DR P11917, KTRC_AREMA; // ID 2.7.3.5 DE Lombricine kinase. CA ATP + lombricine = ADP + N-phospholombricine. CC -!- Also acts on methylated lombricines such as thalassemine; the CC specificity varies with the species. PR PROSITE; PDOC00103; DR O15991, KLOM_EISFO; P11918, KLOM_LUMTE; // ID 2.7.3.6 DE Hypotaurocyamine kinase. CA ATP + hypotaurocyamine = ADP + N(omega)-phosphohypotaurocyamine. CC -!- Also acts, more slowly, on taurocyamine. // ID 2.7.3.7 DE Opheline kinase. CA ATP + guanidinoethyl methyl phosphate = ADP + N'-phosphoguanidinoethyl CA methyl phosphate. CC -!- Has a little activity on taurocyamine, lombricine and CC phosphotaurocyamine. // ID 2.7.3.8 DE Ammonia kinase. CA ATP + NH(3) = ADP + phosphoramide. CC -!- Has a wide specificity. In the reverse direction N-phosphoglycine CC and N-phosphohistidine can also act as phosphate donors, and CC ADP, dADP, GDP, CDP, dTDP, dCDP, IDP and UDP can act as phosphate CC acceptors (in decreasing order of activity). // ID 2.7.3.9 DE Phosphoenolpyruvate--protein phosphatase. AN Enzyme I of the phosphotransferase system. CA Phosphoenolpyruvate + protein L-histidine = pyruvate + protein CA N(pi)-phospho-L-histidine. CC -!- Acts only on histidine residues in specific phosphocarrier proteins CC of low molecular mass (9.5 Kd) involved in bacterial sugar transport. CC -!- A similar reaction where the protein is the enzyme EC 2.7.9.2 is CC part of the mechanism of that enzyme. PR PROSITE; PDOC00527; DR P32670, PT1A_ECOLI; P37177, PT1P_ECOLI; P37178, PT1P_SALTY; DR P23536, PT1_ALCEU ; Q9K8D3, PT1_BACHD ; O69251, PT1_BACME ; DR O83018, PT1_BACSP ; P42014, PT1_BACST ; P08838, PT1_BACSU ; DR O51508, PT1_BORBU ; Q9WXI6, PT1_BUCAI ; Q8KA50, PT1_BUCAP ; DR Q9PK57, PT1_CHLMU ; Q9Z9E3, PT1_CHLPN ; O84340, PT1_CHLTR ; DR P08839, PT1_ECOLI ; P23530, PT1_ENTFA ; P43922, PT1_HAEIN ; DR Q9CJ82, PT1_LACLA ; Q9ZAD8, PT1_LACLC ; O07126, PT1_LACSK ; DR Q92D19, PT1_LISIN ; O31149, PT1_LISMO ; P45617, PT1_MYCCA ; DR P47668, PT1_MYCGE ; P75168, PT1_MYCPN ; P12654, PT1_SALTY ; DR Q931U2, PT1_STAAM ; Q99V14, PT1_STAAN ; P51183, PT1_STAAU ; DR P23533, PT1_STACA ; Q9WXK9, PT1_STRBO ; Q9KZP1, PT1_STRCO ; DR P45595, PT1_STRMU ; P30299, PT1_STRSL ; P23388, PTF1_RHOCA; DR P45597, PTF1_XANCP; P77439, YPDD_ECOLI; // ID 2.7.3.10 DE Agmatine kinase. AN Phosphagen phosphokinase. CA ATP + agmatine = ADP + N(4)-phosphoagmatine. CC -!- L-arginine can act as acceptor, more slowly. // ID 2.7.3.11 DE Protein-histidine pros-kinase. AN Protein kinase (histidine). CA ATP + protein L-histidine = ADP + protein N(pi)-phospho-L-histidine. CC -!- A number of histones can act as acceptor. // ID 2.7.3.12 DE Protein-histidine tele-kinase. AN Protein kinase (histidine). CA ATP + protein L-histidine = ADP + protein N(tau)-phospho-L-histidine. CC -!- A number of histones can act as acceptor. // ID 2.7.4.1 DE Polyphosphate kinase. AN Polyphosphoric acid kinase. AN ATP-polyphosphate phosphotransferase. CA ATP + {phosphate}(N) = ADP + {phosphate}(N+1). DR P58991, PPK1_CHLTE; O68984, PPK2_CHLTE; Q9X4M8, PPK_ACIBA ; DR Q9KD27, PPK_BACHD ; O32350, PPK_CAMCO ; Q9PMU0, PPK_CAMJE ; DR P28688, PPK_ECOLI ; Q9ZM10, PPK_HELPJ ; O25654, PPK_HELPY ; DR Q07411, PPK_KLEAE ; O33127, PPK_MYCLE ; P95111, PPK_MYCTU ; DR Q9JW42, PPK_NEIMA ; Q9JXS9, PPK_NEIMB ; Q9S646, PPK_PSEAE ; DR Q8Z4R0, PPK_SALTI ; O86090, PPK_SALTY ; Q9KZV6, PPK_STRCO ; DR Q9EUS8, PPK_STRGR ; Q55898, PPK_SYNY3 ; Q9KU07, PPK_VIBCH ; DR Q87S51, PPK_VIBPA ; Q8DEW2, PPK_VIBVU ; Q9PAC7, PPK_XYLFA ; DR Q87A63, PPK_XYLFT ; Q8ZCX2, PPK_YERPE ; // ID 2.7.4.2 DE Phosphomevalonate kinase. CA ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate. PR PROSITE; PDOC00545; DR P24521, ERG8_YEAST; Q9VIT2, PMVK_DROME; Q15126, PMVK_HUMAN; DR Q29081, PMVK_PIG ; // ID 2.7.4.3 DE Adenylate kinase. AN Myokinase. AN Adenylic kinase. AN Adenylokinase. CA ATP + AMP = ADP + ADP. CC -!- Inorganic triphosphate can also act as donor. DI Hemolytic anemia due to deficiency of adenylate kinase; MIM:103000. PR PROSITE; PDOC00104; DR Q8YPJ8, KAD1_ANASP; P00570, KAD1_BOVIN; Q20140, KAD1_CAEEL; DR P05081, KAD1_CHICK; P00568, KAD1_HUMAN; Q9R0Y5, KAD1_MOUSE; DR P00571, KAD1_PIG ; P00569, KAD1_RABIT; P39069, KAD1_RAT ; DR P33075, KAD1_SCHPO; P73302, KAD1_SYNY3; P07170, KAD1_YEAST; DR Q8Z0M3, KAD2_ANASP; P08166, KAD2_BOVIN; P54819, KAD2_HUMAN; DR Q9WTP6, KAD2_MOUSE; P29410, KAD2_RAT ; P72641, KAD2_SYNY3; DR P26364, KAD2_YEAST; P27144, KAD4_HUMAN; Q9WUR9, KAD4_MOUSE; DR Q9WUS0, KAD4_RAT ; Q9Y6K8, KAD5_HUMAN; Q920P5, KAD5_MOUSE; DR Q9YDD2, KADA_AERPE; O82514, KADA_ARATH; P43408, KADA_METIG; DR P43409, KADA_METJA; Q8TZB0, KADA_METKA; O26135, KADA_METTH; DR P43410, KADA_METTL; P43411, KADA_METVO; Q08479, KADA_ORYSA; DR Q9V1V9, KADA_PYRAB; Q8ZWP7, KADA_PYRAE; Q8U020, KADA_PYRFU; DR O59443, KADA_PYRHO; P35028, KADA_SULAC; Q9UX83, KADA_SULSO; DR Q975K4, KADA_SULTO; Q9HIT1, KADA_THEAC; Q97BV2, KADA_THEVO; DR Q9FK35, KADB_ARATH; Q08480, KADB_ORYSA; Q9ZUU1, KADC_ARATH; DR P43188, KADC_MAIZE; Q8HSW1, KADC_SOLTU; Q9FIJ7, KADD_ARATH; DR P49983, KADH_TRIVA; P34346, KADX_CAEEL; Q09629, KADY_CAEEL; DR Q8UE38, KAD_AGRT5 ; O66490, KAD_AQUAE ; O29581, KAD_ARCFU ; DR P38372, KAD_BACHD ; P35140, KAD_BACLI ; P27142, KAD_BACST ; DR P16304, KAD_BACSU ; Q8G3Z8, KAD_BIFLO ; O51378, KAD_BORBU ; DR P39068, KAD_BORPE ; Q8YHL9, KAD_BRUME ; Q8G092, KAD_BRUSU ; DR P57556, KAD_BUCAI ; Q8K980, KAD_BUCAP ; P59429, KAD_BUCBP ; DR Q9PHM8, KAD_CAMJE ; Q9A8T2, KAD_CAUCR ; Q9PKR0, KAD_CHLMU ; DR Q9Z8U0, KAD_CHLPN ; Q8KD69, KAD_CHLTE ; O84130, KAD_CHLTR ; DR Q97EJ9, KAD_CLOAB ; Q8XHU4, KAD_CLOPE ; Q8FS39, KAD_COREF ; DR P49973, KAD_CORGL ; P12115, KAD_CYPCA ; Q9RSK7, KAD_DEIRA ; DR Q8FK84, KAD_ECOL6 ; P05082, KAD_ECOLI ; O96907, KAD_ENTHI ; DR Q8RE31, KAD_FUSNN ; P49982, KAD_GIALA ; P24323, KAD_HAEIN ; DR Q9HPA7, KAD_HALN1 ; Q9ZLL8, KAD_HELPJ ; P56104, KAD_HELPY ; DR P58117, KAD_LACLA ; P27143, KAD_LACLC ; Q9XD15, KAD_LEPIN ; DR Q927M8, KAD_LISIN ; Q8Y449, KAD_LISMO ; Q8TRS3, KAD_METAC ; DR Q8PV26, KAD_METMA ; P33107, KAD_MICLU ; P10251, KAD_MYCCA ; DR O52352, KAD_MYCGA ; P47417, KAD_MYCGE ; O33007, KAD_MYCLE ; DR Q8EUD3, KAD_MYCPE ; Q50299, KAD_MYCPN ; Q98Q02, KAD_MYCPU ; DR O53796, KAD_MYCTU ; Q59591, KAD_NEIAN ; Q59594, KAD_NEICI ; DR Q59596, KAD_NEIFL ; P49979, KAD_NEIGO ; Q59615, KAD_NEILA ; DR P49980, KAD_NEIMA ; P49981, KAD_NEIMU ; Q59628, KAD_NEIPH ; DR Q59627, KAD_NEIPO ; Q9HE76, KAD_NEUCR ; Q8ETW3, KAD_OCEIH ; DR P10772, KAD_PARDE ; P57837, KAD_PASMU ; O24464, KAD_PRUAR ; DR Q9HXV4, KAD_PSEAE ; Q9Z409, KAD_PSEPK ; Q9UZN1, KAD_PYRAB ; DR Q8U207, KAD_PYRFU ; O58844, KAD_PYRHO ; Q8XWE1, KAD_RALSO ; DR Q98N36, KAD_RHILO ; Q93FE6, KAD_RHIME ; Q92GY7, KAD_RICCN ; DR Q9ZCS6, KAD_RICPR ; P37407, KAD_SALTY ; P25824, KAD_SCHMA ; DR Q8EFF5, KAD_SHEON ; Q99S40, KAD_STAAM ; P35141, KAD_STACA ; DR Q8CRI0, KAD_STAEP ; Q8E7S0, KAD_STRA3 ; P43414, KAD_STRCO ; DR P53398, KAD_STRGR ; P49974, KAD_STRLI ; Q8DS33, KAD_STRMU ; DR Q8K8X1, KAD_STRP3 ; Q8P2Z4, KAD_STRP8 ; Q97SU1, KAD_STRPN ; DR P82549, KAD_STRPY ; Q8DRD4, KAD_STRR6 ; P43417, KAD_STRSC ; DR Q8DML4, KAD_SYNEL ; O24706, KAD_SYNP6 ; Q9X1I8, KAD_THEMA ; DR Q8R7X4, KAD_THETN ; O83604, KAD_TREPA ; Q9PQP0, KAD_UREPA ; DR Q9KTB7, KAD_VIBCH ; Q87RH4, KAD_VIBPA ; Q8DFM1, KAD_VIBVU ; DR Q8D227, KAD_WIGBR ; Q8PH23, KAD_XANAC ; Q8P5P5, KAD_XANCP ; DR Q9PGM3, KAD_XYLFA ; Q87ES6, KAD_XYLFT ; P43412, KAD_YEREN ; DR O69172, KAD_YERPE ; // ID 2.7.4.4 DE Nucleoside-phosphate kinase. AN NMP-kinase. CA ATP + nucleoside phosphate = ADP + nucleoside diphosphate. CC -!- Many nucleotides can act as acceptors. CC -!- Other nucleoside triphosphates can act instead of ATP. // ID 2.7.4.5 DE Transferred entry: 2.7.4.14. // ID 2.7.4.6 DE Nucleoside-diphosphate kinase. AN Nucleoside 5'-diphosphate phosphotransferase. AN Nucleoside diphosphokinase. AN NDK. CA ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. CC -!- Many nucleoside diphosphates can act as acceptors. CC -!- Many ribo- and deoxyribonucleoside triphosphates can act as donors. PR PROSITE; PDOC00409; DR P39207, NDK1_ARATH; O81372, NDK1_MESCR; Q07661, NDK1_ORYSA; DR P47922, NDK1_PEA ; P93554, NDK1_SACOF; Q39839, NDK1_SOYBN; DR Q02254, NDK1_SPIOL; P70010, NDK1_XENLA; O64903, NDK2_ARATH; DR P47923, NDK2_PEA ; Q01402, NDK2_SPIOL; P70011, NDK2_XENLA; DR O49203, NDK3_ARATH; Q13232, NDK3_HUMAN; Q9WV85, NDK3_MOUSE; DR P81766, NDK3_SPIOL; O75414, NDK6_HUMAN; O88425, NDK6_MOUSE; DR O88426, NDK6_RAT ; Q9Y5B8, NDK7_HUMAN; Q9QXL8, NDK7_MOUSE; DR Q9QXL7, NDK7_RAT ; O60361, NDK8_HUMAN; P52174, NDKA_BOVIN; DR P08879, NDKA_DROME; P47919, NDKA_FLABI; P15531, NDKA_HUMAN; DR P15532, NDKA_MOUSE; Q05982, NDKA_RAT ; P52175, NDKB_BOVIN; DR P47920, NDKB_FLABI; P22392, NDKB_HUMAN; Q01768, NDKB_MOUSE; DR P19804, NDKB_RAT ; P22887, NDKC_DICDI; P87355, NDKM_COLLI; DR P34093, NDKM_DICDI; O00746, NDKM_HUMAN; Q9WV84, NDKM_MOUSE; DR Q9Y9B0, NDK_AERPE ; Q8UGB6, NDK_AGRT5 ; Q8YRP2, NDK_ANASP ; DR O67528, NDK_AQUAE ; O29491, NDK_ARCFU ; Q9KCB9, NDK_BACHD ; DR P31103, NDK_BACSU ; O51419, NDK_BORBU ; P48817, NDK_BRUMA ; DR Q8YGA4, NDK_BRUME ; Q9PIG7, NDK_CAMJE ; Q9UR66, NDK_CANAL ; DR Q9M7P6, NDK_CAPAN ; Q9A7M2, NDK_CAUCR ; Q9PJP1, NDK_CHLMU ; DR Q9Z7T5, NDK_CHLPN ; Q8KAZ6, NDK_CHLTE ; O84508, NDK_CHLTR ; DR Q8XIZ1, NDK_CLOPE ; Q90380, NDK_COLLI ; Q8NN43, NDK_CORGL ; DR Q9RRJ1, NDK_DEIRA ; P24233, NDK_ECOLI ; Q8TFN0, NDK_EMENI ; DR P27950, NDK_GINCI ; P43802, NDK_HAEIN ; Q9HQH5, NDK_HALN1 ; DR Q96559, NDK_HELAN ; Q9ZMN4, NDK_HELPJ ; P56075, NDK_HELPY ; DR Q92A79, NDK_LISIN ; Q8Y5X4, NDK_LISMO ; P47921, NDK_LYCES ; DR Q8TQL6, NDK_METAC ; Q58661, NDK_METJA ; Q8TV10, NDK_METKA ; DR Q8PU77, NDK_METMA ; O26358, NDK_METTH ; Q9CBZ0, NDK_MYCLE ; DR O85501, NDK_MYCSM ; P71904, NDK_MYCTU ; P15266, NDK_MYXXA ; DR Q9JQU6, NDK_NEIMA ; Q9UUY8, NDK_NEUCR ; Q9CM17, NDK_PASMU ; DR Q59636, NDK_PSEAE ; Q9UZ13, NDK_PYRAB ; Q8ZWY4, NDK_PYRAE ; DR Q8U2A8, NDK_PYRFU ; O58429, NDK_PYRHO ; Q8Y033, NDK_RALSO ; DR Q984N8, NDK_RHILO ; Q92QX9, NDK_RHIME ; P95653, NDK_RHOSU ; DR Q92JI4, NDK_RICCN ; Q9ZE91, NDK_RICPR ; Q8XFN4, NDK_SALTY ; DR P49740, NDK_SCHPO ; P50588, NDK_STAAM ; Q8NWN1, NDK_STAAW ; DR P50589, NDK_STRCO ; Q97NQ9, NDK_STRPN ; Q980Q7, NDK_SULSO ; DR Q976A0, NDK_SULTO ; P50590, NDK_SYNP7 ; P74494, NDK_SYNY3 ; DR Q9HJ59, NDK_THEAC ; Q8RBR5, NDK_THETN ; Q97BK5, NDK_THEVO ; DR O83974, NDK_TREPA ; Q9KTX4, NDK_VIBCH ; Q87S20, NDK_VIBPA ; DR Q8DEZ5, NDK_VIBVU ; Q8D1Y6, NDK_WIGBR ; Q8NKZ9, NDK_XANAC ; DR Q9PG44, NDK_XYLFA ; Q87B35, NDK_XYLFT ; P36010, NDK_YEAST ; DR Q8ZCT2, NDK_YERPE ; // ID 2.7.4.7 DE Phosphomethylpyrimidine kinase. AN Hydroxymethylpyrimidine phosphokinase. CA ATP + 4-amino-2-methyl-5-phosphomethylpyrimidine = ADP + 4-amino-2- CA methyl-5-diphosphomethylpyrimidine. DR O67772, THID_AQUAE; P39610, THID_BACSU; P76422, THID_ECOLI; DR P44697, THID_HAEIN; Q9ZL00, THID_HELPJ; O25515, THID_HELPY; DR Q9ZBL1, THID_MYCLE; P96268, THID_MYCTU; P56904, THID_RHIME; DR P55882, THID_SALTY; Q9ZBR6, THID_STRCO; O85786, THID_SYNP7; DR O83153, THID_TREPA; // ID 2.7.4.8 DE Guanylate kinase. AN Deoxyguanylate kinase. AN GMP kinase. AN Guanosine monophosphate kinase. CA ATP + GMP = ADP + GDP. CC -!- dGMP can also act as acceptor. CC -!- dATP can act as donor. PR PROSITE; PDOC00670; DR Q8UGD7, KGUA_AGRT5; Q8Z0I7, KGUA_ANASP; Q9K9Y2, KGUA_BACHD; DR O34328, KGUA_BACSU; P46195, KGUA_BOVIN; Q89MV4, KGUA_BRAJA; DR Q8YFQ1, KGUA_BRUME; P57509, KGUA_BUCAI; Q8K9C7, KGUA_BUCAP; DR Q89AC8, KGUA_BUCBP; Q9PNB8, KGUA_CAMJE; Q9A7N9, KGUA_CAUCR; DR Q9PL09, KGUA_CHLMU; Q9Z961, KGUA_CHLPN; O84033, KGUA_CHLTR; DR Q97ID0, KGUA_CLOAB; Q8XJK8, KGUA_CLOPE; Q895Q5, KGUA_CLOTE; DR Q8NQ42, KGUA_CORGL; Q9RS38, KGUA_DEIRA; Q8XD88, KGUA_ECO57; DR P24234, KGUA_ECOLI; Q8RHI9, KGUA_FUSNN; P44310, KGUA_HAEIN; DR Q9ZMB7, KGUA_HELPJ; P56103, KGUA_HELPY; Q16774, KGUA_HUMAN; DR Q9CEE3, KGUA_LACLA; Q88WL7, KGUA_LACPL; Q92AI1, KGUA_LISIN; DR Q8Y672, KGUA_LISMO; Q64520, KGUA_MOUSE; Q9KX62, KGUA_MYCGA; DR P47353, KGUA_MYCGE; Q9CCQ7, KGUA_MYCLE; P75526, KGUA_MYCPN; DR Q98PN5, KGUA_MYCPU; P71659, KGUA_MYCTU; Q9JT96, KGUA_NEIMA; DR Q9JYB5, KGUA_NEIMB; Q8ER28, KGUA_OCEIH; P57888, KGUA_PASMU; DR P31006, KGUA_PIG ; Q9HTM2, KGUA_PSEAE; Q88C87, KGUA_PSEPK; DR Q88BE2, KGUA_PSESM; Q8XXF9, KGUA_RALSO; Q984S9, KGUA_RHILO; DR Q92QZ2, KGUA_RHIME; Q92GC9, KGUA_RICCN; Q9ZCH7, KGUA_RICPR; DR Q8Z2H9, KGUA_SALTI; Q9X6M5, KGUA_SALTY; Q9P6I5, KGUA_SCHPO; DR Q8EJU6, KGUA_SHEON; Q99UQ9, KGUA_STAAM; Q8NX22, KGUA_STAAW; DR Q8CSW4, KGUA_STAEP; Q8E756, KGUA_STRA3; Q9KXS0, KGUA_STRCO; DR Q8GAU4, KGUA_STRKA; Q8DVK6, KGUA_STRMU; Q8P001, KGUA_STRP3; DR Q97PA3, KGUA_STRPN; Q99YM5, KGUA_STRPY; Q8DNR5, KGUA_STRR6; DR Q8DMQ7, KGUA_SYNEL; P72648, KGUA_SYNY3; Q9X215, KGUA_THEMA; DR Q8R9S6, KGUA_THETN; Q9PQS9, KGUA_UREPA; Q9KNM4, KGUA_VIBCH; DR Q87TA9, KGUA_VIBPA; Q8DDV6, KGUA_VIBVU; Q8PH65, KGUA_XANAC; DR Q8P5T7, KGUA_XANCP; Q9PD76, KGUA_XYLFA; Q87DG5, KGUA_XYLFT; DR P15454, KGUA_YEAST; Q8ZJQ2, KGUA_YERPE; // ID 2.7.4.9 DE Thymidylate kinase. AN dTMP kinase. AN Thymidylic acid kinase. AN TMPK. CA ATP + thymidine 5'-phosphate = ADP + thymidine 5'-diphosphate. PR PROSITE; PDOC01034; DR Q9UXG7, KTH1_SULSO; Q975E6, KTH1_SULTO; P58157, KTH2_SULSO; DR Q970Q8, KTH2_SULTO; Q9YA48, KTHY_AERPE; Q8UFA0, KTHY_AGRT5; DR Q8YN62, KTHY_ANASP; O67099, KTHY_AQUAE; O30175, KTHY_ARCFU; DR P42490, KTHY_ASFB7; Q9KGL9, KTHY_BACHD; P37537, KTHY_BACSU; DR Q8YH15, KTHY_BRUME; P57434, KTHY_BUCAI; Q8K9J3, KTHY_BUCAP; DR P59500, KTHY_BUCBP; Q22018, KTHY_CAEEL; Q9PPF3, KTHY_CAMJE; DR Q9RQJ9, KTHY_CAUCR; Q9PKK5, KTHY_CHLMU; Q9Z8R5, KTHY_CHLPN; DR Q8KCU7, KTHY_CHLTE; O84191, KTHY_CHLTR; Q9RY40, KTHY_DEIRA; DR Q8X8H6, KTHY_ECO57; Q8FIN9, KTHY_ECOL6; P37345, KTHY_ECOLI; DR P44719, KTHY_HAEIN; Q9HNV4, KTHY_HALN1; Q9ZJE5, KTHY_HELPJ; DR O26009, KTHY_HELPY; P23919, KTHY_HUMAN; Q9CIG4, KTHY_LACLA; DR Q927E8, KTHY_LISIN; Q8Y3Y6, KTHY_LISMO; Q8THS9, KTHY_METAC; DR Q57741, KTHY_METJA; Q8PXV5, KTHY_METMA; O27793, KTHY_METTH; DR P97930, KTHY_MOUSE; P47252, KTHY_MYCGE; P75106, KTHY_MYCPN; DR Q98RF7, KTHY_MYCPU; Q9JVE7, KTHY_NEIMA; Q9K0D9, KTHY_NEIMB; DR Q9CKE9, KTHY_PASMU; Q9HZN8, KTHY_PSEAE; Q9V1E9, KTHY_PYRAB; DR Q8ZY35, KTHY_PYRAE; Q8U071, KTHY_PYRFU; O59366, KTHY_PYRHO; DR Q8XYH4, KTHY_RALSO; Q98MV4, KTHY_RHILO; Q92PW7, KTHY_RHIME; DR Q92GS5, KTHY_RICCN; Q9ZCN9, KTHY_RICPR; Q8XGI1, KTHY_SALTY; DR P36590, KTHY_SCHPO; Q99WC1, KTHY_STAAM; Q8NY05, KTHY_STAAW; DR Q8K8H4, KTHY_STRP3; Q8P2B1, KTHY_STRP8; Q97R91, KTHY_STRPN; DR Q9A190, KTHY_STRPY; Q55593, KTHY_SYNY3; Q9HLZ2, KTHY_THEAC; DR Q9X0I3, KTHY_THEMA; Q8RDE6, KTHY_THETN; Q97CC8, KTHY_THEVO; DR O83373, KTHY_TREPA; Q9PRC5, KTHY_UREPA; P13410, KTHY_VACCV; DR P33803, KTHY_VARV ; Q9KQI2, KTHY_VIBCH; Q87N26, KTHY_VIBPA; DR Q8D8H5, KTHY_VIBVU; Q8D3A7, KTHY_WIGBR; Q8PFG7, KTHY_XANAC; DR Q8P3Y6, KTHY_XANCP; Q9PFS7, KTHY_XYLFA; Q87B89, KTHY_XYLFT; DR P00572, KTHY_YEAST; O69169, KTHY_YERPE; // ID 2.7.4.10 DE Nucleoside-triphosphate--adenylate kinase. CA GTP + AMP = GDP + ADP. CC -!- Many nucleoside triphosphates can act as donors. PR PROSITE; PDOC00104; DR P08760, KAD3_BOVIN; Q9UIJ7, KAD3_HUMAN; Q9WTP7, KAD3_MOUSE; DR P29411, KAD3_RAT ; // ID 2.7.4.11 DE (Deoxy)adenylate kinase. CA ATP + dAMP = ADP + dADP. CC -!- AMP can also act as acceptor. // ID 2.7.4.12 DE T2-induced deoxynucleotide kinase. CA ATP + dGMP (or dTMP) = ADP + dGDP (or dTDP). CC -!- dTMP and dAMP can act as acceptors. CC -!- dATP can act as donor. // ID 2.7.4.13 DE (Deoxy)nucleoside-phosphate kinase. CA ATP + deoxynucleoside phosphate = ADP + deoxynucleoside diphosphate. CC -!- dATP can substitute for ATP. DR P04531, KDNM_BPT4 ; // ID 2.7.4.14 DE Cytidylate kinase. AN Deoxycytidylate kinase. AN Deoxycytidine kinase. AN dCMP kinase. AN Cytidine monophosphate kinase. AN CMP kinase. CA ATP + (d)CMP = ADP + (d)CDP. CC -!- UMP and dCMP can also act as acceptors. CC -!- Formerly EC 2.7.4.5. PR PROSITE; PDOC00104; DR O51154, KCY1_BORBU; P43892, KCY1_HAEIN; O51759, KCY2_BORBU; DR P43893, KCY2_HAEIN; Q9YDD5, KCY_AERPE ; Q8U8I9, KCY_AGRT5 ; DR O67907, KCY_AQUAE ; O28379, KCY_ARCFU ; O05386, KCY_BACCE ; DR Q9RC80, KCY_BACHD ; P38493, KCY_BACSU ; Q9RND6, KCY_BORBR ; DR Q8YEG2, KCY_BRUME ; P59580, KCY_BUCBP ; Q9A2H3, KCY_CAUCR ; DR Q9PJU0, KCY_CHLMU ; Q9Z7Y5, KCY_CHLPN ; O84458, KCY_CHLTR ; DR Q97I08, KCY_CLOAB ; Q8XLF7, KCY_CLOPE ; Q8NQK7, KCY_CORGL ; DR Q9RRE9, KCY_DEIRA ; P20425, KCY_DICDI ; P23863, KCY_ECOLI ; DR Q8RII8, KCY_FUSNN ; Q9HPA5, KCY_HALN1 ; P30085, KCY_HUMAN ; DR Q9CEY1, KCY_LACLA ; Q92A69, KCY_LISIN ; Q8Y5W6, KCY_LISMO ; DR Q8TRR6, KCY_METAC ; Q58071, KCY_METJA ; Q8TZB3, KCY_METKA ; DR Q8PV21, KCY_METMA ; O26138, KCY_METTH ; Q9DBP5, KCY_MOUSE ; DR P47572, KCY_MYCGE ; Q49885, KCY_MYCLE ; P75308, KCY_MYCPN ; DR Q98RC0, KCY_MYCPU ; O33211, KCY_MYCTU ; P57064, KCY_NEIMA ; DR P57065, KCY_NEIMB ; P57875, KCY_PASMU ; Q29561, KCY_PIG ; DR Q9HZ70, KCY_PSEAE ; Q9UZJ6, KCY_PYRAB ; Q8ZTJ1, KCY_PYRAE ; DR Q8U2L4, KCY_PYRFU ; O58988, KCY_PYRHO ; Q8Y0Y5, KCY_RALSO ; DR Q98CC2, KCY_RHILO ; Q92SV4, KCY_RHIME ; Q9X4E0, KCY_RHOSH ; DR Q92HM3, KCY_RICCN ; Q9ZD27, KCY_RICPR ; Q8Z803, KCY_SALTI ; DR Q8ZQC4, KCY_SALTY ; Q99U12, KCY_STAAM ; Q9EWW6, KCY_STRCO ; DR Q8K7Z9, KCY_STRP3 ; Q8P1H8, KCY_STRP8 ; Q97PK6, KCY_STRPN ; DR Q9A0F0, KCY_STRPY ; O05982, KCY_SULAC ; Q9UX81, KCY_SULSO ; DR Q975K7, KCY_SULTO ; Q55074, KCY_SYNY3 ; Q9HIT3, KCY_THEAC ; DR Q9X1F6, KCY_THEMA ; Q8RA78, KCY_THETN ; Q97BV0, KCY_THEVO ; DR O83362, KCY_TREPA ; Q9PQE9, KCY_UREPA ; Q9KQT2, KCY_VIBCH ; DR Q87N44, KCY_VIBPA ; Q8D8J1, KCY_VIBVU ; Q8PK76, KCY_XANAC ; DR Q8P8P4, KCY_XANCP ; Q9PAQ6, KCY_XYLFA ; Q87BJ6, KCY_XYLFT ; DR Q8ZGB3, KCY_YERPE ; // ID 2.7.4.15 DE Thiamine-diphosphate kinase. CA ATP + thiamine diphosphate = ADP + thiamine triphosphate. // ID 2.7.4.16 DE Thiamine-phosphate kinase. AN Thiamine-monophosphate kinase. CA ATP + thiamine phosphate = ADP + thiamine diphosphate. DR O29525, THIL_ARCFU; O05514, THIL_BACSU; P57532, THIL_BUCAI; DR Q8K9A5, THIL_BUCAP; P77785, THIL_ECOLI; Q57190, THIL_HAEIN; DR Q60337, THIL_METJA; O27447, THIL_METTH; Q9V1N8, THIL_PYRAB; DR O59497, THIL_PYRHO; P55881, THIL_SALTY; Q54757, THIL_SYNP7; // ID 2.7.4.17 DE 3-phosphoglyceroyl-phosphate-polyphosphate phosphotransferase. CA 3-phospho-D-glyceroyl phosphate + {phosphate}(N) = 3-phosphoglycerate + CA {phosphate}(N+1). // ID 2.7.4.18 DE Farnesyl-diphosphate kinase. CA ATP + farnesyl diphosphate = ADP + farnesyl triphosphate. CC -!- ADP can also act as donor. // ID 2.7.4.19 DE 5-methyldeoxycytidine-5'-phosphate kinase. CA ATP + 5-methyldeoxycytidine 5'-phosphate = ADP + 5-methyldeoxycytidine CA diphosphate. CC -!- The enzyme, from phage XP-12-infected Xanthomonas oryzae, converts CC M(5)-dCMP into M(5)-dCDP and then into M(5)-dCTP. // ID 2.7.4.20 DE Dolichyl-diphosphate--polyphosphate phosphotransferase. CA Dolichyl diphosphate + {phosphate}(N) = dolichyl phosphate + CA {phosphate}(N+1). // ID 2.7.5.1 DE Transferred entry: 5.4.2.2. // ID 2.7.5.2 DE Transferred entry: 5.4.2.3. // ID 2.7.5.3 DE Transferred entry: 5.4.2.1. // ID 2.7.5.4 DE Transferred entry: 5.4.2.4. // ID 2.7.5.5 DE Transferred entry: 5.4.2.5. // ID 2.7.5.6 DE Transferred entry: 5.4.2.7. // ID 2.7.5.7 DE Transferred entry: 5.4.2.8. // ID 2.7.6.1 DE Ribose-phosphate pyrophosphokinase. AN Ribose-phosphate diphosphokinase. AN Phosphoribosyl pyrophosphate synthetase. AN Phosphoribosyl diphosphate synthetase. CA ATP + D-ribose 5-phosphate = AMP + 5-phospho-alpha-D-ribose CA 1-diphosphate. CC -!- dATP can also act as donor. DI Gout (one form) with urate urolithiasis; MIM:311850. PR PROSITE; PDOC00105; DR Q42581, KPR1_ARATH; O29666, KPR1_ARCFU; P46585, KPR1_CANAL; DR P09329, KPR1_HUMAN; Q9CHB8, KPR1_LACLA; Q92F68, KPR1_LISIN; DR Q48793, KPR1_LISMO; Q97TB4, KPR1_STRPN; Q9A1Z7, KPR1_STRPY; DR P32895, KPR1_YEAST; Q42583, KPR2_ARATH; O28853, KPR2_ARCFU; DR P11908, KPR2_HUMAN; Q9CEI4, KPR2_LACLA; Q92EF1, KPR2_LISIN; DR Q8Y9L8, KPR2_LISMO; P09330, KPR2_RAT ; Q8K7J4, KPR2_STRP3; DR Q8P137, KPR2_STRP8; Q97QV3, KPR2_STRPN; Q99ZR0, KPR2_STRPY; DR P38620, KPR2_YEAST; O64888, KPR3_ARATH; P21108, KPR3_HUMAN; DR P38689, KPR3_YEAST; P38063, KPR4_YEAST; Q12265, KPR5_YEAST; DR Q9EWS0, KPRH_STRCO; Q9YAW0, KPRS_AERPE; Q8UDA9, KPRS_AGRT5; DR Q8YN97, KPRS_ANASP; O67556, KPRS_AQUAE; P42816, KPRS_BACCL; DR Q9KGJ5, KPRS_BACHD; P14193, KPRS_BACSU; Q8YIG1, KPRS_BRUME; DR P57266, KPRS_BUCAI; Q8K9X2, KPRS_BUCAP; P59512, KPRS_BUCBP; DR Q9PP15, KPRS_CAMJE; Q9AAV6, KPRS_CAUCR; Q8KCQ2, KPRS_CHLTE; DR Q97E93, KPRS_CLOAB; Q8XHJ4, KPRS_CLOPE; O33924, KPRS_CORAM; DR Q8NRU9, KPRS_CORGL; Q9RUD2, KPRS_DEIRA; P08330, KPRS_ECOLI; DR Q8RHM2, KPRS_FUSNN; P44328, KPRS_HAEIN; Q9HN88, KPRS_HALN1; DR Q9ZLA1, KPRS_HELPJ; P56184, KPRS_HELPY; Q8TRK8, KPRS_METAC; DR Q58761, KPRS_METJA; Q8TUT6, KPRS_METKA; Q8PUX3, KPRS_METMA; DR O26877, KPRS_METTH; P47304, KPRS_MYCGE; Q9CD45, KPRS_MYCLE; DR P75044, KPRS_MYCPN; Q98R83, KPRS_MYCPU; P96383, KPRS_MYCTU; DR Q9JQV4, KPRS_NEIMA; Q9CP22, KPRS_PASMU; Q9HVC5, KPRS_PSEAE; DR Q9UY08, KPRS_PYRAB; Q8ZU24, KPRS_PYRAE; Q8U458, KPRS_PYRFU; DR O59586, KPRS_PYRHO; O52958, KPRS_PYRKO; Q8Y2E1, KPRS_RALSO; DR Q98HW3, KPRS_RHILO; Q92N73, KPRS_RHIME; P15849, KPRS_SALTY; DR P41831, KPRS_SCHPO; Q99WA3, KPRS_STAAM; Q9K3U0, KPRS_STRCO; DR Q97Z86, KPRS_SULSO; Q973F3, KPRS_SULTO; Q59988, KPRS_SYNP7; DR Q55848, KPRS_SYNY3; Q9HLV6, KPRS_THEAC; Q9X1W3, KPRS_THEMA; DR Q8R753, KPRS_THETN; Q97CA5, KPRS_THEVO; Q9PQV0, KPRS_UREPA; DR Q9KQ22, KPRS_VIBCH; Q8PNU0, KPRS_XANAC; Q8PC63, KPRS_XANCP; DR Q9PA76, KPRS_XYLFA; Q87A22, KPRS_XYLFT; Q8ZEY2, KPRS_YERPE; // ID 2.7.6.2 DE Thiamine pyrophosphokinase. AN Thiamine diphosphokinase. AN Thiamine kinase. CA ATP + thiamine = AMP + thiamine diphosphate. DR P35202, TH80_YEAST; P41888, TNR3_SCHPO; // ID 2.7.6.3 DE 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase. AN 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase. AN 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase. AN 6-hydroxymethyl-7,8-dihydropterin diphosphokinase. AN 7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase. AN 7,8-dihydro-6-hydroxymethylpterin diphosphokinase. CA ATP + 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine = AMP + CA 2-amino-7,8-dihydro-4-hydroxy-6-(diphosphooxymethyl)pteridine. PR PROSITE; PDOC00631; DR P29251, FAS_PNECA ; P53848, FAS_YEAST ; P82602, FOKP_CHLMU; DR Q9Z7E8, FOKP_CHLPN; O84619, FOKP_CHLTR; O66550, HPPK_AQUAE; DR P29252, HPPK_BACSU; Q9PJ54, HPPK_CAMJE; P26281, HPPK_ECOLI; DR P43777, HPPK_HAEIN; Q9ZM35, HPPK_HELPJ; O25680, HPPK_HELPY; DR P71512, HPPK_METEX; O69528, HPPK_MYCLE; O06276, HPPK_MYCTU; DR O83019, HPPK_PORGI; O87790, HPPK_PSEPU; Q8K7K6, HPPK_STRP3; DR Q8P151, HPPK_STRP8; O33726, HPPK_STRPY; P72736, HPPK_SYNY3; DR P22291, SULD_STRPN; P59657, SULD_STRR6; // ID 2.7.6.4 DE Nucleotide pyrophosphokinase. AN Nucleotide diphosphokinase. CA ATP + nucleoside 5'-phosphate = AMP + 5'-phosphonucleoside CA 3'-diphosphate. CC -!- Acts on the 5'-mono-, di- and triphosphate derivatives of purine CC nucleosides. // ID 2.7.6.5 DE GTP pyrophosphokinase. AN GTP diphosphokinase. AN ppGpp synthetase I. AN Stringent factor. AN Guanosine 3',5'-polyphosphate synthase. CA ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate. CC -!- GDP can also act as acceptor. DR O54408, RELA_BACSU; O87331, RELA_CORGL; P11585, RELA_ECOLI; DR P44644, RELA_HAEIN; Q49640, RELA_MYCLE; Q50638, RELA_MYCTU; DR O52177, RELA_MYXXA; O32419, RELA_STAAW; O85709, RELA_STRAT; DR P52560, RELA_STRCO; Q54089, RELA_STREQ; P55133, RELA_VIBSS; // ID 2.7.7.1 DE Nicotinamide-nucleotide adenylyltransferase. AN NAD(+) pyrophosphorylase. AN NAD(+) diphosphorylase. AN NMN adenylyltransferase. CA ATP + nicotinamide ribonucleotide = diphosphate + NAD(+). CC -!- Nicotinate nucleotide can also act as acceptor. CC -!- See also EC 2.7.7.18. DR Q9YER8, NADM_AERPE; O27969, NADM_ARCFU; Q9HSC4, NADM_HALN1; DR Q8TJP9, NADM_METAC; Q57961, NADM_METJA; Q8PZ68, NADM_METMA; DR O26253, NADM_METTH; Q9UXN8, NADM_METTI; Q9UYD4, NADM_PYRAB; DR Q8ZX62, NADM_PYRAE; Q8U3K8, NADM_PYRFU; O58211, NADM_PYRHO; DR P57084, NADM_SULSO; Q974L1, NADM_SULTO; Q55928, NADM_SYNY3; DR Q9HK34, NADM_THEAC; Q97AF1, NADM_THEVO; Q06178, NADM_YEAST; DR Q9HAN9, NMA1_HUMAN; Q9EPA7, NMA1_MOUSE; Q9BZQ4, NMA2_HUMAN; // ID 2.7.7.2 DE FMN adenylyltransferase. AN FAD pyrophosphorylase. AN FAD diphosphorylase. AN FAD synthetase. AN Flavin adenine dinucleotide synthetase. CA ATP + FMN = diphosphate + FAD. DR O74841, FAD1_SCHPO; P38913, FAD1_YEAST; P54575, RIBC_BACSU; DR P57250, RIBF_BUCAI; Q8K9Z1, RIBF_BUCAP; Q59263, RIBF_CORAM; DR P08391, RIBF_ECOLI; P44957, RIBF_HAEIN; P47391, RIBF_MYCGE; DR P75587, RIBF_MYCPN; P22990, RIBF_PSEFL; O84990, RIBF_RHOOP; DR P73651, RIBF_SYNY3; // ID 2.7.7.3 DE Pantetheine-phosphate adenylyltransferase. AN Phosphopantetheine adenylyltransferase. AN PPAT. AN Dephospho-CoA pyrophosphorylase. AN Dephospho-CoA diphosphorylase. AN Dephospho-coenzyme A pyrophosphorylase. AN 3'-dephospho-CoA pyrophosphorylase. CA ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA. CC -!- The enzyme from several bacteria (e.g. Escherichia coli, Bacillus CC subtilis and Haemophilus influenzae) has been shown to be CC bifunctional and also to possess the activity of EC 2.3.1.157. DR Q8UES4, COAD_AGRT5; Q8YN70, COAD_ANASP; O66614, COAD_AQUAE; DR O28077, COAD_ARCFU; Q9K9Q6, COAD_BACHD; O34797, COAD_BACSU; DR Q8A3C0, COAD_BACTN; Q8RT67, COAD_BARBA; Q8G7H5, COAD_BIFLO; DR O51645, COAD_BORBU; Q89L55, COAD_BRAJA; Q8YHB6, COAD_BRUME; DR P57643, COAD_BUCAI; Q9Z613, COAD_BUCAP; Q9PPF2, COAD_CAMJE; DR P58103, COAD_CAUCR; Q8KDS9, COAD_CHLTE; P71154, COAD_CHRVI; DR Q97IB2, COAD_CLOAB; Q8XJM7, COAD_CLOPE; Q895N8, COAD_CLOTE; DR Q8FPP9, COAD_COREF; Q8NQU5, COAD_CORGL; Q9RWM4, COAD_DEIRA; DR Q8FC88, COAD_ECOL6; P23875, COAD_ECOLI; Q8RGX1, COAD_FUSNN; DR P44805, COAD_HAEIN; Q9ZJE4, COAD_HELPJ; O26010, COAD_HELPY; DR Q9XC89, COAD_KLEPN; Q9CDQ6, COAD_LACLA; Q88VC8, COAD_LACPL; DR Q8EYP6, COAD_LEPIN; Q929W5, COAD_LISIN; Q8Y5K7, COAD_LISMO; DR Q8TK70, COAD_METAC; Q58436, COAD_METJA; Q8TGY4, COAD_METKA; DR Q8PZN4, COAD_METMA; O27918, COAD_METTH; P45616, COAD_MYCCA; DR O69466, COAD_MYCLE; Q8EUG2, COAD_MYCPE; Q98RB3, COAD_MYCPU; DR Q50452, COAD_MYCTU; Q9JQY9, COAD_NEIMA; Q8ER64, COAD_OCEIH; DR Q9CLD4, COAD_PASMU; Q8VW75, COAD_PASPI; Q8RSX4, COAD_PROMI; DR Q9I6D1, COAD_PSEAE; Q88CQ7, COAD_PSEPK; Q88AH3, COAD_PSESM; DR Q9UYT0, COAD_PYRAB; Q8ZY96, COAD_PYRAE; Q8U1X0, COAD_PYRFU; DR O58358, COAD_PYRHO; Q8Y2E6, COAD_RALSO; Q98M51, COAD_RHILO; DR Q92PY8, COAD_RHIME; Q8Z2H1, COAD_SALTI; Q8ZL48, COAD_SALTY; DR Q9X980, COAD_SERMA; Q8E8I0, COAD_SHEON; Q99UX9, COAD_STAAM; DR Q8CSZ5, COAD_STAEP; Q8E6R1, COAD_STRA3; Q8E1A6, COAD_STRA5; DR Q9ZBR1, COAD_STRCO; Q8DVH2, COAD_STRMU; Q97NQ2, COAD_STRPN; DR P58104, COAD_STRPY; Q8DNE6, COAD_STRR6; Q8DJQ7, COAD_SYNEL; DR Q55235, COAD_SYNP7; Q55435, COAD_SYNY3; Q9HIY2, COAD_THEAC; DR Q9WZK0, COAD_THEMA; Q8R9U9, COAD_THETN; Q97BQ0, COAD_THEVO; DR O83307, COAD_TREPA; Q9KVC4, COAD_VIBCH; Q87T80, COAD_VIBPA; DR Q8DDY6, COAD_VIBVU; Q8D2R5, COAD_WIGBR; Q8PJK5, COAD_XANAC; DR Q8P857, COAD_XANCP; Q9PEP8, COAD_XYLFA; Q87EM8, COAD_XYLFT; DR Q8ZJN9, COAD_YERPE; Q9RME4, COAD_ZYMMO; // ID 2.7.7.4 DE Sulfate adenylyltransferase. AN Sulfate adenylate transferase. AN ATP-sulfurylase. AN Sulfurylase. CA ATP + sulfate = diphosphate + adenylylsulfate. CC -!- The human phosphoadenosine-phosphosulfate synthase (PAPS) system CC is a bifunctional enzyme: ATP sulfurylase, which catalyzes the CC formation of adenosine 5'-phosphosulfate (APS) from ATP and inorganic CC sulfate and the second step is catalyzed by the APS kinase portion of CC 3'-phosphoadenosine 5'-phosphosulfate (PAPS) synthase, which CC involves the formation of PAPS from enzyme bound APS and ATP. CC -!- This is in contrast to what is found in bacteria, yeast, fungi CC and plants, where the formation of PAPS is carried out by two CC individual polypeptides, EC 2.7.7.4 and EC 2.7.1.25. DR P57499, CYSD_BUCAI; Q8X7X4, CYSD_ECO57; Q8FEJ0, CYSD_ECOL6; DR P21156, CYSD_ECOLI; Q10599, CYSD_MYCTU; O50273, CYSD_PSEAE; DR P56892, CYSD_RHIME; O33580, CYSD_RHITR; Q8XFS4, CYSD_SALTY; DR P59740, CYSD_SHIFL; Q9KP19, CYSD_VIBCH; Q87SY0, CYSD_VIBPA; DR Q8DE72, CYSD_VIBVU; Q9PD79, CYSD_XYLFA; Q87DG8, CYSD_XYLFT; DR P57498, CYSN_BUCAI; Q8X7X7, CYSN_ECO57; Q8FEJ1, CYSN_ECOL6; DR P23845, CYSN_ECOLI; Q10600, CYSN_MYCTU; O50274, CYSN_PSEAE; DR P56893, CYSN_RHIME; O33581, CYSN_RHITR; Q8Z470, CYSN_SALTI; DR Q8ZMF5, CYSN_SALTY; Q8EB10, CYSN_SHEON; Q9KP20, CYSN_VIBCH; DR Q87SX9, CYSN_VIBPA; Q8DE73, CYSN_VIBVU; Q9PD78, CYSN_XYLFA; DR Q87DG7, CYSN_XYLFT; P56862, MET3_ASPTE; Q9Y872, MET3_CANAL; DR Q12555, MET3_EMENI; Q12650, MET3_PENCH; P78937, MET3_SCHPO; DR P08536, MET3_YEAST; Q9X5U0, MMCV_STRLA; P28603, NODP_AZOBR; DR P13441, NODP_RHIME; P72338, NODP_RHIS3; O07308, NODP_RHISB; DR P52995, NODP_RHITR; P28604, NODQ_AZOBR; P13442, NODQ_RHIME; DR P72339, NODQ_RHIS3; O07309, NODQ_RHISB; P52978, NODQ_RHITR; DR O54820, PPS1_CAVPO; O43252, PPS1_HUMAN; Q60967, PPS1_MOUSE; DR O95340, PPS2_HUMAN; O88428, PPS2_MOUSE; Q27128, PPS_URECA ; DR O34764, SAT1_BACSU; O06736, SAT2_BACSU; O67174, SATC_AQUAE; DR Q9YCR4, SAT_AERPE ; O28606, SAT_ARCFU ; O66036, SAT_CHRVI ; DR P56864, SAT_DEIRA ; O76156, SAT_ENTHI ; P56863, SAT_PYRAB ; DR Q54506, SAT_RIFPS ; P74241, SAT_SYNY3 ; // ID 2.7.7.5 DE Sulfate adenylyltransferase (ADP). AN Adenosine diphosphate sulfurylase. AN ADP-sulfurylase. CA ADP + sulfate = phosphate + adenylylsulfate. DR P16550, APA1_YEAST; // ID 2.7.7.6 DE DNA-directed RNA polymerase. AN RNA polymerase I. AN RNA polymerase II. AN RNA polymerase III. AN RNA nucleotidyltransferase (DNA-directed). CA N nucleoside triphosphate = N diphosphate + {RNA}(N). CC -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA CC strand by one nucleotide at a time. CC -!- Can initiate a chain de novo. CC -!- In eukaryotes three forms of the enzyme have been distinguished on CC the basis of sensitivity of alpha-amanitin, and the type of RNA CC synthesized. CC -!- See also EC 2.7.7.19 and EC 2.7.7.48. PR PROSITE; PDOC00410; PR PROSITE; PDOC00106; PR PROSITE; PDOC00790; PR PROSITE; PDOC00411; PR PROSITE; PDOC00854; PR PROSITE; PDOC00889; PR PROSITE; PDOC00856; PR PROSITE; PDOC00855; DR Q39211, RP3A_ARATH; Q39212, RP3B_ARATH; P91875, RPA1_DROME; DR P28363, RPA1_EUPOC; P15350, RPA1_HALHA; P15349, RPA1_HALMO; DR O95602, RPA1_HUMAN; Q58445, RPA1_METJA; O27125, RPA1_METTH; DR P09846, RPA1_METTW; P41556, RPA1_METVA; O35134, RPA1_MOUSE; DR O54889, RPA1_RAT ; P15398, RPA1_SCHPO; P11512, RPA1_SULAC; DR Q980R2, RPA1_SULSO; Q03585, RPA1_THEAC; P31813, RPA1_THECE; DR P16355, RPA1_TRYBB; P10964, RPA1_YEAST; Q9YAU2, RPA2_AERPE; DR O28390, RPA2_ARCFU; P20028, RPA2_DROME; P28365, RPA2_EUPOC; DR P15353, RPA2_HALMO; P15354, RPA2_HALN1; Q9H9Y6, RPA2_HUMAN; DR Q8TRB8, RPA2_METAC; Q58446, RPA2_METJA; Q8PUR2, RPA2_METMA; DR O27126, RPA2_METTH; P09847, RPA2_METTW; P14247, RPA2_METVA; DR P70700, RPA2_MOUSE; O74633, RPA2_NEUCR; Q9V113, RPA2_PYRAB; DR Q8ZYQ7, RPA2_PYRAE; Q8U0M5, RPA2_PYRFU; O93777, RPA2_PYRHO; DR O54888, RPA2_RAT ; Q9P7X8, RPA2_SCHPO; P11514, RPA2_SULAC; DR P58192, RPA2_SULSO; Q976A6, RPA2_SULTO; Q03586, RPA2_THEAC; DR P29158, RPA2_THECE; Q979F5, RPA2_THEVO; P22138, RPA2_YEAST; DR O14086, RPA3_SCHPO; Q01080, RPA3_YEAST; O43036, RPA4_SCHPO; DR P46669, RPA4_YEAST; O15160, RPA5_HUMAN; P52432, RPA5_MOUSE; DR P50106, RPA8_YEAST; Q9Y2S0, RPA9_HUMAN; P97304, RPA9_MOUSE; DR O94703, RPA9_SCHPO; P32529, RPA9_YEAST; P18616, RPB1_ARATH; DR O28392, RPB1_ARCFU; P35074, RPB1_CAEBR; P16356, RPB1_CAEEL; DR P11414, RPB1_CRIGR; P35084, RPB1_DICDI; P04052, RPB1_DROME; DR P28364, RPB1_EUPOC; P15351, RPB1_HALN1; P24928, RPB1_HUMAN; DR Q60181, RPB1_METJA; O27124, RPB1_METTH; P09845, RPB1_METTW; DR P41557, RPB1_METVA; P08775, RPB1_MOUSE; P14248, RPB1_PLAFD; DR P36594, RPB1_SCHPO; P17545, RPB1_TRYBB; P04050, RPB1_YEAST; DR P38420, RPB2_ARATH; Q10578, RPB2_CAEEL; P08266, RPB2_DROME; DR P15352, RPB2_HALN1; P30876, RPB2_HUMAN; Q42877, RPB2_LYCES; DR Q58444, RPB2_METJA; O27123, RPB2_METTH; P09844, RPB2_METTW; DR P41558, RPB2_METVA; Q02061, RPB2_SCHPO; P17546, RPB2_TRYBB; DR P08518, RPB2_YEAST; P19387, RPB3_HUMAN; P97760, RPB3_MOUSE; DR P37382, RPB3_SCHPO; P16370, RPB3_YEAST; O15514, RPB4_HUMAN; DR O74825, RPB4_SCHPO; P20433, RPB4_YEAST; P19388, RPB5_HUMAN; DR Q9P4B9, RPB5_KLUMA; Q09191, RPB5_SCHPO; P20434, RPB5_YEAST; DR P42484, RPB6_ASFB7; Q08399, RPB6_ASFM2; Q17684, RPB6_CAEEL; DR Q24320, RPB6_DROME; P41584, RPB6_HUMAN; O88828, RPB6_RAT ; DR P36595, RPB6_SCHPO; P20435, RPB6_YEAST; P38421, RPB7_ARATH; DR P52433, RPB7_HUMAN; O14459, RPB7_SCHPO; P46279, RPB7_SOYBN; DR P34087, RPB7_YEAST; Q19826, RPB8_CAEEL; P52434, RPB8_HUMAN; DR Q92399, RPB8_SCHPO; P20436, RPB8_YEAST; P36958, RPB9_DROME; DR P36954, RPB9_HUMAN; O74635, RPB9_SCHPO; P27999, RPB9_YEAST; DR Q9SYA6, RPBX_ARATH; P42488, RPBX_ASFB7; Q39290, RPBX_BRANA; DR Q9VC49, RPBX_DROME; P52436, RPBX_HUMAN; O13877, RPBX_SCHPO; DR P22139, RPBX_YEAST; Q38859, RPBY_ARATH; Q9XVH6, RPBY_CAEEL; DR Q9VJE4, RPBY_DROME; P52435, RPBY_HUMAN; O08740, RPBY_MOUSE; DR P87123, RPBY_SCHPO; P38902, RPBY_YEAST; P25202, RPC1_GIALA; DR O14802, RPC1_HUMAN; P27625, RPC1_PLAFA; O94666, RPC1_SCHPO; DR P08968, RPC1_TRYBB; P04051, RPC1_YEAST; P25167, RPC2_DROME; DR Q9NW08, RPC2_HUMAN; P59470, RPC2_MOUSE; Q10233, RPC2_SCHPO; DR P22276, RPC2_YEAST; P32349, RPC3_YEAST; P05423, RPC4_HUMAN; DR Q91WD1, RPC4_MOUSE; P25441, RPC4_YEAST; Q9NVU0, RPC5_HUMAN; DR Q9CZT4, RPC5_MOUSE; O94616, RPC5_SCHPO; P07703, RPC5_YEAST; DR P91529, RPC6_CAEEL; Q9VD25, RPC6_DROME; Q9H1D9, RPC6_HUMAN; DR Q921X6, RPC6_MOUSE; O94553, RPC6_SCHPO; P32910, RPC6_YEAST; DR Q9Y535, RPC8_HUMAN; Q9D2C6, RPC8_MOUSE; P17890, RPC8_YEAST; DR P34476, RPC9_CAEEL; Q09177, RPC9_SCHPO; P28000, RPC9_YEAST; DR P53803, RPCX_HUMAN; Q63871, RPCX_MOUSE; P48011, RPCX_SCHPO; DR P40422, RPCX_YEAST; P35718, RPCY_YEAST; Q9Y2Y1, RPCZ_HUMAN; DR O13896, RPCZ_SCHPO; Q04307, RPCZ_YEAST; Q57840, RPE1_METJA; DR Q57839, RPE2_METJA; P42486, RPO1_ASFB7; Q9J593, RPO1_FOWPV; DR P20504, RPO1_VACCC; P07392, RPO1_VACCV; P33053, RPO1_VARV ; DR P42487, RPO2_ASFB7; P16716, RPO2_CAPVK; P17474, RPO2_COWPX; DR Q9J544, RPO2_FOWPV; P19798, RPO2_VACCV; P33811, RPO2_VARV ; DR P19749, RPO4_CAPVK; Q9J540, RPO4_FOWPV; P21087, RPO4_VACCC; DR P24757, RPO4_VACCV; P33812, RPO4_VARV ; Q9J5C0, RPO5_FOWPV; DR P21082, RPO5_VACCC; P21603, RPO5_VACCV; P33796, RPO5_VARV ; DR Q85280, RPO6_FOWPV; P18620, RPO6_MYXVL; P07391, RPO6_VACCV; DR P33054, RPO6_VARV ; Q05569, RPO7_FOWPV; P20984, RPO7_VACCV; DR P33813, RPO7_VARV ; P21967, RPO8_FOWPV; P21034, RPO8_VACCC; DR P04310, RPO8_VACCV; P33058, RPO8_VARV ; Q9J5A4, RPO9_FOWPV; DR Q98229, RPO9_MCV1 ; Q9Q8P6, RPO9_MYXVL; Q9Q921, RPO9_SFVKA; DR Q89560, RPO9_VACCV; Q07047, RPO9_VARV ; Q9DHQ8, RPO9_YLDV ; DR P92429, RPOA_AEGTA; P92209, RPOA_AGRCR; Q9R710, RPOA_AGRT5; DR Q8YPK3, RPOA_ANASP; O66483, RPOA_AQUAE; P56762, RPOA_ARATH; DR P34778, RPOA_ASTLO; P93993, RPOA_AUSVE; O50634, RPOA_BACHD; DR P20429, RPOA_BACSU; Q9FDC7, RPOA_BARHE; O51455, RPOA_BORBU; DR P37368, RPOA_BORPE; P92220, RPOA_BROIN; Q8YHL6, RPOA_BRUME; DR P57566, RPOA_BUCAI; O69232, RPOA_BUCAP; P59455, RPOA_BUCBP; DR Q9PM80, RPOA_CAMJE; Q9A8S9, RPOA_CAUCR; Q8M9V7, RPOA_CHAGL; DR Q9PJN4, RPOA_CHLMU; Q9Z7S8, RPOA_CHLPN; Q8KAJ8, RPOA_CHLTE; DR Q46449, RPOA_CHLTR; P56298, RPOA_CHLVU; Q97EK6, RPOA_CLOAB; DR Q9LBW9, RPOA_CLOPE; Q8NSV2, RPOA_CORGL; P92225, RPOA_CRIDE; DR Q8SKY1, RPOA_CUSRE; Q9TLV2, RPOA_CYACA; P48118, RPOA_CYAPA; DR Q9RSJ6, RPOA_DEIRA; P00574, RPOA_ECOLI; P93974, RPOA_EREDI; DR Q8SL94, RPOA_EUGAN; Q8SL92, RPOA_EUGGA; P48337, RPOA_EUGGR; DR Q8SL90, RPOA_EUGMY; Q8SL88, RPOA_EUGST; Q8SL86, RPOA_EUGVI; DR P93968, RPOA_FESFE; P93956, RPOA_FESSE; Q8RE44, RPOA_FUSNN; DR O46914, RPOA_GUITH; P43737, RPOA_HAEIN; Q9ZJT5, RPOA_HELPJ; DR P56001, RPOA_HELPY; P92389, RPOA_HETPI; P92392, RPOA_HORVU; DR Q9CDY3, RPOA_LACLA; Q9XD09, RPOA_LEPIN; Q927N3, RPOA_LISMO; DR Q8MAI6, RPOA_LOPEL; Q9BBQ4, RPOA_LOTJA; P09562, RPOA_MAIZE; DR P06270, RPOA_MARPO; Q9BBN0, RPOA_MARQU; Q9MUV0, RPOA_MESVI; DR Q9RDV6, RPOA_MYCGA; P47423, RPOA_MYCGE; Q9X798, RPOA_MYCLE; DR Q50295, RPOA_MYCPN; Q98Q08, RPOA_MYCPU; P38018, RPOA_MYCSP; DR O06324, RPOA_MYCTU; Q9JR06, RPOA_NEIMA; Q9TL28, RPOA_NEPOL; DR P49465, RPOA_ODOSI; Q9MTJ3, RPOA_OENHO; P12090, RPOA_ORYSA; DR P57941, RPOA_PASMU; P13911, RPOA_PEA ; Q8MC99, RPOA_PHAAN; DR P41629, RPOA_PINTH; P51293, RPOA_PORPU; P92418, RPOA_PSAFR; DR P93960, RPOA_PSARU; P93962, RPOA_PSAST; O52760, RPOA_PSEAE; DR Q8WHZ1, RPOA_PSINU; Q01569, RPOA_PYRSA; Q8XV38, RPOA_RALSO; DR O21260, RPOA_RECAM; Q98N33, RPOA_RHILO; Q925Z2, RPOA_RHIME; DR Q92GZ0, RPOA_RICCN; Q9ZCS9, RPOA_RICPR; P19587, RPOA_SCEOB; DR P93964, RPOA_SECST; P74963, RPOA_SHESP; Q9S0Q8, RPOA_SHEVI; DR Q9XQN8, RPOA_SINAL; O98462, RPOA_SPIMX; P06505, RPOA_SPIOL; DR Q99S45, RPOA_STAAM; P72404, RPOA_STRCO; Q9X4V6, RPOA_STRGT; DR Q8K8W9, RPOA_STRP3; Q97ST7, RPOA_STRPN; Q9A1U9, RPOA_STRPY; DR O24710, RPOA_SYNP6; P73297, RPOA_SYNY3; Q9KWU8, RPOA_THEAQ; DR Q9X1I2, RPOA_THEMA; Q9Z9H6, RPOA_THETH; Q8R7Y2, RPOA_THETN; DR P92439, RPOA_THIBE; P06269, RPOA_TOBAC; O83242, RPOA_TREPA; DR Q9PQN4, RPOA_UREPA; Q9KP08, RPOA_VIBCH; Q87SZ0, RPOA_VIBPA; DR Q8DE63, RPOA_VIBVU; P12073, RPOA_WHEAT; Q8D1Y8, RPOA_WIGBR; DR Q9Z3E7, RPOA_XANCP; Q9PE52, RPOA_XYLFA; Q8ZJ87, RPOA_YERPE; DR P22703, RPOB_ANASP; O67762, RPOB_AQUAE; P50546, RPOB_ARATH; DR P27059, RPOB_ASTLO; Q9Z9M2, RPOB_BACHD; P37870, RPOB_BACSU; DR Q59191, RPOB_BORBU; P57146, RPOB_BUCAI; P41184, RPOB_BUCAP; DR Q89B20, RPOB_BUCBP; Q46124, RPOB_CAMJE; P56869, RPOB_CHLMU; DR Q9Z9A0, RPOB_CHLPN; O84317, RPOB_CHLTR; P56299, RPOB_CHLVU; DR Q97EG9, RPOB_CLOAB; Q93R88, RPOB_CLOPE; O87903, RPOB_COXBU; DR Q9TM35, RPOB_CYACA; P48119, RPOB_CYAPA; P00575, RPOB_ECOLI; DR P23579, RPOB_EUGGR; O78485, RPOB_GUITH; P43738, RPOB_HAEIN; DR P36440, RPOB_HETCA; P41187, RPOB_LIBAF; P36251, RPOB_LIBAS; DR Q92F22, RPOB_LISIN; Q9RLT9, RPOB_LISMO; Q9BBS9, RPOB_LOTJA; DR P16023, RPOB_MAIZE; P06272, RPOB_MARPO; Q9MUS5, RPOB_MESVI; DR P47715, RPOB_MYCGA; P47583, RPOB_MYCGE; P30760, RPOB_MYCLE; DR P78013, RPOB_MYCPN; Q9RQZ7, RPOB_MYCPR; P47766, RPOB_MYCTU; DR P57009, RPOB_NEIMA; Q59622, RPOB_NEIMB; Q9TL06, RPOB_NEPOL; DR P41452, RPOB_NPVAC; O12934, RPOB_NPVOP; P49466, RPOB_ODOSI; DR Q9MTM5, RPOB_OENHO; P12091, RPOB_ORYSA; P41607, RPOB_PINTH; DR P21421, RPOB_PLAFA; P51252, RPOB_PORPU; Q51561, RPOB_PSEAE; DR P19175, RPOB_PSEPU; Q9RH41, RPOB_RICCN; Q9RH43, RPOB_RICMA; DR O52271, RPOB_RICPR; P77941, RPOB_RICTY; P06173, RPOB_SALTY; DR P08036, RPOB_SAPOF; P46818, RPOB_SINAL; P47767, RPOB_SPICI; DR P11703, RPOB_SPIOL; P47768, RPOB_STAAU; P11513, RPOB_SULAC; DR P77965, RPOB_SYNY3; Q03587, RPOB_THEAC; Q9KWU7, RPOB_THEAQ; DR P31814, RPOB_THECE; P29398, RPOB_THEMA; P06271, RPOB_TOBAC; DR O83269, RPOB_TREPA; P59642, RPOB_TROW8; P59643, RPOB_TROWH; DR Q93GF2, RPOB_TROWT; Q9PQV6, RPOB_UREPA; Q9KV30, RPOB_VIBCH; DR Q9XPS7, RPOB_WHEAT; Q9PA86, RPOB_XYLFA; Q87A32, RPOB_XYLFT; DR P22704, RPOC_ANASP; O67763, RPOC_AQUAE; Q9X6Y2, RPOC_AQUPY; DR P56763, RPOC_ARATH; P58131, RPOC_ASTLO; P77819, RPOC_BACAN; DR Q9Z9M1, RPOC_BACHD; P37871, RPOC_BACSU; O51349, RPOC_BORBU; DR P77839, RPOC_BROTH; P57145, RPOC_BUCAI; P41185, RPOC_BUCAP; DR Q89B21, RPOC_BUCBP; Q9PI30, RPOC_CAMJE; Q9PK79, RPOC_CHLMU; DR Q9Z999, RPOC_CHLPN; O84316, RPOC_CHLTR; P56300, RPOC_CHLVU; DR Q97EH0, RPOC_CLOAB; Q93R87, RPOC_CLOPE; O19897, RPOC_CYACA; DR P42080, RPOC_CYAPA; P00577, RPOC_ECOLI; P23580, RPOC_EUGGR; DR P42074, RPOC_FISMU; O78484, RPOC_GUITH; P43739, RPOC_HAEIN; DR P36441, RPOC_HETCA; P94892, RPOC_LEUME; P94899, RPOC_LEUPS; DR P77882, RPOC_LISGR; P77879, RPOC_LISIN; Q8YA96, RPOC_LISMO; DR Q9BBS8, RPOC_LOTJA; P16024, RPOC_MAIZE; P06273, RPOC_MARPO; DR Q9MUS6, RPOC_MESVI; P47716, RPOC_MYCGA; P47582, RPOC_MYCGE; DR P30761, RPOC_MYCLE; P75271, RPOC_MYCPN; P47769, RPOC_MYCTU; DR Q9TL05, RPOC_NEPOL; P14563, RPOC_NOSCO; P49467, RPOC_ODOSI; DR P95405, RPOC_OENOE; P12092, RPOC_ORYSA; P77917, RPOC_PEDAC; DR P52733, RPOC_PINTH; P21422, RPOC_PLAFA; O33431, RPOC_PORCN; DR P51251, RPOC_PORPU; P42075, RPOC_PROHO; P42076, RPOC_PROMA; DR P42078, RPOC_PROSC; P42077, RPOC_PROV1; Q9HWC9, RPOC_PSEAE; DR P19176, RPOC_PSEPU; Q9RH40, RPOC_RICCN; Q9ZE20, RPOC_RICPR; DR Q9L9J7, RPOC_SALTY; P46819, RPOC_SINAL; P11705, RPOC_SPIOL; DR P47770, RPOC_STAAU; Q8K8W2, RPOC_STRP3; Q8P2Y2, RPOC_STRP8; DR P95816, RPOC_STRPY; Q55085, RPOC_SYNP2; P42079, RPOC_SYNP7; DR Q55346, RPOC_SYNPW; Q55348, RPOC_SYNPZ; P74177, RPOC_SYNY3; DR Q9KWU6, RPOC_THEAQ; P36252, RPOC_THEMA; P12116, RPOC_TOBAC; DR O83270, RPOC_TREPA; Q9PQV5, RPOC_UREPA; Q9KV29, RPOC_VIBCH; DR P96177, RPOC_WEIHE; P96178, RPOC_WEIPA; Q9XPS8, RPOC_WHEAT; DR Q9PA87, RPOC_XYLFA; Q87A33, RPOC_XYLFT; Q9YB53, RPOD_AERPE; DR P22705, RPOD_ANASP; P56764, RPOD_ARATH; O28002, RPOD_ARCFU; DR P58132, RPOD_ASTLO; P12465, RPOD_CHLVU; Q9TM34, RPOD_CYACA; DR P48120, RPOD_CYAPA; P23581, RPOD_EUGGR; P35018, RPOD_GALSU; DR O78483, RPOD_GUITH; Q9V2W1, RPOD_HALHA; Q00813, RPOD_HALMA; DR Q9HQJ4, RPOD_HALN1; Q9BBS7, RPOD_LOTJA; P16025, RPOD_MAIZE; DR P06274, RPOD_MARPO; Q9MUS7, RPOD_MESVI; Q57648, RPOD_METJA; DR Q8TVB8, RPOD_METKA; Q8PV16, RPOD_METMA; O26144, RPOD_METTH; DR P14564, RPOD_NOSCO; P49468, RPOD_ODOSI; P12093, RPOD_ORYSA; DR P12227, RPOD_PEA ; P41606, RPOD_PINTH; P51250, RPOD_PORPU; DR Q9V198, RPOD_PYRAB; Q8ZYQ3, RPOD_PYRAE; Q8U0E4, RPOD_PYRFU; DR O59303, RPOD_PYRHO; Q9THV5, RPOD_SINAL; Q01923, RPOD_SORBI; DR P11704, RPOD_SPIOL; P39471, RPOD_SULAC; P95989, RPOD_SULSO; DR Q96YW0, RPOD_SULTO; P73334, RPOD_SYNY3; Q9HJD9, RPOD_THEAC; DR Q97B93, RPOD_THEVO; P38550, RPOD_TOBAC; Q9XPS9, RPOD_WHEAT; DR P39466, RPOE_SULAC; Q9YAT3, RPOH_AERPE; O28394, RPOH_ARCFU; DR P15740, RPOH_HALN1; Q8TRB4, RPOH_METAC; Q58443, RPOH_METJA; DR Q8PUQ8, RPOH_METMA; O27122, RPOH_METTH; P41559, RPOH_METVA; DR Q9V116, RPOH_PYRAB; Q8ZYR0, RPOH_PYRAE; Q8U0M2, RPOH_PYRFU; DR O74019, RPOH_PYRHO; P11521, RPOH_SULAC; Q980Q9, RPOH_SULSO; DR Q976A3, RPOH_SULTO; Q03588, RPOH_THEAC; P31815, RPOH_THECE; DR Q979F2, RPOH_THEVO; Q58785, RPOI_METJA; Q9YDJ9, RPOK_AERPE; DR O29134, RPOK_ARCFU; P29200, RPOK_HALMA; Q9HQJ0, RPOK_HALN1; DR Q8TT40, RPOK_METAC; Q57650, RPOK_METJA; Q8PW42, RPOK_METMA; DR O26148, RPOK_METTH; Q8ZTF9, RPOK_PYRAE; Q8U0E8, RPOK_PYRFU; DR Q9V193, RPOK_PYRHO; P39463, RPOK_SULAC; Q97ZJ9, RPOK_SULSO; DR Q972B1, RPOK_SULTO; Q9HJ14, RPOK_THEAC; P58232, RPOK_THEVO; DR Q9YEZ1, RPOL_AERPE; O30032, RPOL_ARCFU; P18147, RPOL_BPK11; DR P06221, RPOL_BPSP6; P07659, RPOL_BPT3 ; P00573, RPOL_BPT7 ; DR Q9HR53, RPOL_HALN1; P05472, RPOL_KLULA; Q8TSS4, RPOL_METAC; DR Q57832, RPOL_METJA; Q8TZ81, RPOL_METKA; Q8PVT0, RPOL_METMA; DR O27372, RPOL_METTH; Q9V2M4, RPOL_PYRAB; Q8ZW46, RPOL_PYRAE; DR Q8U4N1, RPOL_PYRFU; P57671, RPOL_PYRHO; P46217, RPOL_SULAC; DR Q980K0, RPOL_SULSO; Q96YA7, RPOL_SULTO; Q9HIC5, RPOL_THEAC; DR Q978F5, RPOL_THEVO; P92969, RPOM_ARATH; O29033, RPOM_ARCFU; DR O00411, RPOM_HUMAN; Q58548, RPOM_METJA; O27369, RPOM_METTH; DR P38671, RPOM_NEUCR; O13993, RPOM_SCHPO; Q07271, RPOM_SULAC; DR Q56254, RPOM_THECE; P13433, RPOM_YEAST; Q9YB47, RPON_AERPE; DR O29135, RPON_ARCFU; P29199, RPON_HALMA; Q9HQJ1, RPON_HALN1; DR Q8TT41, RPON_METAC; Q57649, RPON_METJA; Q8TVB4, RPON_METKA; DR Q8PW43, RPON_METMA; O26147, RPON_METTH; Q9V194, RPON_PYRAB; DR Q8ZYP9, RPON_PYRAE; O59298, RPON_PYRHO; P39472, RPON_SULAC; DR Q980Z8, RPON_SULSO; Q96YW4, RPON_SULTO; Q9HL09, RPON_THEAC; DR Q979K0, RPON_THEVO; P33539, RPOP_AGABT; O30180, RPOP_ARCFU; DR P22372, RPOP_CLAPU; O03685, RPOP_GELSP; Q9HSG9, RPOP_HALN1; DR P10581, RPOP_MAIZE; Q8TPX9, RPOP_METAC; P59283, RPOP_METJA; DR Q8TYC4, RPOP_METKA; P33540, RPOP_NEUCR; P33541, RPOP_NEUIN; DR Q01521, RPOP_PODAN; Q9V201, RPOP_PYRAB; Q8ZVI9, RPOP_PYRAE; DR Q8TZI3, RPOP_PYRFU; O74105, RPOP_PYRHO; Q97ZX7, RPOP_SULSO; DR Q975R9, RPOP_SULTO; O24600, RPOT_ARATH; Q8UGK8, RPOZ_AGRT5; DR Q8YNB9, RPOZ_ANASP; O66570, RPOZ_AQUAE; Q9K9Y3, RPOZ_BACHD; DR O35011, RPOZ_BACSU; Q8G3H3, RPOZ_BIFLO; Q9RH70, RPOZ_BRAJA; DR Q8YG64, RPOZ_BRUME; Q8G1Q6, RPOZ_BRUSU; Q9PN25, RPOZ_CAMJE; DR P58066, RPOZ_CAUCR; Q97IC9, RPOZ_CLOAB; Q8XJK9, RPOZ_CLOPE; DR Q8FT46, RPOZ_COREF; Q8NQ43, RPOZ_CORGL; O19907, RPOZ_CYACA; DR Q9RRJ6, RPOZ_DEIRA; P08374, RPOZ_ECOLI; O78442, RPOZ_GUITH; DR P43740, RPOZ_HAEIN; O25467, RPOZ_HELPY; Q9CEE4, RPOZ_LACLA; DR Q88WL6, RPOZ_LACPL; Q92AI2, RPOZ_LISIN; Q8Y673, RPOZ_LISMO; DR Q9MUL7, RPOZ_MESVI; Q9CCQ6, RPOZ_MYCLE; P71660, RPOZ_MYCTU; DR Q9JQS9, RPOZ_NEIMA; Q8ER27, RPOZ_OCEIH; Q9CMB2, RPOZ_PASMU; DR P51376, RPOZ_PORPU; Q9HTM1, RPOZ_PSEAE; Q88C82, RPOZ_PSEPK; DR Q88BE3, RPOZ_PSESM; Q8XXG0, RPOZ_RALSO; Q985B3, RPOZ_RHILO; DR Q92R52, RPOZ_RHIME; Q92H89, RPOZ_RICCN; Q9ZCX4, RPOZ_RICPR; DR Q8EJU7, RPOZ_SHEON; Q99UQ8, RPOZ_STAAM; Q8CSW3, RPOZ_STAEP; DR Q8E755, RPOZ_STRA3; Q9KXS1, RPOZ_STRCO; Q8GAU3, RPOZ_STRKA; DR Q8DVK5, RPOZ_STRMU; Q97PA4, RPOZ_STRPN; P82577, RPOZ_STRPY; DR Q8DGQ8, RPOZ_SYNEL; P74352, RPOZ_SYNY3; Q9EVV4, RPOZ_THEAQ; DR Q9X214, RPOZ_THEMA; Q8RQE7, RPOZ_THETH; Q8R9S7, RPOZ_THETN; DR O83699, RPOZ_TREPA; Q9KNM3, RPOZ_VIBCH; Q87TB0, RPOZ_VIBPA; DR Q8DDV5, RPOZ_VIBVU; Q8D2E9, RPOZ_WIGBR; Q8NL41, RPOZ_XANAC; DR Q9PD77, RPOZ_XYLFA; Q87DG6, RPOZ_XYLFT; Q8ZJQ3, RPOZ_YERPE; // ID 2.7.7.7 DE DNA-directed DNA polymerase. AN DNA nucleotidyltransferase (DNA-directed). CA N deoxynucleoside triphosphate = N diphosphate + {DNA}(N). CC -!- Catalyzes DNA-template-directed extension of the 3'-end of an RNA CC strand by one nucleotide at a time. CC -!- Cannot initiate a chain de novo. CC -!- Requires a primer which may be DNA or RNA. CC -!- See also EC 2.7.7.49. PR PROSITE; PDOC00412; PR PROSITE; PDOC00107; PR PROSITE; PDOC00452; DR O28552, DP2L_ARCFU; Q9HMX8, DP2L_HALN1; Q8THG5, DP2L_METAC; DR Q59024, DP2L_METJA; Q8TUV3, DP2L_METKA; Q8PXH2, DP2L_METMA; DR O27579, DP2L_METTH; Q9V2F4, DP2L_PYRAB; P81409, DP2L_PYRFU; DR O57861, DP2L_PYRHO; Q9HM33, DP2L_THEAC; Q97CR6, DP2L_THEVO; DR O28484, DP2S_ARCFU; Q9HMR7, DP2S_HALN1; Q58113, DP2S_METJA; DR O27456, DP2S_METTH; Q9V2F3, DP2S_PYRAB; P81412, DP2S_PYRFU; DR O57863, DP2S_PYRHO; Q9HLK5, DP2S_THEAC; O67125, DP3A_AQUAE; DR Q9K838, DP3A_BACHD; O34623, DP3A_BACSU; O51526, DP3A_BORBU; DR P57332, DP3A_BUCAI; Q8K9S3, DP3A_BUCAP; Q9PPI9, DP3A_CAMJE; DR Q9PJJ7, DP3A_CHLMU; Q9Z7N8, DP3A_CHLPN; O84549, DP3A_CHLTR; DR Q9RX08, DP3A_DEIRA; P10443, DP3A_ECOLI; P43743, DP3A_HAEIN; DR Q9ZJF9, DP3A_HELPJ; P56157, DP3A_HELPY; Q9CI70, DP3A_LACLA; DR Q49405, DP3A_MYCGE; Q9X7F0, DP3A_MYCLE; P75404, DP3A_MYCPN; DR Q10779, DP3A_MYCTU; Q9JVX8, DP3A_NEIMA; Q9JXZ2, DP3A_NEIMB; DR Q9CPK3, DP3A_PASMU; Q9HXZ1, DP3A_PSEAE; Q9XDH6, DP3A_PSEFL; DR O05974, DP3A_RICPR; P34699, DP3A_SACER; P14567, DP3A_SALTY; DR Q9F1K0, DP3A_STAAU; Q9Z618, DP3A_STRCO; Q8K7A1, DP3A_STRP3; DR Q8P0S5, DP3A_STRP8; Q9FDF6, DP3A_STRPY; P74750, DP3A_SYNY3; DR Q9XDH5, DP3A_THEAQ; Q9ZHG4, DP3A_THEMA; O83675, DP3A_TREPA; DR Q9PQ74, DP3A_UREPA; P52022, DP3A_VIBCH; Q9PGU4, DP3A_XYLFA; DR Q87EY0, DP3A_XYLFT; O68770, DP3A_YERPE; P24701, DP3B_ACTPL; DR O67725, DP3B_AQUAE; Q9RCA1, DP3B_BACHD; P05649, DP3B_BACSU; DR P33761, DP3B_BORBU; P57127, DP3B_BUCAI; P29439, DP3B_BUCAP; DR Q89B36, DP3B_BUCBP; Q9EVE4, DP3B_BUCRP; P48198, DP3B_CAUCR; DR Q9PKW4, DP3B_CHLMU; Q9Z8K0, DP3B_CHLPN; O84078, DP3B_CHLTR; DR P00583, DP3B_ECOLI; P43744, DP3B_HAEIN; Q9ZLX4, DP3B_HELPJ; DR O25242, DP3B_HELPY; Q9CJJ1, DP3B_LACLA; O54376, DP3B_LACLC; DR P21174, DP3B_MICLU; O33914, DP3B_MYCBO; P24117, DP3B_MYCCA; DR P47247, DP3B_MYCGE; P46387, DP3B_MYCLE; Q9L7L6, DP3B_MYCPA; DR Q50313, DP3B_MYCPN; Q98RK6, DP3B_MYCPU; P52851, DP3B_MYCSM; DR Q50790, DP3B_MYCTU; P22838, DP3B_PROMI; Q9I7C4, DP3B_PSEAE; DR P13455, DP3B_PSEPK; P31861, DP3B_RHOCA; Q92I37, DP3B_RICCN; DR Q9ZDB3, DP3B_RICPR; P26464, DP3B_SALTY; P29438, DP3B_SERMA; DR P34029, DP3B_SPICI; P50029, DP3B_STAAM; P27903, DP3B_STRCO; DR O06672, DP3B_STRPN; P59651, DP3B_STRR6; P52023, DP3B_SYNP7; DR P72856, DP3B_SYNY3; O83048, DP3B_TREPA; Q9KVX5, DP3B_VIBCH; DR P52620, DP3B_VIBHA; O67074, DP3E_AQUAE; P57337, DP3E_BUCAI; DR Q08880, DP3E_BUCAP; Q89AN3, DP3E_BUCBP; P03007, DP3E_ECOLI; DR P43745, DP3E_HAEIN; Q9CPE0, DP3E_PASMU; O68045, DP3E_RHOCA; DR Q92GL1, DP3E_RICCN; Q9ZCJ9, DP3E_RICPR; P14566, DP3E_SALTY; DR O83649, DP3E_TREPA; P09122, DP3X_BACSU; P57553, DP3X_BUCAI; DR Q8K983, DP3X_BUCAP; Q89A95, DP3X_BUCBP; P06710, DP3X_ECOLI; DR P43746, DP3X_HAEIN; P47659, DP3X_MYCGE; P75177, DP3X_MYCPN; DR O69688, DP3X_MYCTU; P74876, DP3X_SALTY; P47658, DP3Z_MYCGE; DR Q8UFV3, DP41_AGRT5; Q9KCU7, DP41_BACHD; P54545, DP41_BACSU; DR Q8PYH6, DP41_METMA; Q10787, DP41_MYCTU; Q98LV1, DP41_RHILO; DR Q92QM8, DP41_RHIME; P96022, DP41_SULSO; Q8UJK7, DP42_AGRT5; DR Q9K9A8, DP42_BACHD; P54560, DP42_BACSU; Q8PT42, DP42_METMA; DR P95102, DP42_MYCTU; Q98JM5, DP42_RHILO; Q92XH8, DP42_RHIME; DR Q97W02, DP42_SULSO; Q98NW7, DP43_RHILO; P24482, DPB2_YEAST; DR P27344, DPB3_YEAST; O48520, DPD2_ARATH; P49004, DPD2_BOVIN; DR Q19366, DPD2_CAEEL; Q9W088, DPD2_DROME; P49005, DPD2_HUMAN; DR O35654, DPD2_MOUSE; Q9LRE5, DPD2_ORYSA; P87324, DPD2_SCHPO; DR O93610, DPD2_XENLA; P46957, DPD2_YEAST; Q19196, DPE2_CAEEL; DR P56282, DPE2_HUMAN; O54956, DPE2_MOUSE; Q92076, DPG1_CHICK; DR Q27607, DPG1_DROME; P54098, DPG1_HUMAN; P54099, DPG1_MOUSE; DR Q9QYV8, DPG1_RAT ; Q91684, DPG1_XENLA; Q9UHN1, DPG2_HUMAN; DR Q9QZM2, DPG2_MOUSE; Q9W6G7, DPG2_XENLA; O93745, DPO1_AERPE; DR Q59156, DPO1_ANATH; O67779, DPO1_AQUAE; Q04957, DPO1_BACCA; DR P52026, DPO1_BACST; O34996, DPO1_BACSU; O51498, DPO1_BORBU; DR O08307, DPO1_CHLAU; P52027, DPO1_DEIRA; P00582, DPO1_ECOLI; DR P43741, DPO1_HAEIN; Q9ZJE9, DPO1_HELPJ; P56105, DPO1_HELPY; DR P09804, DPO1_KLULA; Q9CDS1, DPO1_LACLA; O32801, DPO1_LACLC; DR P46835, DPO1_MYCLE; Q07700, DPO1_MYCTU; Q9S1G2, DPO1_RHILE; DR Q9RAA9, DPO1_RICFE; Q9RLB6, DPO1_RICHE; O05949, DPO1_RICPR; DR Q9F173, DPO1_SALTY; P59199, DPO1_STRPN; P59200, DPO1_STRR6; DR P95690, DPO1_SULAC; O50607, DPO1_SULOH; P26811, DPO1_SULSO; DR Q55971, DPO1_SYNY3; P19821, DPO1_THEAQ; P80194, DPO1_THECA; DR O52225, DPO1_THEFI; P74933, DPO1_TREPA; O93746, DPO2_AERPE; DR P21189, DPO2_ECOLI; P05468, DPO2_KLULA; Q07635, DPO2_SULSO; DR Q9KA72, DPO3_BACHD; P13267, DPO3_BACSU; Q8XJR3, DPO3_CLOPE; DR Q9CDT7, DPO3_LACLA; Q92C34, DPO3_LISIN; Q8Y7G1, DPO3_LISM