PIR:S48702 >P1;S48702 glutamyl-tRNA(Glu) reductase - Barley C;Species: Hordeum vulgare (barley) C;Date: 01-Aug-1995 #sequence_revision 01-Aug-1995 #text_change 01-Aug-1995 C;Accession: S48702 R;Pontoppidan, B.; Kannangara, C.G. Eur. J. Biochem. 225, 529-537, 1994 A;Title: Purification and partial characterisation of barley glutamyl-tRNA(Glu) reductase, the enzyme that directs glutamate to chlorophyll biosynthesis. A;Reference number: S48702 A;Accession: S48702 A;Status: preliminary A;Residues: 1-20 >S48702 DAGGDAQAASKAASITALQK PIR:S65773 >P1;S65773 glutamyl-tRNA reductase 2 precursor - Arabidopsis thaliana C;Species: Arabidopsis thaliana (mouse-ear cress) C;Date: 28-Oct-1996 #sequence_revision 28-Oct-1996 #text_change 28-Oct-1996 C;Accession: S65773 R;Kumar, A.M.; Csankovszki, G.; Soell, D. Plant Mol. Biol. 30, 419-426, 1996 A;Title: A second and differentially expressed glutamyl-tRNA reductase gene from Arabidopsis thaliana. A;Reference number: S65773 A;Accession: S65773 A;Status: preliminary A;Residues: 1-530 A;Cross-references: EMBL:U27118 >S65773 MAVSSAFVVTPKLEKLLANHHNPTYSSSPAPLDVIGIRALPMNNRNKRGLIQRARCEISP SNKAASISALEQLKTSAIDRYTKERSSIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAEL CGLNHIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGIPVSEICQHRFLLYNKD VTQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTE TNIAAGAVSVSSAAVELALMKLPESSHASSARMLVVGAGKMGKLVIKHLVAKGCTKMVVV NRSEEKVAAVRNEMPPGVEIIYKPLDEMLSCAAEADVVFTSTASETPLFLKEQVETLPPV RDARLFVDISVPRNVGSCVAEIDGTRVFNVDDLKEVVAANKEDRVRKAMEAQAIITDESK HFEAWRDSLETVPTIKKLRGYTERIIAAEIEKSLPKMGIDMNKKMRKTVDDLIRGIVNKL LHGPMQHLRCDGNDSRTLSETLDNMQALNRMYGLDAEILEEKIRAKVEKK PIR:H64317 >P1;H64317 glutamyl-tRNA reductase - Methanococcus jannaschii C;Species: Methanococcus jannaschii C;Date: 13-Sep-1996 #sequence_revision 13-Sep-1996 #text_change 13-Sep-1996 C;Accession: H64317 R;Bult, C.J.; White, O.; Olsen, G.J.; Zhou, L.; Fleischmann, R.D.; Sutton, G.G.; Blake, J.A.; FitzGerald, L.M.; Clayton, R.A.; Gocayne, J.D.; Kerlavage, A.R.; Dougherty, B.A.; Tomb, J.F.; Adams, M.D.; Reich, C.I.; Overbeek, R.; Kirkness, E.F.; Weinstock, K.G.; Merrick, J.M.; Glodek, A.; Scott, J.L.; Geoghagen, N.S.M.; Weidman, J.F.; Fuhrmann, J.L.; Nguyen, D.; Utterback, T.R.; Kelley, J.M.; Peterson, J.D.; Sadow, P.W.; Hanna, M.C.; Cotton, M.D.; Roberts, K.M.; Hurst, M.A.; Kaine, B.P. Science 273, 1058-1073, 1996 A;Authors: Borodovsky, M.; Klenk, H.P.; Fraser, C.M.; Smith, H.O.; Woese, C.R.; Venter, J.C. A;Title: Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii. A;Reference number: A64300 A;Accession: H64317 A;Status: preliminary; nucleic acid sequence not shown; translation not shown A;Molecule type: DNA A;Residues: 1-392 A;Cross-references: GB:L77117; TIGR:MJ0143; CDS_PID:g1510276 C;Genetics: A;Map position: FOR140221-141399 >H64317 MIILKADYKKYNVSELEKLRMDEEKFYETFDNAILLQTCNRVEIIFDADSLEEIKGIENI DLEKFDILFGDKAIEHLFRVACGLESMIVGEDQILGQLKNAYLKAKEKGRISKKLEKIIL KAIHTGQRARVETKINEGGVSIGSAAVELAEKIFGLEGKNVLLIGAGEMANLVIKALKEK NIKAIIVANRTYEKAEKLAKELGGMAIKFDKLEEALRYADIVISATGAPHPILNKERLKN AGKTIIIDIANPRDTTDDIRELPDIFLFTIDDLRLVAEENLKKRKEEIPKVEMIICEELE RLKEFLDKMRFETAIKELGQYIENVRKKEVEKAKKILKNKNKPVEEVLEDFSKALCKRII YDIIKIFENVEDKEVFECLAKEFKKLGNKNKN PIR:S27546 >P1;S27546 glutamyl-tRNA reductase - Chlorobium sp. C;Species: Chlorobium sp. C;Date: 22-Nov-1993 #sequence_revision 26-May-1995 #text_change 03-May-1996 C;Accession: S27546 R;Majumdar, D.; Avissar, Y.J.; Wyche, J.H.; Beale, S.I. submitted to the EMBL Data Library, July 1991 A;Description: Structure and expression of the Chlorobium vibrioforme hemA gene. A;Reference number: S27546 A;Accession: S27546 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-415 A;Cross-references: EMBL:M59194 A;Note: the source is designated as Chlorobium vibrioforme C;Superfamily: hemA protein >S27546 MNIISVGVNHKTAPIEIRERIALSEVQNKEFVTDLVSSGLASEAMVVSTCNRTELYVVPG MPEVNCDYLKDYIISYKDARNAVRPEHFFNRFYCGTARHLFEVSSAIDSLVLGEGQILGQ VKDAYRIAAEVGTAGILLTRLCHSPFSVAKKVKTRTKLMEGAVSVSYAAVELAQKIFSNL SMKKVLLIGAVKQSWQQSTCTPRTPGTSSSPTGRNPRPRACEELGTNRVLPYESYKEHLH EFDIIITAVSTKEYILNAAEMQQSMAKRRLKPVIILDLGLPRNVDPEVGALQNMFLKDID ALKHIIDKNLERRRAELPKVKSIIDEELIASASGSTPSRYVRPSLTCNPSSSKSRRKNSS VPPQGERRGVEAHGTPDRQDPEKNPASSYQDAQGSGRYRRQHPQQSQPRQEHLRS PIR:A48359 >P1;A48359 glutamyl-tRNA reductase HemA - Chlorobium vibrioforme C;Species: Chlorobium vibrioforme C;Date: 19-Nov-1993 #sequence_revision 18-Nov-1994 #text_change 19-Oct-1995 C;Accession: A48359 R;Majumdar, D.; Avissar, Y.J.; Wyche, J.H.; Beale, S.I. Arch. Microbiol. 156, 281-289, 1991 A;Title: Structure and expression of the Chlorobium vibrioforme hemA gene. A;Reference number: A48359; MUID:92171712 A;Accession: A48359 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-415 A;Cross-references: NCBIN:86184; NCBIP:86186 A;Note: sequence extracted from NCBI backbone C;Superfamily: hemA protein >A48359 MNIISVGVNHKTAPIEIRERIALSEVQNKEFVTDLVSSGLASEAMVVSTCNRTELYVVPG MPEVNCDYLKDYIISYKDARNAVRPEHFFNRFYCGTARHLFEVSSAIDSLVLGEGQILGQ VKDAYRIAAEVGTAGILLTRLCHSPFSVAKKVKTRTKLMEGAVSVSYAAVELAQKIFSNL SMKKVLLIGAVKQSWQQSTCTPRTPGTSSSPTGRNPRPRACEELGTNRVLPYESYKEHLH EFDIIITAVSTKEYILNAAEMQQSMAKRRLKPVIILDLGLPRNVDPEVGALQNMFLKDID ALKHIIDKNLERRRAELPKVKSIIDEELIASASGSTPSRYVRPSLTCNPSSSKSRRKNSS VPPQGERRGVEAHGTPDRQDPEKNPASSYQDAQGSGRYRRQHPQQSQPRQEHLRS PIR:S51136 >P1;S51136 glutamyl-tRNA reductase - Methanobacterium thermoautotrophicum C;Species: Methanobacterium thermoautotrophicum C;Date: 07-May-1995 #sequence_revision 01-Sep-1995 #text_change 19-Oct-1995 C;Accession: S51136 R;Hungerer, C.; Weiss, D.; Thauer, R.K.; Jahn, D. submitted to the EMBL Data Library, January 1995 A;Description: Cloning and characterization of the Methanobacterium thermoautotrophicum hemA gene encoding glutamyl-tRNA reductase. A;Reference number: S51136 A;Accession: S51136 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-398 A;Cross-references: EMBL:X83691 C;Genetics: A;Start codon: GTG C;Superfamily: hemA protein >S51136 MILNIRLDHKTSDVKTMETASGRIEEIVGELEALGAVTEKVPLMTCNRVEYYLHVTGVPP EFDFNGFTVEKDEDALLHLLRLASGLESMIIGEDQILGQIKAARLQALREGTCGPLLDMV FTKAVHVGQTVRRKTKINRGSVSIGSAAVDLAESIHGDLKCKKVLVIGAGKMGTLVARAL AEKHLKAIMVANRTYERAYQLACELGGDAIHFDRLNRALRDADVVISATGSPHYILTRER VMDAVPPERRSSIVMVDIANPRDIEESVRELGVRLFTIDDLRGVAEENRKRREAEAREAE GIVRAELELLLRAMKHREVEPLLAEIRGRMESLRQREAGKAIKKIENSKDPERVVEGLTR SIVDKIFHDIALKIRDAAERDDREFLRMCSELFDCDES PIR:A38087 >P1;A38087 glutamyl-tRNA reductase - Synechocystis sp. (PCC 6803) C;Species: Synechocystis sp. C;Date: 19-May-1994 #sequence_revision 19-May-1994 #text_change 19-Oct-1995 C;Accession: A38087; S37660 R;Verkamp, E.; Jahn, M.; Jahn, D.; Kumar, A.M.; Soell, D. J. Biol. Chem. 267, 8275-8280, 1992 A;Title: Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression. A;Reference number: A38087 A;Accession: A38087 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-427 A;Cross-references: GB:M84218 R;Grimm, B. Hereditas 117, 195-197, 1992 A;Title: Identification of a hemA gene from Synechocystis by complementation of an E. coli hemA mutant. A;Reference number: S37660 A;Accession: S37660 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-427 A;Cross-references: EMBL:X65963 C;Genetics: A;Gene: hemA C;Superfamily: hemA protein >A38087 MNIAVVGLSHKTAPVEIREKLSIQEAKLEEALTHLRSYPHIEEVTVISTCNRLEIYAVVT DTEKGVVEITQFLSETGNIPLATLRRYLFTLLHEDAVRHLMRVAAGLESLVLGEGQILAQ VRTTHKLGQKYKGVGRLLDRLFKQAITAGRRVRTETDIGTGAVSISSAAVELVHRQVDLS SQKTVIIGAGKMACLLVKHLLAKGATDITIVNRSQRRSQDLANQFPQAQLTLCPLTDMFT AIAAGDIVFTSTGATEPILNCENLTGCVINRKSLMLVDISVPRNVAADVHAMEQVRAFNV DDLKEVVAQNQASRRQMARQAEALLEEEIAAFDLWWRSLETVPTISSLRSKVEDIREQEL EKALSRLGSEFAEKHQEVIEALTRGIVNKILHEPMVQLRAQQDIEARKQCLRSLKMLFDL EVEEQFG SWISSNEW:HEM1_ECOLI ID HEM1_ECOLI STANDARD; PRT; 418 AA. AC P13580; DT 01-JAN-1990 (REL. 13, CREATED) DT 01-JAN-1990 (REL. 13, LAST SEQUENCE UPDATE) DT 01-JUN-1996 (REL. 34, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 89359103. RA VERKAMP E., CHELM B.K.; RL J. BACTERIOL. 171:4728-4735(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 90060810. RA LI J.-M., RUSSELL C.S., COSLOY S.D.; RL GENE 82:209-217(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 89313673. RA DROLET M., PELOQUIN L., ECHELARD Y., COUSINEAU L., SASARMAN A.; RL MOL. GEN. GENET. 216:347-352(1989). RN [4] RP SEQUENCE FROM N.A. RA REMLER P., WOISETSCHLAEGER M., STROHMAIER H.; RL SUBMITTED (DEC-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [5] RP SEQUENCE OF 1-48 FROM N.A. RX MEDLINE; 93051347. RA IKEMI M., MURAKAMI K., HASHIMOTO M., MUROOKA Y.; RL GENE 121:127-132(1992). RN [6] RP FUNCTION. RX MEDLINE; 92235044. RA VERKAMP E., JAHN M., JAHN D., KUMAR A.M., SOELL D.; RL J. BIOL. CHEM. 267:8275-8280(1992). CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN IN POSITIONS 151 CC TO 172 DUE TO FRAMESHIFTS. DR EMBL; M25323; G146333; -. DR EMBL; M30785; G146330; -. DR EMBL; D10264; G216523; -. DR EMBL; U18555; G968929; -. DR PIR; S04414; BVECHA. DR PIR; A45918; A45918. DR ECOGENE; EG10427; HEMA. DR PROSITE; PS00747; GLUTR. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP. FT CONFLICT 243 243 A -> R (IN REF. 2 AND 4). FT CONFLICT 365 365 A -> R (IN REF. 3). SQ SEQUENCE 418 AA; 46306 MW; 5F338C6F CRC32; >HEM1_ECOLI MTLLALGINHKTAPVSLRERVSFSPDKLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVE EQDNLQEALIRWLCDYHNLNEEDLRKSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQ VKKAFADSQKGHMKASELERMFQKSFSVAKRVRTETDIGASAVSVAFAACTLARQIFESL STVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQILADEVGAEVIALSDIDERL READIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSV DDLQSIISHNLAQRKAAAVEAETIVAQETSEFMAWLRAQSASETIREYRSQAEQVRDELT AKALAALEQGGDAQAIMQDLAWKLTNRLIHAPTKSLQQAARDGDNERLNILRDSLGLE SWISSPROT:HEMX_SYNY3 ID HEMX_SYNY3 STANDARD; PRT; 42 AA. AC P29107; DT 01-DEC-1992 (REL. 24, CREATED) DT 01-DEC-1992 (REL. 24, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE PUTATIVE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR) (FRAGMENT). OS SYNECHOCYSTIS SP. (STRAIN PCC 6803). OC PROKARYOTA; GRACILICUTES; OXYPHOTOBACTERIA; OC CYANOBACTERIA (BLUE-GREEN ALGAE); CHROOCOCCALES. RN [1] RP SEQUENCE. RX MEDLINE; 91236752. RA RIEBLE S., BEALE S.I.; RL J. BIOL. CHEM. 266:9740-9745(1991). CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- SUBUNIT: HOMOOCTAMER. CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC INVOLVED IN CHLOROPHYLL BIOSYNTHESIS. CC -!- INDUCTION: REGULATION BY LIGHT. CC -!- ENZYME REGULATION: FEEDBACK INHIBITION BY HEME. CC -!- SIMILARITY: THIS ENZMYE IS NOT SIMILAR TO ALL OTHER CURRENTLY CC KNOWN GLUTAMYL-TRNA REDUCTASES AND COULD POSSIBLY BE A SECOND CC FORM OF THE ENZYME. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. FT NON_TER 42 42 SQ SEQUENCE 42 AA; 4537 MW; 47673320 CRC32; >HEMX_SYNY3 ARMYYDQDANLDLLAGKTVAIIGYGSQXHAHALNLKDXGVNV SWISSPROT:HEM2_ARATH ID HEM2_ARATH STANDARD; PRT; 530 AA. AC P49294; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE 2 PRECURSOR (EC 1.2.1.-) (GLUTR). GN HEMA2. OS ARABIDOPSIS THALIANA (MOUSE-EAR CRESS). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; OC CAPPARALES; CRUCIFERAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE; 96189258. RA KUMAR A.M., CSANKOVSZKI G., SOLL D.; RL PLANT MOL. BIOL. 30:419-426(1996). CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SUBCELLULAR LOCATION: CHLOROPLAST (BY SIMILARITY). CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; U27118; G1049057; -. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP; TRANSIT PEPTIDE; KW CHLOROPLAST; MULTIGENE FAMILY. FT TRANSIT 1 ? CHLOROPLAST (POTENTIAL). FT CHAIN ? 530 GLUTAMYL-TRNA REDUCTASE 2. SQ SEQUENCE 530 AA; 58305 MW; B08953B6 CRC32; >HEM2_ARATH MAVSSAFVVTPKLEKLLANHHNPTYSSSPAPLDVIGIRALPMNNRNKRGLIQRARCEISP SNKAASISALEQLKTSAIDRYTKERSSIVVIGLSIHTAPVEMREKLAIPEAEWPRAIAEL CGLNHIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSKTSGIPVSEICQHRFLLYNKD VTQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAITVGKRVRTE TNIAAGAVSVSSAAVELALMKLPESSHASSARMLVVGAGKMGKLVIKHLVAKGCTKMVVV NRSEEKVAAVRNEMPPGVEIIYKPLDEMLSCAAEADVVFTSTASETPLFLKEQVETLPPV RDARLFVDISVPRNVGSCVAEIDGTRVFNVDDLKEVVAANKEDRVRKAMEAQAIITDESK HFEAWRDSLETVPTIKKLRGYTERIIAAEIEKSLPKMGIDMNKKMRKTVDDLIRGIVNKL LHGPMQHLRCDGNDSRTLSETLDNMQALNRMYGLDAEILEEKIRAKVEKK SWISSPROT:HEM1_XANCH ID HEM1_XANCH STANDARD; PRT; 426 AA. AC P42808; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA. OS XANTHOMONAS CAMPESTRIS (PV. PHASEOLI). OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC PSEUDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=HUT 8925; RX MEDLINE; 94176146. RA ASAHARA N., MURAKAMI K., KOBRISATE S., HASHIMOTO Y., MUROOKA Y.; RL APPL. MICROBIOL. BIOTECHNOL. 40:846-850(1994). CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; D15073; G976260; -. DR PROSITE; PS00747; GLUTR. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP. SQ SEQUENCE 426 AA; 46768 MW; 171E1C8C CRC32; >HEM1_XANCH MTLWVLGLNHQTAPVDLRERAAFAGDALPRALESLRALPQVSEAALLSTCNRTELYAMAE EAHSLVTWLETHAPALSGYLYQHQEAEAVRHLFRVATGLDSMVLGEPQILGQVKDAWAVA RAHGTLGSGLDRLFQQTFSVAKRARTDTRVGANPVSVASTAVRLAQDSFARLNESTVLLI GAGETIELAAKHLSEGRVRRLLIANRTLAHAQTLASQHGGFALPLTDLERHLAEADVVFS ATAAREPLVTRAQVEQALRARKRKPMLLFDLAVPRDIEASVGELSDAYLYTVDDLERAVE DNRRGRREAADQAEAIIDLQVARYVETLQANARQAPLKRLRAFGDSTRDELLAKARQQLH NGKPADEVLEQLAHALTNRLLHPPTAALRDAALNNDLELTTAADRLFPEKPGLPTSPHSY PDREDR SWISSPROT:HEM1_SYNY3 ID HEM1_SYNY3 STANDARD; PRT; 427 AA. AC P28463; DT 01-DEC-1992 (REL. 24, CREATED) DT 01-DEC-1992 (REL. 24, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA. OS SYNECHOCYSTIS SP. (STRAIN PCC 6803). OC PROKARYOTA; GRACILICUTES; OXYPHOTOBACTERIA; OC CYANOBACTERIA (BLUE-GREEN ALGAE); CHROOCOCCALES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 92235044. RA VERKAMP E., JAHN M., JAHN D., KUMAR A.M., SOELL D.; RL J. BIOL. CHEM. 267:8275-8280(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 93093989. RA GRIMM B.; RL HEREDITAS 117:195-197(1992). CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- SUBUNIT: HOMOOCTAMER. CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC INVOLVED IN CHLOROPHYLL BIOSYNTHESIS. CC -!- ENZYME REGULATION: FEEDBACK INHIBITION BY HEME. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; M84218; G154470; -. DR EMBL; X65963; G288422; -. DR PIR; S37660; S37660. DR PIR; A38087; A38087. DR PROSITE; PS00747; GLUTR. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 427 AA; 47525 MW; 84CCF5CA CRC32; >HEM1_SYNY3 MNIAVVGLSHKTAPVEIREKLSIQEAKLEEALTHLRSYPHIEEVTVISTCNRLEIYAVVT DTEKGVVEITQFLSETGNIPLATLRRYLFTLLHEDAVRHLMRVAAGLESLVLGEGQILAQ VRTTHKLGQKYKGVGRLLDRLFKQAITAGRRVRTETDIGTGAVSISSAAVELVHRQVDLS SQKTVIIGAGKMACLLVKHLLAKGATDITIVNRSQRRSQDLANQFPQAQLTLCPLTDMFT AIAAGDIVFTSTGATEPILNCENLTGCVINRKSLMLVDISVPRNVAADVHAMEQVRAFNV DDLKEVVAQNQASRRQMARQAEALLEEEIAAFDLWWRSLETVPTISSLRSKVEDIREQEL EKALSRLGSEFAEKHQEVIEALTRGIVNKILHEPMVQLRAQQDIEARKQCLRSLKMLFDL EVEEQFG SWISSPROT:HEM1_SALTY ID HEM1_SALTY STANDARD; PRT; 418 AA. AC P13581; DT 01-JAN-1990 (REL. 13, CREATED) DT 01-JAN-1990 (REL. 13, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA. OS SALMONELLA TYPHIMURIUM. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 89291746. RA ELLIOTT T.; RL J. BACTERIOL. 171:3948-3960(1989). CC -!- FUNCTION: IN ENTERIC BACTERIA THE SYNTHESIS OF 5-AMINOLEVULINATE CC REQUIRES BOTH HEMA AND HEML PROTEINS; HEMA PROTEIN MAY BE AN ALA CC SYNTHASE WHOSE ACTION OR SYNTHESIS IS FACILITATED BY HEML PROTEIN. CC HOWEVER, THE MECHANISM OF ALA SYNTHESIS IN ENTERIC BACTERIA IS NOT CC YET KNOWN. CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; J04243; G154103; -. DR PIR; A32661; BVEBHA. DR STYGENE; SG10149; HEMA. DR PROSITE; PS00747; GLUTR. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP. SQ SEQUENCE 418 AA; 46132 MW; EFB9BB69 CRC32; >HEM1_SALTY MTLLALGINHKTAPVSLRERVTFSPDTLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVE EQDNLQEALIRWLCDYHNLNEDDLRNSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQ VKKAFADSQKGHLNASALRRMFQKSFSVAKRVRTETDIGASAVSVAFAACTLARQIFESL STVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQALADEVGAEVISLSDIDARL QDADIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSV DDLQSIISHNLAQRQAAAVEAETIVEQEASEFMAWLRAQGASETIREYRSQSEQIRDELT TKALSALQQGGDAQAILQDLAWKLTNRLIHAPTKSLQQAARDGDDERLNILRDSLGLE SWISSPROT:HEM1_PSEAE ID HEM1_PSEAE STANDARD; PRT; 388 AA. AC P42807; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA. OS PSEUDOMONAS AERUGINOSA. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC PSEUDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=PAO1; RX MEDLINE; 95189718. RA HUNGERER C., TROUP B., ROEMLING U., JAHN D.; RL J. BACTERIOL. 177:1435-1443(1995). CC -!- FUNCTION: IN ENTERIC BACTERIA THE SYNTHESIS OF 5-AMINOLEVULINATE CC REQUIRES BOTH HEMA AND HEML PROTEINS; HEMA PROTEIN MAY BE AN ALA CC SYNTHASE WHOSE ACTION OR SYNTHESIS IS FACILITATED BY HEML PROTEIN. CC HOWEVER, THE MECHANISM OF ALA SYNTHESIS IN ENTERIC BACTERIA IS NOT CC YET KNOWN. CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; X82071; G575674; -. DR PROSITE; PS00747; GLUTR. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP. SQ SEQUENCE 388 AA; 42492 MW; B19A26A2 CRC32; >HEM1_PSEAE MCRLTTSREAAILSTCNRSELYLEVDHPTADDVLAWLADYHRLTLDELRACAYVHQDEDA VRHMMRVASGLDSMVLGEPQILGQMKSAYAVAREAGTVGPLLGRLFQATFSTAKTVRTET DIGENPVSVAFAAVSLAKQIFSDLHRSQALLIGAGETITLVARHLFEQGVKRIVVANRTL ERASLLAEQFGAHAVLLSEIPEELANSDIVISSTASQLPILGKGAVERALKQRKHKPMFM VDIAVPRDIEPEVGELDDVYLYSVDDLHEVVAENLKSRQAAAQAAEELVGSGVAEFMQRL RELAAVDVVRAYRQQAERLRDEELGKAQRQLANGADPAEVMAQLARGLTNKLLHAPSVQM KKMSAEGRIDALALAQELFALDECAPRH SWISSPROT:HEM1_MYCTU ID HEM1_MYCTU STANDARD; PRT; 468 AA. AC Q11139; DT 01-OCT-1996 (REL. 34, CREATED) DT 01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA OR MTCY20G9.36. OS MYCOBACTERIUM TUBERCULOSIS. OC PROKARYOTA; FIRMICUTES; ACTINOMYCETALES; MYCOBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=H37RV; RA MURPHY L., HARRIS D., BARRELL B.G., RAJANDREAM M.A., WALSH S.V.; RL SUBMITTED (JUL-1996) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; Z77162; E255158; -. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP. SQ SEQUENCE 468 AA; 49361 MW; ED6291F5 CRC32; >HEM1_MYCTU MSVLLFGVSHRSAPVVVLEQLSIDESDQVKIIDRVLASPLVTEAMVLSTCNRVEVYAVVD AFHGGLSVIGQVLAEHSGMSMGELTKYAYVRYSEAAVEHLFAVASGLDSAVIGEQQVLGQ VRRAYAVAESNRTVGRVLHELAQRALSVGKRVHSETAIDAAGASVVSVALGMAERKLGSL AGTTAVVIGAGAMGALSAVHLTRAGVGHIQVLNRSLSRAQRLARRIRESGVPAEALALDR LANVLADADVVVSCTGAVRPVVSLADVHHALAAARRDEATRPLVICDLGMPRDVDPAVAR LPCVWVVDVDSVQHEPSAHAAAADVEAARHIVAAEVASYLVGQRMAEVTPTVTALRQRAA EVVEAELLRLDNRLPGLQSVQREEVARTVRRVVDKLLHAPTVRIKQLASAPGGDSYAEAL RELFELDQTAVDAVATAGELPVVPSGFDAESRRGGGDMQSSPKRSPSN SWISSPROT:HEM1_MYCLE ID HEM1_MYCLE STANDARD; PRT; 467 AA. AC P46724; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA OR B2168_C3_261. OS MYCOBACTERIUM LEPRAE. OC PROKARYOTA; FIRMICUTES; ACTINOMYCETALES; MYCOBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RA SMITH D.R., ROBISON K.; RL SUBMITTED (MAR-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; U00018; G467059; -. DR PROSITE; PS00747; GLUTR. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP. SQ SEQUENCE 467 AA; 49483 MW; 0C88BAA6 CRC32; >HEM1_MYCLE MSILLFGVSHRSAPVSVLEQLSLDRSDQIKIVDRVLQSPLVTEAMVLSTCNRVEVYAVVE AFHAGLSVIGQVLSEYSAMSIGDLTKYAYVRYSEAAVEHLFTVASGLDSAVVGEQQVLGQ VRRAYAAAEANRTVGQVLHEVAQRALSVGKRVHSETAIDAAGVSVVSVALGIAGRTLGGL AGRIAVVIGAGAMGALSSSYLTQANVGRIHVLNRSLSRARRLAGKIGESGVPADVWTLNH LDEALADADLVVSCTGAVSPVVSLADVHHALAAMRRDETTRPLVICDLGMPRDVDPAVAK LPGVWVVDVEGVQREPSARASAADVDAARRIVAAEVATYLTRQRMAEVAPTVTALRQRAA DVVEAELLRLDHRLPGLESAQREEVARTVRRVVDKLLHAPTVRIKQLASAPGGDSYTEAL RELFELDQTAVDAVATAGELPVMVSGFSDTTRYGTSPAQSSSKYHAE SWISSPROT:HEM1_METTH ID HEM1_METTH STANDARD; PRT; 398 AA. AC P42809; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA. OS METHANOBACTERIUM THERMOAUTOTROPHICUM. OC ARCHAEBACTERIA; EURYARCHAEOTA; METHANOBACTERIALES; OC METHANOBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=MARBURG; RA HUNGERER C., WEISS D., THAUER R.K., JAHN D.; RL SUBMITTED (JAN-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; X83691; G809718; -. DR PROSITE; PS00747; GLUTR. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP. SQ SEQUENCE 398 AA; 44536 MW; 96EE317E CRC32; >HEM1_METTH MILNIRLDHKTSDVKTMETASGRIEEIVGELEALGAVTEKVPLMTCNRVEYYLHVTGVPP EFDFNGFTVEKDEDALLHLLRLASGLESMIIGEDQILGQIKAARLQALREGTCGPLLDMV FTKAVHVGQTVRRKTKINRGSVSIGSAAVDLAESIHGDLKCKKVLVIGAGKMGTLVARAL AEKHLKAIMVANRTYERAYQLACELGGDAIHFDRLNRALRDADVVISATGSPHYILTRER VMDAVPPERRSSIVMVDIANPRDIEESVRELGVRLFTIDDLRGVAEENRKRREAEAREAE GIVRAELELLLRAMKHREVEPLLAEIRGRMESLRQREAGKAIKKIENSKDPERVVEGLTR SIVDKIFHDIALKIRDAAERDDREFLRMCSELFDCDES SWISSPROT:HEM1_ECOLI ID HEM1_ECOLI STANDARD; PRT; 418 AA. AC P13580; DT 01-JAN-1990 (REL. 13, CREATED) DT 01-JAN-1990 (REL. 13, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 89359103. RA VERKAMP E., CHELM B.K.; RL J. BACTERIOL. 171:4728-4735(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 90060810. RA LI J.-M., RUSSELL C.S., COSLOY S.D.; RL GENE 82:209-217(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 89313673. RA DROLET M., PELOQUIN L., ECHELARD Y., COUSINEAU L., SASARMAN A.; RL MOL. GEN. GENET. 216:347-352(1989). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 95362678. RA STROHMAIER H., REMLER P., RENNER W., HOEGENAUER G.; RL J. BACTERIOL. 177:4488-4500(1995). RN [5] RP SEQUENCE OF 1-48 FROM N.A. RX MEDLINE; 93051347. RA IKEMI M., MURAKAMI K., HASHIMOTO M., MUROOKA Y.; RL GENE 121:127-132(1992). RN [6] RP FUNCTION. RX MEDLINE; 92235044. RA VERKAMP E., JAHN M., JAHN D., KUMAR A.M., SOELL D.; RL J. BIOL. CHEM. 267:8275-8280(1992). CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. CC -!- CAUTION: REF.3 SEQUENCE DIFFERS FROM THAT SHOWN IN POSITIONS 151 CC TO 172 DUE TO FRAMESHIFTS. DR EMBL; M25323; G146333; -. DR EMBL; M30785; G146330; -. DR EMBL; D10264; G216523; -. DR EMBL; U18555; G968929; -. DR PIR; S04414; BVECHA. DR PIR; A45918; A45918. DR ECOGENE; EG10427; HEMA. DR PROSITE; PS00747; GLUTR. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP. FT CONFLICT 243 243 A -> R (IN REF. 2 AND 4). FT CONFLICT 365 365 A -> R (IN REF. 3). SQ SEQUENCE 418 AA; 46306 MW; 5F338C6F CRC32; >HEM1_ECOLI MTLLALGINHKTAPVSLRERVSFSPDKLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVE EQDNLQEALIRWLCDYHNLNEEDLRKSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQ VKKAFADSQKGHMKASELERMFQKSFSVAKRVRTETDIGASAVSVAFAACTLARQIFESL STVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQILADEVGAEVIALSDIDERL READIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSV DDLQSIISHNLAQRKAAAVEAETIVAQETSEFMAWLRAQSASETIREYRSQAEQVRDELT AKALAALEQGGDAQAIMQDLAWKLTNRLIHAPTKSLQQAARDGDNERLNILRDSLGLE SWISSPROT:HEM1_CYAPA ID HEM1_CYAPA STANDARD; PRT; 432 AA. AC P48077; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA. OS CYANOPHORA PARADOXA. OG CYANELLE. OC EUKARYOTA; PLANTA; PHYCOPHYTA; GLAUCOPHYTA. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=LB555 / PRINGSHEIM; RA STIREWALT V.L., MICHALOWSKI C.B., LUFFELHARDT W., BOHNERT H.J., RA BRYANT D.A.; RL SUBMITTED (JUL-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; U30821; G1016107; -. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP; CYANELLE. SQ SEQUENCE 432 AA; 48542 MW; 7EE1557C CRC32; >HEM1_CYAPA MNIIVVGLSHKTAPVDFREKLSIPKVRIGEAIRELCNYPHIEEVAILSTCNRLEIYLLTS DTYQGIREATQFLADSSDLSLPELRQHLFILLHQDAVMHLMRVTAGLDSLIIGEGQILSQ VKQCYQLGQQYQGIGPVLNNIFKQAISAGKRVRTETQISTGAVSISSAAVELAQIKKQDL RTANITILGAGKMSRLLVQHLLSKRVKDINIVNRSVERAKLLVDQFKEANINIYNLSELK TILQNSDIVFTGTSSQEPIITPELINDCDNLPSELMLFDIAVPRNVDPNVSQFDNIKVFN VDDLKVVVSQNQQTRRKMAKAAEILLEEELSAFNIWWGSLEAIPTINKLREKAEIIRVKE LEKAISRLGNEFVSDHQEIVESLTRGIVNKILHDPMVQLRAQQDIEIRGRALKILQTLFN LDTIKNGMSPTL SWISSPROT:HEM1_CUCSA ID HEM1_CUCSA STANDARD; PRT; 542 AA. AC P49295; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE PRECURSOR (EC 1.2.1.-) (GLUTR). GN HEMA2. OS CUCUMIS SATIVUS (CUCUMBER). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; OC VIOLALES; CUCURBITACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. AONAGAJIBAI; TISSUE=COTYLEDON; RA TANAKA R., YOSHIDA K., NAKAYASHIKI T., MASUDA T., TSUJI H., RA INOKUCHI H., TANAKA A.; RL SUBMITTED (OCT-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SUBCELLULAR LOCATION: CHLOROPLAST (BY SIMILARITY). CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; D67088; G1015319; -. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP; TRANSIT PEPTIDE; KW CHLOROPLAST. FT TRANSIT 1 ? CHLOROPLAST (POTENTIAL). FT CHAIN ? 542 GLUTAMYL-TRNA REDUCTASE. SQ SEQUENCE 542 AA; 59707 MW; BCC6136F CRC32; >HEM1_CUCSA MAAAVGGLTTCFARPTPEFIAPSTSYSAPVRVFFKPFKVRDLCCAGEVVGVLSARSIPIS PRFELIRLVRMQPGLSALELLKTSSVNRYTKERISIVVIGLNVHTAPVELREKLAIPEAQ WPPGIGELCALNHIEEAAVLSTCNRIEIYVVALSQHRGVKEVTEWMSKRSGIPISELCKH RVLLYNTDATQHLFEVSAGLDSLVLGEGQILAQVKHVVKTGQGVAGFDRKISGLFKHAIT VGKRVRTETNISSGSFSVSSAAVELAQKKLPESSYATAKVMVVGAGKMGKLVIKHLVAKG CRKMVVVNRTQDSVDAVEELKDVEIIYKPLSKILACASEADVIFTCTASKTPLFTKEHVA MLPPAGTETGRRLFVDISVPRNVEQRVSDLETVSVFNVDDLKEVVAANKEDRLKKVQEAQ SIIGEEINKFEAWRDSLETVPTIKKFRAYVERIRAAELDKCLSKMGEDIPKKKKVAINDL SLGIANKLLHGPIQHLRCDGNDSRTLDEILQNMHAINRMFDLETDLSVLEEKIRAKVERG QK SWISSPROT:HEM1_COXBU ID HEM1_COXBU STANDARD; PRT; 413 AA. AC P47846; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA. OS COXIELLA BURNETII. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; RICKETTSIAS; RICKETTSIALES; OC RICKETTSIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NINE MILE PHASE I; RA WILLEMS H., THIELE D., OSWALD W., KRAUSS H.; RL SUBMITTED (APR-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; X78969; G623027; -. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 413 AA; 46586 MW; E588A989 CRC32; >HEM1_COXBU MPLLVCGINHQSAPLTVREKLVFTPERTPLALQSLLAEKAVNEALLLSTCNRTEIYTTVD EAATILRWLSKQPQLSGIDLRSFCYARRDIEMVRHVMRVGSGLDSMVLGEPQILGQMKQA YLLARRIGAVGSELGRLFPAVFAATKRIRSETAIGANPVSIAYAVVQLAKRIFSHLNQCQ ILLIGAGETIELVFSHLYNQGARHFFIANRTLTRAKQIAEPYHAQAIRLSDIPTYLPKVD IVISATMSQLPLVGKGAVESALRQRKRRPLFMADLALPRDIEPETAQLEDVYLYNIDDLQ TLIAQNRQTREAAAKQAEAMVEMQAIHYMRQLQVHKAGDTIRRFRERVEMLRDQELEKAL AHFQRTNDPKAVIAHFAHNLTNKILHQPTTKLRQAAYEDQVQLLLSAKELFDL SWISSPROT:HEM1_CHLVI ID HEM1_CHLVI STANDARD; PRT; 415 AA. AC P28462; DT 01-DEC-1992 (REL. 24, CREATED) DT 01-DEC-1992 (REL. 24, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA. OS CHLOROBIUM VIBRIOFORME. OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; GREEN BACTERIA; OC CHLOROBIACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 92171712. RA MAJUMDAR D., AVISSAR Y.J., WYCHE J.H., BEALE S.I.; RL ARCH. MICROBIOL. 156:281-289(1991). CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC INVOLVED IN CHLOROPHYLL BIOSYNTHESIS. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; M59194; G144475; -. DR EMBL; M96364; G144478; -. DR PIR; S27546; S27546. DR PIR; A48359; A48359. DR PROSITE; PS00747; GLUTR. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 415 AA; 46226 MW; 8900F5C7 CRC32; >HEM1_CHLVI MNIISVGVNHKTAPIEIRERIALSEVQNKEFVTDLVSSGLASEAMVVSTCNRTELYVVPG MPEVNCDYLKDYIISYKDARNAVRPEHFFNRFYCGTARHLFEVSSAIDSLVLGEGQILGQ VKDAYRIAAEVGTAGILLTRLCHSPFSVAKKVKTRTKLMEGAVSVSYAAVELAQKIFSNL SMKKVLLIGAVKQSWQQSTCTPRTPGTSSSPTGRNPRPRACEELGTNRVLPYESYKEHLH EFDIIITAVSTKEYILNAAEMQQSMAKRRLKPVIILDLGLPRNVDPEVGALQNMFLKDID ALKHIIDKNLERRRAELPKVKSIIDEELIASASGSTPSRYVRPSLTCNPSSSKSRRKNSS VPPQGERRGVEAHGTPDRQDPEKNPASSYQDAQGSGRYRRQHPQQSQPRQEHLRS SWISSPROT:HEM1_BACSU ID HEM1_BACSU STANDARD; PRT; 455 AA. AC P16618; DT 01-AUG-1990 (REL. 15, CREATED) DT 01-AUG-1990 (REL. 15, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA. OS BACILLUS SUBTILIS. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 90236876. RA PETRICEK M., RUTBERG L., SCHROEDER I., HEDERSTEDT L.; RL J. BACTERIOL. 172:2250-2258(1990). CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; M32130; -; NOT_ANNOTATED_CDS. DR EMBL; M57676; G143035; -. DR PIR; A35252; A35252. DR SUBTILIST; BG10340; HEMA. DR PROSITE; PS00747; GLUTR. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP. FT MUTAGEN 105 105 C->Y: LOSS OF ACTIVITY. SQ SEQUENCE 455 AA; 50843 MW; D8AB2769 CRC32; >HEM1_BACSU MHILVVGVDYKSAPIEIREKVSFQPNELAEAMVQLKEEKSILENIIVSTCNRTEIYAVVD QLHTGRYYIKKFLADWFQLSKEELSPFLTFYESDAAVEHLFRVACGLDSMVIGETQILGQ VRDSFKTAQQEKTIGTIFNELFKQAVTVGKRTHAETDIGSNAVSVSYAAVELAKKIFGNL SSKHILILGAGKMGELAAENLHGQGIGKVTVINRTYLKAKELADRFSGEARSLNQLESAL AEADILISSTGASEFVVSKEMMENANKLRKGRPLFMVDIAVPRDLDPALNDLEGVFLYDI DDLEGIVEANMKERRETAEKVELLIEETIVEFKQWMNTLGVVPVISALREKALAIQSETM DSIERKLPHLSTREKKLLNKHTKSIINQMLRDPILKVKELAADADSEEKLALFMQIFDIE EAAGRQMMKTVESSQKVHSFKKAESKAGFSPLVSE SWISSPROT:HEM1_ARATH ID HEM1_ARATH STANDARD; PRT; 543 AA. AC P42804; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE 1 PRECURSOR (EC 1.2.1.-) (GLUTR). GN HEMA1 OR HEMA. OS ARABIDOPSIS THALIANA (MOUSE-EAR CRESS). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; OC CAPPARALES; CRUCIFERAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; TISSUE=LEAF; RX MEDLINE; 94198598. RA ILAG L.L., KUMAR A.M., SOELL D.; RL PLANT CELL 6:265-275(1994). CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = GLUTAMATE-1- CC SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SUBCELLULAR LOCATION: CHLOROPLAST. CC -!- TISSUE SPECIFICITY: PRESENT IN ALL TISSUES TESTED. SLIGHTLY MORE CC ABUNDANT IN LEAVES. CC -!- INDUCTION: BY LIGHT. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; U03774; G454359; -. DR PROSITE; PS00747; GLUTR. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP; TRANSIT PEPTIDE; KW CHLOROPLAST; MULTIGENE FAMILY. FT TRANSIT 1 ? CHLOROPLAST (POTENTIAL). FT CHAIN ? 474 GLUTAMYL-TRNA REDUCTASE 1. FT DOMAIN 23 33 POLY-SER. FT DOMAIN 305 308 POLY-VAL. SQ SEQUENCE 543 AA; 59465 MW; E11D2672 CRC32; >HEM1_ARATH MAVSSAFVGCPKLETLLNHHNLSPSSSSSSSVSQTPLGLNGVRVLPKNNRTRRGLIQKAR CVLSASSDSASNAASISALEQLKNSAADRYTKERSSIVVIGLSIHTAPVEMREKLAIPEA EWPRAIAELCGLNHIEEAAVLSTCNRMEIYVLALSQHRGVKEVTEWMSNTSGIPVSEICQ HRFLLYNKDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVNGFGRNISGLFKHAI TVGKRVRTETNIASGAVSVSSAAVELALMKLPQSSNVSARMCVIGAGKMGLLVIKHLMAK GCTKVVVVNRSEERVSAIREEMPGIEIIYRPLDEMLACASEADVVFTSTASETPLFLKEH VENLPQASPEVGGLRHFVDISVPRNVGSCVGEVETARVYNVDDLKEVVAANKEDRMRKAM EAQTIITEESTQFEAWRDSLETVPTIKKLRAYAERIRVAELEKCMSKMGDDINKKTTRAV DDLSRGIVNRFLHGPMQHLRCDGSDSRTLSETLENMHALNRMYGLEKDILEEKLKAMAEQ QHK TREMBL:Q60172 ID Q60172 PRELIMINARY; PRT; 392 AA. AC Q60172; DT 01-NOV-1996 (TREMBLREL. 01, CREATED) DT 01-NOV-1996 (TREMBLREL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1996 (TREMBLREL. 01, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN MJ0143. OS METHANOCOCCUS JANNASCHII. OC ARCHAEBACTERIA; EURYARCHAEOTA; METHANOCOCCALES; METHANOCOCCACEAE. RN [1] RP SEQUENCE FROM N.A. RA BULT C.J., WHITE O., OLSEN G.J., ZHOU L., FLEISCHMANN R.D., RA SUTTON G.G., BLAKE J.A., FITZGERALD L.M., CLAYTON R.A., GOCAYNE J.D., RA KERLAVAGE A.R., DOUGHERTY B.A., TOMB J.F., ADAMS M.D., REICH C.I., RA OVERBEEK R., KIRKNESS E.F., WEINSTOCK K.G., MERRICK J.M., GLODEK A., RA SCOTT J.L., GEOGHAGEN N.S.M., WEIDMAN J.F., FUHRMANN J.L., RA PRESLEY E.A., NGUYEN D., UTTERBACK T.R., KELLEY J.M., PETERSON J.D., RA SADOW P.W., HANNA M.C., COTTON M.D., HURST M.A., ROBERTS K.M., RA KAINE B.P., BORODOVSKY M., KLENK H.P., FRASER C.M., SMITH H.O., RA WOESE C.R., VENTER J.C.; RL SCIENCE 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = CC GLUTAMATE-1- SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; U67471; G1590905; -. DR PROSITE; PS00747; GLUTR. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP. SQ SEQUENCE 392 AA; 44846 MW; 8490E83E CRC32; >Q60172 MIILKADYKKYNVSELEKLRMDEEKFYETFDNAILLQTCNRVEIIFDADSLEEIKGIENI DLEKFDILFGDKAIEHLFRVACGLESMIVGEDQILGQLKNAYLKAKEKGRISKKLEKIIL KAIHTGQRARVETKINEGGVSIGSAAVELAEKIFGLEGKNVLLIGAGEMANLVIKALKEK NIKAIIVANRTYEKAEKLAKELGGMAIKFDKLEEALRYADIVISATGAPHPILNKERLKN AGKTIIIDIANPRDTTDDIRELPDIFLFTIDDLRLVAEENLKKRKEEIPKVEMIICEELE RLKEFLDKMRFETAIKELGQYIENVRKKEVEKAKKILKNKNKPVEEVLEDFSKALCKRII YDIIKIFENVEDKEVFECLAKEFKKLGNKNKN TREMBL:Q59405 ID Q59405 PRELIMINARY; PRT; 418 AA. AC Q59405; DT 01-NOV-1996 (TREMBLREL. 01, CREATED) DT 01-NOV-1996 (TREMBLREL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1996 (TREMBLREL. 01, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 89313673. RA DROLET M., PELOQUIN L., ECHELARD Y., COUSINEAU L., SASARMAN A.; RL MOL. GEN. GENET. 216:347-352(1989). CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = CC GLUTAMATE-1- SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; X17434; G41660; -. DR PROSITE; PS00747; GLUTR. KW TRANSFERASE; ACYLTRANSFERASE; PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; KW NADP. SQ SEQUENCE 418 AA; 46456 MW; F1AFAE2E CRC32; >Q59405 MTLLALGINHKTAPVSLRERVSFSPDKLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVE EQDNLQEALIRWLCDYHNLNEEDLRKSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQ VKKAFADSQKGHMKASELERMFQKSFSVAKPFALKQISVPALCLSLLPACTVARQIFESL STVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQILADEVGAEVIALSDIDERM READIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSV DDLQSIISHNLAQRKAAAVEAETIVAQETSEFMAWLRAQSASETIREYRSQAEQVRDELT AKALRALEQGGDAQAIMQDLAWKLTNRLIHAPTKSLQQAARDGDNERLNILRDSLGLE TREMBL:Q42844 ID Q42844 PRELIMINARY; PRT; 528 AA. AC Q42844; DT 01-NOV-1996 (TREMBLREL. 01, CREATED) DT 01-NOV-1996 (TREMBLREL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1996 (TREMBLREL. 01, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE PRECURSOR (EC 1.2.1.-) (GLUTR). GN HEMA 1. OS HORDEUM VULGARE (BARLEY). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE; OC CYPERALES; GRAMINEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. KLAGES; RA BOUGRI O., GRIMM B.; RL SUBMITTED (OCT-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = CC GLUTAMATE-1- SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; X86101; G1039332; -. DR PROSITE; PS00747; GLUTR. KW TRANSIT PEPTIDE; PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP. FT TRANSIT 1 44 FT CHAIN 45 528 SQ SEQUENCE 528 AA; 57783 MW; A668D581 CRC32; >Q42844 MMAGATSATAAAGAFAAAKARGPAAACPWLVAAGGRRRSGVVRCDAGGDAQAASKAASIT ALEQFKISADRYMKEKSSIAVIGLSVHTAPVEMREKLAVAEELWPRAISELTSLNHIEEA AVLSTCNRMEIYVVALSWNRGIREVVDWMSKKSGIPASELREHLFMLRDSDATRHLFEVS AGLDSLVLGEGQILAQVKQVVRNGQNSGGLGKNIDRMFKDAITAGKRVRCETNISAGAVS VSSAAVELAMMKLPKSECLSARMLLIGAGKMGKLVVKHLIAKGCKKVVVVNRSVERVDAI REEMKDIEIVYRPLTEMYEAAADADVVFTSTASESLLFTKEHAEVLPPISLAMGGVRLFV DISVPRNVGACLSEVEHARVYNVDDLKEVVEANKEDRVRKAMEAQTIITQELKRFEAWRD SLETVPTIKKLRSYADRIRASELEKCLQKIGEDNLNKKMRRSIEELSTGIVNKLLHGPLQ HLRCDGSDSRTLDETLENMHALNRMFSLDTEKAVLEQKIKAKVEKTQS TREMBL:Q42843 ID Q42843 PRELIMINARY; PRT; 527 AA. AC Q42843; DT 01-NOV-1996 (TREMBLREL. 01, CREATED) DT 01-NOV-1996 (TREMBLREL. 01, LAST SEQUENCE UPDATE) DT 01-NOV-1996 (TREMBLREL. 01, LAST ANNOTATION UPDATE) DE GLUTAMYL-TRNA REDUCTASE (EC 1.2.1.-) (GLUTR). GN HEMA1. OS HORDEUM VULGARE (BARLEY). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE; OC CYPERALES; GRAMINEAE. RN [1] RP SEQUENCE FROM N.A. RA BOUGRI O.; RL SUBMITTED (OCT-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: GLUTAMYL-TRNA(GLU) + NADPH = CC GLUTAMATE-1- SEMIALDEHYDE + NADP(+) + TRNA(GLU). CC -!- PATHWAY: FIRST STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- SIMILARITY: TO ALL OTHER KNOWN GLUTAMYL-TRNA REDUCTASES. DR EMBL; X92403; G1041425; -. DR PROSITE; PS00747; GLUTR. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; NADP. FT CHAIN 48 527 POTENTIAL. SQ SEQUENCE 527 AA; 57652 MW; AB786196 CRC32; >Q42843 MAGATSATAAAGAFAAAKARGPAAACPWLVAAGGRRRSGVVRCDAGGDAQAASKAASITA LEQFKISADRYMKEKSSIAVIGLSVHTAPVEMREKLAVAEELWPRAISELTSLNHIEEAA VLSTCNRMEIYVVALSWNRGIREVVDWMSKKSGIPASELREHLFMLRDSDATRHLFEVSA GLDSLVLGEGQILAQVKQVVRNGQNSGGLGKNIDRMFKDAITAGKRVRCETNISAGAVSV SSAAVELAMMKLPKSECLSARMLLIGAGKMGKLVVKHLIAKGCKKVVVVNRSVERVDAIR EEMKDIEIVYRPLTEMYEAAADADVVFTSTASESLLFTKEHAEVLPPISLAMGGVRLFVD ISVPRNVGACLSEVEHARVYNVDDLKEVVEANKEDRVRKAMEAQTIITQELKRFEAWRDS LETVPTIKKLRSYADRIRASELEKCLQKIGEDNLNKKMRRSIEELSTGIVNKLLHGPLQH LRCDGSDSRTLDETLENMHALNRMFSLDTEKAVLEQKIKAKVEKTQS VALUE="TREMBLNEW:ECD757_1" CHECKED >TREMBLNEW:ECD757_1 ID ECD757_1 standard; PRT; 30 AA. AC D90757; DR EMBL; D90757; ECD757. DE gene: "hemA"; product: "Glutamyl-tRNA reductase"; DE Escherichia coli genomic DNA (27.2-27.6 min). OS Escherichia coli OC Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OG Chloroplast FT CDS <1..>94 FT /gene="hemA" FT /codon_start=2 FT /product="Glutamyl-tRNA reductase" FT /transl_table=11 FT /db_xref="PID:g1651608" FT /translation="IHAPTKSLQQAARDGDNERLNILRDSLGLE" SQ Sequence 30 BP; >ECD757_1 IHAPTKSLQQAARDGDNERLNILRDSLGLE TREMBLNEW:ECD756_4 ID ECD756_4 standard; PRT; 418 AA. AC D90756; DR EMBL; D90756; ECD756. DE gene: "hemA"; product: "Glutamyl-tRNA reductase"; DE Escherichia coli genomic DNA.(27.0 -27.4 min). OS Escherichia coli OC Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OG Chloroplast FT CDS 7976..9232 FT /gene="hemA" FT /codon_start=1 FT /product="Glutamyl-tRNA reductase" FT /transl_table=11 FT /db_xref="PID:g1651600" FT /translation="MTLLALGINHKTAPVSLRERVSFSPDKLDQALDSLLAQPMVQGGV FT VLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNLNEEDLRKSLYWHQDNDAVSHLMRVA FT SGLDSLVLGEPQILGQVKKAFADSQKGHMKASELERMFQKSFSVAKRVRTETDIGASAV FT SVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQIL FT ADEVGAEVIALSDIDERLREADIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAV FT PRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRKAAAVEAETIVAQETSEFMAWLRAQS FT ASETIREYRSQAEQVRDELTAKALAALEQGGDAQAIMQDLAWKLTNRLIHAPTKSLQQA FT ARDGDNERLNILRDSLGLE" SQ Sequence 418 BP; >ECD756_4 MTLLALGINHKTAPVSLRERVSFSPDKLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVE EQDNLQEALIRWLCDYHNLNEEDLRKSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQ VKKAFADSQKGHMKASELERMFQKSFSVAKRVRTETDIGASAVSVAFAACTLARQIFESL STVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQILADEVGAEVIALSDIDERL READIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSV DDLQSIISHNLAQRKAAAVEAETIVAQETSEFMAWLRAQSASETIREYRSQAEQVRDELT AKALAALEQGGDAQAIMQDLAWKLTNRLIHAPTKSLQQAARDGDNERLNILRDSLGLE TREMBLNEW:CSHEMA2_1 ID CSHEMA2_1 standard; PRT; 542 AA. AC D67088; DR EMBL; D67088; CSHEMA2. DE gene: "hemA2"; product: "glutamyl-tRNA reductase"; DE Cucumber mRNA for glutamyl-tRNA reductase, isozyme 2 complete cds. OS Cucumis sativus (cucumber) OC Eukaryotae; mitochondrial eukaryotes; Viridiplantae; OC Charophyta/Embryophyta group; Embryophyta; Magnoliophyta; OC Magnoliopsida; Violales; Cucurbitaceae; Cucumis. OG Mitochondrion FT CDS 91..1719 FT /gene="hemA2" FT /codon_start=1 FT /product="glutamyl-tRNA reductase" FT /db_xref="PID:g1015319" FT /db_xref="SWISS-PROT:P49295" FT /translation="MAAAVGGLTTCFARPTPEFIAPSTSYSAPVRVFFKPFKVRDLCCA FT GEVVGVLSARSIPISPRFELIRLVRMQPGLSALELLKTSSVNRYTKERISIVVIGLNVH FT TAPVELREKLAIPEAQWPPGIGELCALNHIEEAAVLSTCNRIEIYVVALSQHRGVKEVT FT EWMSKRSGIPISELCKHRVLLYNTDATQHLFEVSAGLDSLVLGEGQILAQVKHVVKTGQ FT GVAGFDRKISGLFKHAITVGKRVRTETNISSGSFSVSSAAVELAQKKLPESSYATAKVM FT VVGAGKMGKLVIKHLVAKGCRKMVVVNRTQDSVDAVEELKDVEIIYKPLSKILACASEA FT DVIFTCTASKTPLFTKEHVAMLPPAGTETGRRLFVDISVPRNVEQRVSDLETVSVFNVD FT DLKEVVAANKEDRLKKVQEAQSIIGEEINKFEAWRDSLETVPTIKKFRAYVERIRAAEL FT DKCLSKMGEDIPKKKKVAINDLSLGIANKLLHGPIQHLRCDGNDSRTLDEILQNMHAIN FT RMFDLETDLSVLEEKIRAKVERGQK" SQ Sequence 542 BP; >CSHEMA2_1 MAAAVGGLTTCFARPTPEFIAPSTSYSAPVRVFFKPFKVRDLCCAGEVVGVLSARSIPIS PRFELIRLVRMQPGLSALELLKTSSVNRYTKERISIVVIGLNVHTAPVELREKLAIPEAQ WPPGIGELCALNHIEEAAVLSTCNRIEIYVVALSQHRGVKEVTEWMSKRSGIPISELCKH RVLLYNTDATQHLFEVSAGLDSLVLGEGQILAQVKHVVKTGQGVAGFDRKISGLFKHAIT VGKRVRTETNISSGSFSVSSAAVELAQKKLPESSYATAKVMVVGAGKMGKLVIKHLVAKG CRKMVVVNRTQDSVDAVEELKDVEIIYKPLSKILACASEADVIFTCTASKTPLFTKEHVA MLPPAGTETGRRLFVDISVPRNVEQRVSDLETVSVFNVDDLKEVVAANKEDRLKKVQEAQ SIIGEEINKFEAWRDSLETVPTIKKFRAYVERIRAAELDKCLSKMGEDIPKKKKVAINDL SLGIANKLLHGPIQHLRCDGNDSRTLDEILQNMHAINRMFDLETDLSVLEEKIRAKVERG QK TREMBLNEW:CSD407_1 ID CSD407_1 standard; PRT; 552 AA. AC D50407; DR EMBL; D50407; CSD407. DE gene: "hemA"; product: "glutamyl-tRNA reductase"; DE Cucumber mRNA for glutamyl-tRNA reductase, isozyme 1 complete cds. OS Cucumis sativus (cucumber) OC Eukaryotae; mitochondrial eukaryotes; Viridiplantae; OC Charophyta/Embryophyta group; Embryophyta; Magnoliophyta; OC Magnoliopsida; Violales; Cucurbitaceae; Cucumis. OG Mitochondrion FT CDS 78..1736 FT /gene="hemA" FT /codon_start=1 FT /product="glutamyl-tRNA reductase" FT /db_xref="PID:g1694926" FT /translation="MAVSTSFSGAKLEALLFKSASNSSSTRNLSSSHLPGFCKSIRTRR FT ILFQRTGVSSFTPFKCELASSDVLVQNDEIDPPKSSNLSALEQLKTSAVDRYTKERSSI FT VVIGLSIHTTPVEMREKLAIPEAEWPRAIGELCGLNHIEEAAVLSTCNRMEIYVVALSQ FT HRGVKEVTEWMSKTSGIPVSEICQHRFLLYNNDATQHIFEVSAGLDSLVLGEGQILAQV FT KQVVKVGQGVAGFGRNISGLFKHAITVGKRVRTETNIAAGAVSVSSAAVELALMKLPEP FT SHATARMLVIGAGKMGKLVIKHLVAKGCTKMVVVNRSEERVTAIREEMKDVEIIYKPLT FT EMLSCTAEADVIFTSTASESLLFTKEQVKDLPPVGHDVGGLRLFIDISVPRNVGACINN FT LEDVRVYNVDDLKEVVAANKEDRLRKAMEAQSIITEESKQFEAWRDSLETVPTIKKLRA FT YAERIRTAELEKCLSKMGDDIPKKTRRAVDDLSRGIVNKLLHGPMQHLRCDGSDSRTLS FT ETLENMHALNRMFSLETEIAVLEQKIRAKVEQNQK" SQ Sequence 552 BP; >CSD407_1 MAVSTSFSGAKLEALLFKSASNSSSTRNLSSSHLPGFCKSIRTRRILFQRTGVSSFTPFK CELASSDVLVQNDEIDPPKSSNLSALEQLKTSAVDRYTKERSSIVVIGLSIHTTPVEMRE KLAIPEAEWPRAIGELCGLNHIEEAAVLSTCNRMEIYVVALSQHRGVKEVTEWMSKTSGI PVSEICQHRFLLYNNDATQHIFEVSAGLDSLVLGEGQILAQVKQVVKVGQGVAGFGRNIS GLFKHAITVGKRVRTETNIAAGAVSVSSAAVELALMKLPEPSHATARMLVIGAGKMGKLV IKHLVAKGCTKMVVVNRSEERVTAIREEMKDVEIIYKPLTEMLSCTAEADVIFTSTASES LLFTKEQVKDLPPVGHDVGGLRLFIDISVPRNVGACINNLEDVRVYNVDDLKEVVAANKE DRLRKAMEAQSIITEESKQFEAWRDSLETVPTIKKLRAYAERIRTAELEKCLSKMGDDIP KKTRRAVDDLSRGIVNKLLHGPMQHLRCDGSDSRTLSETLENMHALNRMFSLETEIAVLE QKIRAKVEQNQK