PIR:B48301 >F1;B48301 glutamate-1-semialdehyde 2,1-aminomutase (EC 5.4.3.8) - barley (fragments) C;Species: Hordeum vulgare (barley) C;Date: 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 31-Dec-1993 C;Accession: B48301 R;Grimm, B.; Bull, A.; Welinder, K.G.; Gough, S.P.; Kannangara, C.G. Carlsberg Res. Commun. 54, 67-79, 1989 A;Title: Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and synechococcus. A;Reference number: A48301 A;Accession: B48301 A;Status: preliminary A;Molecule type: protein A;Residues: 1-42 C;Keywords: intramolecular transferase; isomerase >B48301 AVSIDEKAYTVQKSEEIFNGALXLVXAFTGREKILKFEXXYH PIR:JQ2263 >P1;JQ2263 glutamate 1-semialdehyde aminotransferase (EC 2.6.1.-) precursor - soybean C;Species: Glycine max (soybean) C;Date: 30-Sep-1993 #sequence_revision 20-Aug-1994 #text_change 20-Aug-1994 C;Accession: JQ2263 R;Sangwan, I.; O'Brian, M.R. Plant Physiol. 102, 829-834, 1993 A;Title: Expression of the soybean (Glycine max) glutamate 1-semialdehyde aminotransferase gene in symbiotic root nodules. A;Reference number: JQ2263 A;Accession: JQ2263 A;Molecule type: mRNA A;Residues: 1-466 C;Comment: This enzyme catalyzes delta-aminolevulinic acid synthesis from glutamate 1-semialdehyde for tetrapyrrole formation. C;Keywords: aminotransferase F;1-28/Domain: signal sequence #status predicted F;29-466/Product: glutamate 1-semialdehyde aminotransferase #status predicted >JQ2263 MAVSAITGARLTLGMSLSSSTRSRTVAMAVSIDPKTDNKLTLTKSEEAFAAAKELMPGGV NSPVRAFKSVGGQPIVIDSVKGSRMWDIDGNEYIDYVGSWGPAIIGHADDQVLAALGETM KKGTSFGAPCLLENTLAELVIDAVPSIEMVRFVNSGTEACMGALRLARAYTGREKIIKFE GCYHGHADPFLVKAGSGVATLGLPDSPGVPKAATFETLTAPYNDTEAIEKLFEANKGEIA AVFLEPVVGNAGFIVPKPDFHSFLRKITKENNTLLVFDEVMTGFRLSYGGAQEYFGITPD ITTLGKIIGGGLPVGAYGGRRDIMEKVAPAGPMYQAGTLSGNPLAMTAGIETLQRIKEPG TYEYLDKITGELVEGIIEAGKRAGHAICGGHIRGMFGFFFTEGPVYNFADAKKSDTAKFA RFFWGMLAEGVYLAPSQFEAGFTSLAHTSDDIKKTIAAAEKVFREI PIR:S43788 >P1;S43788 glutamate-1-semialdehyde aminotransferase - Chlamydomonas reinhardtii C;Species: Chlamydomonas reinhardtii C;Date: 10-Dec-1994 #sequence_revision 26-May-1995 #text_change 26-May-1995 C;Accession: S43788 R;Matters, G.L.; Beale, S.I. Plant Mol. Biol. 24, 617-629, 1994 A;Title: Structure and light-regulated expression of the gsa gene encoding the chlorophyll biosynthetic enzyme, glutamate 1-semialdehyde aminotransferase, in Chlamydomonas reinhardtii. A;Reference number: S43787 A;Accession: S43788 A;Status: preliminary; translation not shown A;Molecule type: DNA A;Residues: 1-98 A;Cross-references: EMBL:U03633 C;Genetics: A;Introns: 44/3 >S43788 MQMQLNAKTVQGAFKAQRPRSVRGNVAVRAVAAPPKLVTKRSEEIFKEAQELLPGGVNSP VRAFRSVGGGPIVFDRVKGAYCWDVDGNKYIDYVGSWG PIR:S43787 >P1;S43787 glutamate-1-semialdehyde aminotransferase - Chlamydomonas reinhardtii C;Species: Chlamydomonas reinhardtii C;Date: 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 13-Jan-1995 C;Accession: S43787 R;Matters, G.L.; Beale, S.I. Plant Mol. Biol. 24, 617-629, 1994 A;Title: Structure and light-regulated expression of the gsa gene encoding the chlorophyll biosynthetic enzyme, glutamate 1-semialdehyde aminotransferase, in Chlamydomonas reinhardtii. A;Reference number: S43787 A;Accession: S43787 A;Status: preliminary A;Molecule type: mRNA A;Residues: 1-463 A;Cross-references: EMBL:U03632 >S43787 MQMQLNAKTVQGAFKAQRPRSVRGNVAVRAVAAPPKLVTKRSEEIFKEAQELLPGGVNSP VRAFRSVGGGPIVFDRVKGAYCWDVDGNKYIDYVGSWGPAICGHGNDEVNNALKAQIDKG TSFGAPCELENVLAKMVIDRVPSVEMVRFVSSGTEACLSVLRLMRAYTGREKVLKFTGCY HGHADSFLVKAGSGVITLGLPDSPGVPKSTAAATLTATYNNLDSVRELFAANKGEIAGVI LEPVVGNSGFIVPTKEFLQGLREICTAEGAVLCFDEVMTGFRIAKGCAQEHFGITPDLTT MGKVIGGGMPVGAYGGKKEIMKMVAPAGPMYQAGTLSGNPMAMTAGIKTLEILGRPGAYE HLEKVTKRLIDGIMAAAKEHSHEITGGNISGMFGFFFCKGPVTCFEDALAADTAKFARFH RGMLEEGVYLAPSQFEAGFTSLAHSEADVDATIAAARRVFARI PIR:A48301 >F1;A48301 glutamate-1-semialdehyde 2,1-aminomutase (EC 5.4.3.8) - Synechococcus sp. (PCC 6301) (fragment) C;Species: Synechococcus sp. C;Date: 31-Dec-1993 #sequence_revision 31-Dec-1993 #text_change 31-Dec-1993 C;Accession: A48301 R;Grimm, B.; Bull, A.; Welinder, K.G.; Gough, S.P.; Kannangara, C.G. Carlsberg Res. Commun. 54, 67-79, 1989 A;Title: Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and synechococcus. A;Reference number: A48301 A;Accession: A48301 A;Status: preliminary A;Molecule type: protein A;Residues: 1-16 C;Keywords: intramolecular transferase; isomerase >A48301 VTINPFKTIKSDEIFA PIR:S13326 >P1;S13326 glutamate-1-semialdehyde 2,1-aminomutase (EC 5.4.3.8) - Synechococcus sp. (PCC 6301) N;Alternate names: glutamate 1-semialdehyde aminotransferase C;Species: Synechococcus sp. C;Date: 07-Apr-1994 #sequence_revision 07-Apr-1994 #text_change 07-Apr-1994 C;Accession: S13326; S21022 R;Grimm, B.; Bull, A.; Breu, V. Mol. Gen. Genet. 225, 1-10, 1991 A;Title: Structural genes of glutamate 1-semialdehyde aminotransferase for porphyrin synthesis in a cyanobacterium and Escherichia coli. A;Reference number: S13326; MUID:91155920 A;Accession: S13326 A;Molecule type: DNA A;Residues: 1-433 A;Cross-references: EMBL:X53695 R;Grimm, B. submitted to the EMBL Data Library, July 1990 A;Reference number: S21022 A;Accession: S21022 A;Molecule type: DNA A;Residues: 1-50,'I',52-107,'N',109-132,'VV',135-171,'S',173-178,'K',180-186,'T',188-433 A;Cross-references: EMBL:X53695 C;Keywords: intramolecular transferase; isomerase >S13326 MVTSSPFKTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVDGNRY IDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEMVIDAVPSIEMVRFV NSGTEACMAVLRLMRAYTGRDKIIKFEGCYHGHADMFLVKAGSGVATLGLPDSPGVPKST TANTLTAPYNDLEAVKALFAENPGEIAGVILEPIVGNSGFIVPDAGFLEGLREITLEHDA LLVFDEVMTGFRIAYGGVQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPM YQAGTLSGNPLAMTAGIKTLELLRQPGTYEYLDQITKRLSDGLLAIAQETGHAACGGQVS GMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFEAGFTSLAHTEEDID ATLAAARTVMSAL PIR:A37848 >P1;A37848 hemL protein - Salmonella typhimurium C;Species: Salmonella typhimurium C;Date: 21-Jun-1991 #sequence_revision 21-Jun-1991 #text_change 23-Mar-1993 C;Accession: A37848 R;Elliott, T.; Avissar, Y.J.; Rhie, G.E.; Beale, S.I. J. Bacteriol. 172, 7071-7084, 1990 A;Title: Cloning and sequence of the Salmonella typhimurium hemL gene and identification of the missing enzyme in hemL mutants as glutamate-1-semialdehyde aminotransferase. A;Reference number: A37848; MUID:91072261 A;Accession: A37848 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-426 A;Cross-references: GB:M36054 >A37848 MSKSENLYSAARELIPGGVNSPVRAFTGVGGTPLFIEKADGAYLYDVDGKAYIDYVGSWG PMVLGHNHPAIRNAVIEAAERGLSFGAPTEMEVKMAELVTNLVPTMDMVRMVNSGTEATM SAIRLARGFTGRDKIIKFEGCYHGHADCLLVKAGSGALTLGQPNSPGVPADFAKHTLTCT YNDLTSVRAAFEQYPQEIASIIVEPVAGNMNCVPPLPEFLPGLRALCDEFGALLIIDEVM TGFRVALAGAQDYYGVVPDLTCLGKIIGGGMPVGAFGGRRDVMDALAPTGPVYQAGTLSG NPIAMAAGFACLNEVAQPGIHETLDELTTRLAEGLCEAAQEAGIPLVVNHVGGMFGIFFT DAESVTCYQDVMACDVERFKRFFHLMLEEGVYLAPSAFEAGFMSVAHSMDDINNTIDAAR RVFAKL PIR:S45223 >P1;S45223 glutamate-1-semialdehyde aminotransferase - Escherichia coli C;Species: Escherichia coli C;Date: 20-Feb-1995 #sequence_revision 03-Aug-1995 #text_change 03-Aug-1995 C;Accession: S45223; S13327 R;Fujita, N. submitted to the EMBL Data Library, January 1994 A;Reference number: S45181 A;Accession: S45223 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-426 A;Cross-references: EMBL:D26562 R;Grimm, B.; Bull, A.; Breu, V. Mol. Gen. Genet. 225, 1-10, 1991 A;Title: Structural genes of glutamate 1-semialdehyde aminotransferase for porphyrin synthesis in a cyanobacterium and Escherichia coli. A;Reference number: S13326; MUID:91155920 A;Accession: S13327 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-426 A;Cross-references: EMBL:X53696 >S45223 MRKSENLYQAARELIPGGVNSPVRAFTGVGGTPLFIEKADGAYLYDVDGKAYIDYVGSWG PMVLGHNHPAIRNAVIEAAERGLSFGAPTEMEVKMAQLVTELVPTMDMVRMVNSGTEATM SAIRLARGFTGRDKIIKFEGCYHGHADCLLVKAGSGALTLGQPNSPGVPADFAKYTLTCT YNDLASVRAAFEQYPQEIACIIVEPVAGNMNCVPPLPEFLPGLRALCDEFGALLIIDEVM TGFRVALAGAQDYYGVVPDLTCLGKIIGGGMPVGAFGGRRDVMDALAPTGPVYQAGTLSG NPIAMAAGFACLNEVAQPGVHETLDELTTRLAEGLLEAAEEAGIPLVVNHVGGMFGIFFT DAESVTCYQDVMACDVERFKRFFHMMLDEGVYLAPSAFEAGFMSVAHSMEDINNTIDAAR RVFAKL SWISSPROT:GSA_XANCH ID GSA_XANCH STANDARD; PRT; 429 AA. AC Q06741; DT 01-JUN-1994 (REL. 29, CREATED) DT 01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE (EC 5.4.3.8) (GSA) DE (GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE) (GSA-AT). GN HEML. 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; 93159751. RA MURAKAMI K., KORBSRISATE S., ASAHARA N., HASHIMOTO Y., MUROOKA Y.; RL APPL. MICROBIOL. BIOTECHNOL. 38:502-506(1993). CC -!- CATALYTIC ACTIVITY: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; D12642; G303936; -. DR PIR; A48377; A48377. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3. KW PORPHYRIN BIOSYNTHESIS; ISOMERASE; PYRIDOXAL PHOSPHATE. FT BINDING 267 267 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 429 AA; 45044 MW; B80FA660 CRC32; >GSA_XANCH MNHSRSHALFAQAQTLLPGGVNSPVRAFKSVGGEPFFVARADGPYLFDVDDNRYIDYVGS WGPMIAGHNHPAVREAVEQSIRNGLSFGAPCAAEVTMAQTIARLVPSCEMVRMVNSGTEA TLSAVRLARGATGRNRIIKFEGCYHGHGDSFLVKAGSGMLTLGVPTSPGVPAGLSELTAT LSFNDFEGATALFDEIGAEVAAVIIEPVVGNANCIPPQAGYLQHLRTLCTRHGALLIFDE VMTGFRVALGGAQAHYGVTPDLTTFGKIIGGGMPVGAYGGRRDLMEQVAPAGPIYQAGTL SGNPVAMAAGLAMLELVQEPGFHTRLSEATSMLCEGLEDAARAAGIAVTTNQVGGMFGLF FTDDVVESYAQATACDITSFNRFFHAMLQRGVYLAPSAYEAGFMSSAHDEAVIEATLAAA REAFADVAR SWISSPROT:GSA_TOBAC ID GSA_TOBAC STANDARD; PRT; 478 AA. AC P31593; DT 01-JUL-1993 (REL. 26, CREATED) DT 01-JUL-1993 (REL. 26, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE PRECURSOR (EC 5.4.3.8) (GSA) DE (GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE) (GSA-AT). GN GSA. OS NICOTIANA TABACUM (COMMON TOBACCO). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; OC SOLANALES; SOLANACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. SR1; RX MEDLINE; 94173902. RA HOEFGEN R., AXELSEN K.B., KANNANGARA C.G., SCHUETTKE I., RA POHLENZ H.-D., WILLMITZER L., GRIMM B., VON WETTSTEIN D.; RL PROC. NATL. ACAD. SCI. U.S.A. 91:1726-1730(1994). CC -!- CATALYTIC ACTIVITY: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC INVOLVED IN CHLOROPHYLL BIOSYNTHESIS. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CHLOROPLAST. CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; X65973; G19873; -. DR EMBL; X65974; G19875; -. DR PIR; S21454; S21454. DR PIR; S21455; S21455. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; ISOMERASE; KW PYRIDOXAL PHOSPHATE; TRANSIT PEPTIDE; CHLOROPLAST. FT TRANSIT 1 ? CHLOROPLAST. FT CHAIN ? 478 GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE. FT BINDING 318 318 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT VARIANT 18 18 G -> S (IN ISOZYME 2). FT VARIANT 104 104 E -> D (IN ISOZYME 2). FT VARIANT 221 221 G -> V (IN ISOZYME 2). FT VARIANT 227 227 S -> T (IN ISOZYME 2). FT VARIANT 245 245 E -> K (IN ISOZYME 2). FT VARIANT 270 270 L -> P (IN ISOZYME 2). FT VARIANT 375 375 E -> D (IN ISOZYME 2). FT VARIANT 411 411 L -> F (IN ISOZYME 2). FT VARIANT 413 413 A -> V (IN ISOZYME 2). FT VARIANT 466 466 K -> R (IN ISOZYME 2). SQ SEQUENCE 478 AA; 50877 MW; 973F2270 CRC32; >GSA_TOBAC MAAVNGVGISWPSKLTQGQRPKLVFSPSPRRCTPSSSTIKMTASVDEKKKTFTLQKSEEA FSKAKELMPGGVNSPVRAFKSVGGQPIIIDSVKGSRMRDIDGNEYIDYVGSWGPAIIGHA DDEVLAALAETMKKGTSFGAPCLLENTLAEMVISAVPSIEMVRFVNSGTEACMGVLRLAR AFTGRPKIIKFEGCYHGHADPFLVKAGSGVATLGLPDSPGGPKAATSDTLTAPYNDISAV ESLFEEHKGEVAAIILEPVVGNAGFIQPNLDFLAAIRKITKENDALLIFDEVMTGFRLAY GGAQEYFGITPDLTTLGKIIGGGLPVGAYGGRRDIMEMVAPAGPMYQAGTLSGNPLAMTA GIHTLKRLQGPGTYEYLDKITGELTQGILDAGKKTGHAMCGGYIRGMFGFLFAEGPVNNF SDAKKSDTEKFGRFYRGMLEEGVYFAPSQFEAGFTSLAHTSEDIQKTVAAAEKVLKQI SWISSPROT:GSA_SYNP6 ID GSA_SYNP6 STANDARD; PRT; 432 AA. AC P24630; DT 01-MAR-1992 (REL. 21, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE (EC 5.4.3.8) (GSA) DE (GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE) (GSA-AT). GN GSA. OS SYNECHOCOCCUS SP. (STRAIN PCC 6301). OC PROKARYOTA; GRACILICUTES; OXYPHOTOBACTERIA; OC CYANOBACTERIA (BLUE-GREEN ALGAE); CHROOCOCCALES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 91155920. RA GRIMM B., BULL A., BREU V.; RL MOL. GEN. GENET. 225:1-10(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 91286277. RA GRIMM B., SMITH A.J., KANNANGARA C.G., SMITH M.; RL J. BIOL. CHEM. 266:12495-12501(1991). RN [3] RP PRELIMINARY SEQUENCE OF 1-16. RX MEDLINE; 89374545. RA GRIMM B., BULL A., WELINDER K.G., GOUGH S.P., KANNANGARA C.G.; RL CARLSBERG RES. COMMUN. 54:67-79(1989). CC -!- CATALYTIC ACTIVITY: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC INVOLVED IN CHLOROPHYLL BIOSYNTHESIS. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: MONOMER. CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; X53695; G581789; -. DR PIR; S13326; S13326. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; ISOMERASE; KW PYRIDOXAL PHOSPHATE. FT INIT_MET 0 0 FT BINDING 272 272 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 432 AA; 45918 MW; 7B7486D1 CRC32; >GSA_SYNP6 VTSSPFKTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAIAWDVDGNRYI DYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEMVNDAVPSIEMVRFVN SGTEACMAVLRVVRAYTGRDKIIKFEGCYHGHADMFLVKAGSGVATLGLPSSPGVPKKTT ANTLTTPYNDLEAVKALFAENPGEIAGVILEPIVGNSGFIVPDAGFLEGLREITLEHDAL LVFDEVMTGFRIAYGGVQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPMY QAGTLSGNPLAMTAGIKTLELLRQPGTYEYLDQITKRLSDGLLAIAQETGHAACGGQVSG MFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFEAGFTSLAHTEEDIDA TLAAARTVMSAL SWISSPROT:GSA_SOYBN ID GSA_SOYBN STANDARD; PRT; 466 AA. AC P45621; 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 GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE PRECURSOR (EC 5.4.3.8) (GSA) DE (GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE) (GSA-AT). GN GSA1 OR GSA. OS GLYCINE MAX (SOYBEAN). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; FABALES; OC FABACEAE. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=ROOT NODULES; RX MEDLINE; 94105331. RA SANGWAN I., O'BRIAN M.R.; RL PLANT PHYSIOL. 102:829-834(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. ESSEX; RX MEDLINE; 95221396. RA FRUSTACI J.M., SANGWAN I., O'BRIAN M.R.; RL J. BIOL. CHEM. 270:7387-7393(1995). CC -!- CATALYTIC ACTIVITY: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC INVOLVED IN CHLOROPHYLL BIOSYNTHESIS. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CHLOROPLAST. CC -!- TISSUE SPECIFICITY: STRONGLY EXPRESSED IN LEAVES OF ETIOLATED CC PLANTLETS INDEPENDENTLY OF LIGHT TREATMENT AND, TO A MUCH LESSER CC EXTENT, IN LEAVES OF MATURE PLANTS. CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; L12453; G310567; -. DR EMBL; U20260; G747968; -. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; ISOMERASE; KW PYRIDOXAL PHOSPHATE; TRANSIT PEPTIDE; CHLOROPLAST. FT TRANSIT 1 28 CHLOROPLAST (POTENTIAL). FT CHAIN 29 466 GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE. FT BINDING 306 306 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 466 AA; 49646 MW; 9BD132A9 CRC32; >GSA_SOYBN MAVSAITGARLTLGMSLSSSTRSRTVAMAVSIDPKTDNKLTLTKSEEAFAAAKELMPGGV NSPVRAFKSVGGQPIVIDSVKGSRMWDIDGNEYIDYVGSWGPAIIGHADDQVLAALGETM KKGTSFGAPCLLENTLAELVIDAVPSIEMVRFVNSGTEACMGALRLARAYTGREKIIKFE GCYHGHADPFLVKAGSGVATLGLPDSPGVPKAATFETLTAPYNDTEAIEKLFEANKGEIA AVFLEPVVGNAGFIVPKPDFHSFLRKITKENNTLLVFDEVMTGFRLSYGGAQEYFGITPD ITTLGKIIGGGLPVGAYGGRRDIMEKVAPAGPMYQAGTLSGNPLAMTAGIETLQRIKEPG TYEYLDKITGELVEGIIEAGKRAGHAICGGHIRGMFGFFFTEGPVYNFADAKKSDTAKFA RFFWGMLAEGVYLAPSQFEAGFTSLAHTSDDIKKTIAAAEKVFREI SWISSPROT:GSA_SALTY ID GSA_SALTY STANDARD; PRT; 426 AA. AC P21267; DT 01-MAY-1991 (REL. 18, CREATED) DT 01-MAY-1991 (REL. 18, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE (EC 5.4.3.8) (GSA) DE (GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE) (GSA-AT). GN HEML. OS SALMONELLA TYPHIMURIUM. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=LT2; RX MEDLINE; 91072261. RA ELLIOTT T., AVISSAR Y.J., RHIE G.E., BEALE S.I.; RL J. BACTERIOL. 172:7071-7084(1990). CC -!- CATALYTIC ACTIVITY: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; M60064; G154106; -. DR PIR; A37848; A37848. DR STYGENE; SG10152; HEML. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3. KW PORPHYRIN BIOSYNTHESIS; ISOMERASE; PYRIDOXAL PHOSPHATE. FT BINDING 265 265 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 426 AA; 45325 MW; 4430B4FD CRC32; >GSA_SALTY MSKSENLYSAARELIPGGVNSPVRAFTGVGGTPLFIEKADGAYLYDVDGKAYIDYVGSWG PMVLGHNHPAIRNAVIEAAERGLSFGAPTEMEVKMAELVTNLVPTMDMVRMVNSGTEATM SAIRLARGFTGRDKIIKFEGCYHGHADCLLVKAGSGALTLGQPNSPGVPADFAKHTLTCT YNDLTSVRAAFEQYPQEIASIIVEPVAGNMNCVPPLPEFLPGLRALCDEFGALLIIDEVM TGFRVALAGAQDYYGVVPDLTCLGKIIGGGMPVGAFGGRRDVMDALAPTGPVYQAGTLSG NPIAMAAGFACLNEVAQPGIHETLDELTTRLAEGLCEAAQEAGIPLVVNHVGGMFGIFFT DAESVTCYQDVMACDVERFKRFFHLMLEEGVYLAPSAFEAGFMSVAHSMDDINNTIDAAR RVFAKL SWISSPROT:GSA_PSEAE ID GSA_PSEAE STANDARD; PRT; 427 AA. AC P48247; 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 GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE (EC 5.4.3.8) (GSA) DE (GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE) (GSA-AT). GN HEML. 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; 96004705. RA HUNGERER C., TROUP B., ROMLING U., JAHN D.; RL MOL. GEN. GENET. 248:375-380(1995). CC -!- CATALYTIC ACTIVITY: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; X82072; G557262; -. KW PORPHYRIN BIOSYNTHESIS; ISOMERASE; PYRIDOXAL PHOSPHATE. FT BINDING 265 265 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 427 AA; 45414 MW; 26641A3E CRC32; >GSA_PSEAE MSRSETLFNNAQKHIPGGVNSPVRAFKSVGGTPLFFKHAEGAYVLDEDDKRYVDYVGSWG PMILGHSHPDVLDAVRRQLDHGLSYGAPTALEVEMADLVCSMVPSMEMVRMVSSGTEATM SAIRLARGYTGRDSIIKFEGCYHGHSDSLLVKAGSGSLTFGVPNSPGVPAAFAKHTLTLP FNDIEAVRKTLGEVGKEVACIIVEPVAGNMNCVPPAPGFLEGLREACDEHGVVLIFDEVM TGFRVALGGAQAYYGVTPDLSTFGKIIGGGMPVGAFGGKREIMQQISPLGPVYQAGTLSG NPLAMAAGLTTLRLISRPGFHDELTAYTTRMLDGLQQRADAAGIPFVTTQAGGMFGLYFS GADAIVTFEDVMASDVERFKRFFHLMLDGGVYLAPSAFEAGFTSIAHGDKELEITLNAAE KAFAALK SWISSPROT:GSA_PROFR ID GSA_PROFR STANDARD; PRT; 441 AA. AC Q06774; DT 01-JUN-1994 (REL. 29, CREATED) DT 01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE) DT 01-FEB-1995 (REL. 31, LAST ANNOTATION UPDATE) DE GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE (EC 5.4.3.8) (GSA) DE (GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE) (GSA-AT). GN HEML. OS PROPIONIBACTERIUM FREUDENREICHII SHERMANII. OC PROKARYOTA; FIRMICUTES; IRREGULAR ASPOROGENOUS RODS; OC PROPONIBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=IFO 12424; RX MEDLINE; 93175878. RA MURAKAMI K., HASHIMOTO Y., MUROOKA Y.; RL APPL. ENVIRON. MICROBIOL. 59:347-350(1993). CC -!- CATALYTIC ACTIVITY: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; D12643; G286160; -. DR EMBL; S55475; -; NOT_ANNOTATED_CDS. DR PIR; A48959; A48959. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3. KW PORPHYRIN BIOSYNTHESIS; ISOMERASE; PYRIDOXAL PHOSPHATE. FT BINDING 270 270 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 441 AA; 45932 MW; 5A3DF267 CRC32; >GSA_PROFR MSVSDELFAEALKVMPGGVSSPVRAYRSVGGTPRFVKRALGSHIVDVDDKRYVDLVCSWG PMIAGHAHPEVVAAVLQAVADSTSFGAPSEVELRLAQAVVARMGGAIDKVRFTCSGTEAV MTAARLARGITKRPLLVKFVGCYHGHSDSFLVSAGSGVASLGLPDSPGVPKEVAGDTVAL PYGRIDMVEELFAERGDQVAAIVTEGVPANMGVIVPPEGFNRRLHDIAHAHGALLIQDEV LTGFRLSPTGAWGLQGAKEGWTPDLFTFGKVIGGGMPLAAVGGSAQLMDYLAPEGPVYQA GTLSGNPAACAAGLATLALMDDAAYSRLDATADRVSAMADAALESAGVPHRINKVSNLFS VFLTDAPVTDFASASKQDTKAFSRFFHAALDAGLWLAPSGFEAWFCSTALDDDDLEVIDA GLHKAAQAAAQGLSSLEDVRR SWISSPROT:GSA_MYCLE ID GSA_MYCLE STANDARD; PRT; 446 AA. AC P46716; 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 GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE (EC 5.4.3.8) (GSA) DE (GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE) (GSA-AT). GN HEML OR GSA OR B2168_C1_190. 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: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; U00018; G467041; -. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3. KW PORPHYRIN BIOSYNTHESIS; ISOMERASE; PYRIDOXAL PHOSPHATE. FT BINDING 277 277 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 446 AA; 45790 MW; 38244BFF CRC32; >GSA_MYCLE MGSTDQATAPAGPAVSISAKLFEDACAVIPGGVNSPVRAFSAVGGTPLFITEARGCWLTD ADGRRYVDLVCSWGPMILGHAHPAVVDAVATVAASGLSFGAPTPAETQLAAEIIGRMAPV ERIRLVNSGTEATMSAVRLARGFTGRTKIIKFSGCYHGHVDALLADAGSGVATLSLPSSP GVTGAAAADTIVLPYNDIEAVRQTFARLGDQIAAVITEASPGNMGVVPPAPGYNAALRAI TAEHGALLIIDEVMTGFRVSRSGWYGLDPVAADLFIFGKVMSGGMPAAAFGGRAEVMERL APLGPVYQAGTLSGNPVAMAAGLATLRAAADAVYATLDRNADRLVAMLSEALTDAGVPHQ IPRAGNMFSVFFSEAPVTDFASACNSQVWRYPAFFHALLDAGVYPPCSTFEAWFVSAALD DAAFGRIVDALPGAAAAAVAARHRES SWISSPROT:GSA_HORVU ID GSA_HORVU STANDARD; PRT; 469 AA. AC P18492; DT 01-NOV-1990 (REL. 16, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE PRECURSOR (EC 5.4.3.8) (GSA) DE (GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE) (GSA-AT). GN GSA. OS HORDEUM VULGARE (BARLEY). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE; OC CYPERALES; GRAMINEAE. RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=CV. BONUS; TISSUE=SEEDLING; RX MEDLINE; 90272675. RA GRIMM B.; RL PROC. NATL. ACAD. SCI. U.S.A. 87:4169-4173(1990). RN [2] RP PARTIAL SEQUENCE. RX MEDLINE; 89374545. RA GRIMM B., BULL A., WELINDER K.G., GOUGH S.P., KANNANGARA C.G.; RL CARLSBERG RES. COMMUN. 54:67-79(1989). CC -!- CATALYTIC ACTIVITY: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC INVOLVED IN CHLOROPHYLL BIOSYNTHESIS. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CHLOROPLAST. CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -!- CAUTION: THE RESIDUE IN POSITION 309 IS GLN IN REF.1, BUT IS CC SAID TO BE LYS IN FURTHER PAPERS BY THE SAME GROUP. DR EMBL; M31545; G506383; -. DR PIR; A35789; A35789. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; ISOMERASE; KW PYRIDOXAL PHOSPHATE; TRANSIT PEPTIDE; CHLOROPLAST. FT TRANSIT 1 34 CHLOROPLAST. FT CHAIN 35 469 GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE. FT BINDING 309 309 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT CONFLICT 309 309 K -> Q (IN REF. 1; SEE COMMENT). SQ SEQUENCE 469 AA; 49494 MW; 09BEB290 CRC32; >GSA_HORVU MAGAAAAVASGISIRPVAAPKISRAPRSRSVVRAAVSIDEKAYTVQKSEEIFNAAKELMP GGVNSPVRAFKSVGGQPIVFDSVKGSHMWDVDGNEYIDYVGSWGPAIIGHADDKVNAALI ETLKKGTSFGAPCALENVLAQMVISAVPSIEMVRFVNSGTEACMGALRLVRAFTGREKIL KFEGCYHGHADSFLVKAGSGVATLGLPDSPGVPKGATVGTLTAPYNDADAVKKLFEDNKG EIAAVFLEPVVGNAGFIPPQPAFLNALREVTKQDGALLVFDEVMTGFRLAYGGAQEYFGI TPDVTTLGKIIGGGLPVGAYGGRKDIMEMVAPAGPMYQAGTLSGNPLAMTAGIHTLKRLM EPGTYEYLDKVTGELVRGILDVGAKTGHEMCGGHIRGMFGFFFAGGPVHNFDDAKKSDTA KFGRFHRGMLGEGVYLAPSQFEAGFTSLAHTTQDIEKTVEAAEKVLRWI SWISSPROT:GSA_ECOLI ID GSA_ECOLI STANDARD; PRT; 426 AA. AC P23893; DT 01-NOV-1991 (REL. 20, CREATED) DT 01-NOV-1991 (REL. 20, LAST SEQUENCE UPDATE) DT 01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE (EC 5.4.3.8) (GSA) DE (GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE) (GSA-AT). GN HEML OR GSA OR POPC. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 91155920. RA GRIMM B., BULL A., BREU V.; RL MOL. GEN. GENET. 225:1-10(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12 / W3110; RX MEDLINE; 94261430. RA FUJITA N., MORI H., YURA T., ISHIHAMA A.; RL NUCLEIC ACIDS RES. 22:1637-1639(1994). RN [3] RP CHARACTERIZATION. RX MEDLINE; 91258321. RA ILAG L.L., JAHN D., EGGERTSSON G., SOELL D.; RL J. BACTERIOL. 173:3408-3413(1991). RN [4] RP MUTAGENESIS OF LYS-265. RX MEDLINE; 92353044. RA ILAG L.L., JAHN D.; RL BIOCHEMISTRY 31:7143-7151(1992). CC -!- CATALYTIC ACTIVITY: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER. CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; X53696; G41621; -. DR EMBL; D26562; G473813; -. DR PIR; S13327; S13327. DR PIR; S45223; S45223. DR ECOGENE; EG10432; HEML. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3. KW PORPHYRIN BIOSYNTHESIS; ISOMERASE; PYRIDOXAL PHOSPHATE. FT BINDING 265 265 PYRIDOXAL PHOSPHATE (PROBABLE). FT MUTAGEN 265 265 K->R: 2% OF WILD-TYPE ACTIVITY. SQ SEQUENCE 426 AA; 45476 MW; 374D1A20 CRC32; >GSA_ECOLI MRKSENLYQAARELIPGGVNSPVRAFTGVGGTPLFIEKADGAYLYDVDGKAYIDYVGSWG PMVLGHNHPAIRNAVIEAAERGLSFGAPTEMEVKMAQLVTELVPTMDMVRMVNSGTEATM SAIRLARGFTGRDKIIKFEGCYHGHADCLLVKAGSGALTLGQPNSPGVPADFAKYTLTCT YNDLASVRAAFEQYPQEIACIIVEPVAGNMNCVPPLPEFLPGLRALCDEFGALLIIDEVM TGFRVALAGAQDYYGVVPDLTCLGKIIGGGMPVGAFGGRRDVMDALAPTGPVYQAGTLSG NPIAMAAGFACLNEVAQPGVHETLDELTTRLAEGLLEAAEEAGIPLVVNHVGGMFGIFFT DAESVTCYQDVMACDVERFKRFFHMMLDEGVYLAPSAFEAGFMSVAHSMEDINNTIDAAR RVFAKL SWISSPROT:GSA_BACSU ID GSA_BACSU STANDARD; PRT; 430 AA. AC P30949; DT 01-JUL-1993 (REL. 26, CREATED) DT 01-JUL-1993 (REL. 26, LAST SEQUENCE UPDATE) DT 01-FEB-1995 (REL. 31, LAST ANNOTATION UPDATE) DE GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE (EC 5.4.3.8) (GSA) DE (GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE) (GSA-AT). GN HEML OR HEMK. OS BACILLUS SUBTILIS. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 91193218. RA HANSSON M., RUTBERG L., SCHROEDER I., HEDERSTEDT L.; RL J. BACTERIOL. 173:2590-2599(1991). CC -!- CATALYTIC ACTIVITY: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; M57676; G143040; -. DR PIR; D42728; D42728. DR SUBTILIST; BG10345; HEML. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3. KW PORPHYRIN BIOSYNTHESIS; ISOMERASE; PYRIDOXAL PHOSPHATE. FT BINDING 268 268 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 430 AA; 46449 MW; 9CFF860D CRC32; >GSA_BACSU MRSYEKSKTAFKEAQKLMPGGVNSPVRAFKSVDMDPIFMERGKGSKIFDIDGNEYIDYVL SWGPLILGHTNDRVVESLKKVAEYGTSFGAPTEVENELAKLVIDRVPSVEIVRMVSSGTE ATMSALRLARGYTGRNKILKFEGCYHGHGDSLLIKAGSGVATLGLPDSPGVPEGIAKNTI TVPYNDLESVKLAFQQFGEDIAGVIVEPVAGNMGVVPPQEGFLQGLRDITEQYGSLLIFD EVMTGFRVDYNCAQGYFGVTPDLTCLGKVIGGGLPVGAYGGKAEIMEQIAPSGPIYQAGT LSGNPLAMTAGLETLKQLTPESYKNFIKKGDRLEEGISKTAGAHGIPHTFNRAGSMIGFF FTNEPVINYETAKSSDLKLFASYYKGMANEGVFLPPSQFEGLFLSTAHTDEDIENTIQAA EKVFAEISRR SWISSPROT:GSA_ARATH ID GSA_ARATH STANDARD; PRT; 474 AA. AC P42799; 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 GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE PRECURSOR (EC 5.4.3.8) (GSA) DE (GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE) (GSA-AT). GN GSA1. 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: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC INVOLVED IN CHLOROPHYLL BIOSYNTHESIS. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CHLOROPLAST. CC -!- TISSUE SPECIFICITY: PRESENT IN ALL TISSUES TESTED. CC -!- INDUCTION: BY LIGHT. IN ETIOLATED SEEDLINGS, INITIAL EXPRESSION CC IS REDUCED BUT AFTER FURTHER ILLUMINATION, LEVELS STEADILY CC INCREASE. CC -!- SIMILARITY: BELONGS TO CLASS-III OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; U03773; G454357; -. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; ISOMERASE; KW PYRIDOXAL PHOSPHATE; TRANSIT PEPTIDE; CHLOROPLAST. FT TRANSIT 1 38 CHLOROPLAST (BY SIMILARITY). FT CHAIN 39 474 GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE. FT BINDING 314 314 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 474 AA; 50369 MW; A0FAD05F CRC32; >GSA_ARATH MSATLTGSGTALGFSCSSKISKRVSSSPASNRCCIKMSVSVDEKKKSFSLQKSEEAFNAA KNLMPGGVNSPVRAFKSVGGQPVLIDSVKGSKMWDIDGNEYIDYVGSWGPAIIGHADDEV LAALAETMKKGTSFGAPCLLENVLAEMVISAVPSIEMVRFVNSGTEACMGVLRLARAFTN KEKFIKFEGCYHGHANAFLVKAGSGVATLGLPDSPGVPKAATSDTLTAPYNDLEAVEKLF AAHKGEISAVILEPVVGNSGFIPPTPEFINGLRQLTKDNGVLLIFDEVMTGFRLAYGGAQ EYFGITPDLTTLGKIIGGGLPVGAYGGRRDIMEMVAPAGPMYQAGTLSGNPLAMTAGIHT LKRLKQAGTYEYLDKITKELTNGILEAGKKTGHPMCGGYISGMFGFFFAEGPVYNFADSK KSDTEKFGRFFRGMLEEGVYFAPSQFEAGFTSLAHTPEDIQLTIAAAERVLSRI TREMBL:Q59928 ID Q59928 PRELIMINARY; PRT; 70 AA. AC Q59928; 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 N-ACETYLORNITHINE AMINOTRANSFERASE (EC 2.6.1.11) (FRAGMENT). GN ARGD. OS STREPTOCOCCUS MUTANS. OC PROKARYOTA; FIRMICUTES; COCCI; STREPTOCOCCAEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=JH1005; RA GUTIERREZ J.A., CROWLEY P.J., BROWN D.P., HILLMAN J.D., YOUNGMAN P., RA BLEIWEIS A.S.; RL SUBMITTED (MAR-1996) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: N2-ACETYL-L-ORNITHINE + 2-OXOGLUTARATE = CC N-ACETYL-L-GLUTAMATE 5-SEMIALDEHYDE + L-GLUTAMATE. CC -!- COFACTOR: PYRIDOXAL-PHOSPHATE. DR EMBL; U48887; G1213508; -. KW TRANSFERASE; AMINOTRANSFERASE. FT NON_TER 1 1 FT NON_TER 70 70 SQ SEQUENCE 70 AA; 7475 MW; 3A86075B CRC32; >Q59928 NSGAEANEAAIKIARKATGKQEIITFQNSFHGRTFGSMSATGQDKIKVGFGDAVPHFNYA VFNDLNSVKA TREMBL:Q59282 ID Q59282 PRELIMINARY; PRT; 389 AA. AC Q59282; 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 ACETYLORNITHINE AMINOTRANSFERASE (EC 2.6.1.11). GN ARGD. OS CORYNEBACTERIUM GLUTAMICUM. OC PROKARYOTA; FIRMICUTES; IRREGULAR ASPOROGENOUS RODS; CORYNEFORM GROUP. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 13032; RX MEDLINE; 96146054. RA SAKANYAN V., PETROSYAN P., LECOCQ M., BOYEN A., LEGRAIN C., RA DEMAREZ M.N., HALLET J.N., GLANSDORFF N.; RL MICROBIOLOGY 142:99-108(1996). CC -!- CATALYTIC ACTIVITY: N2-ACETYL-L-ORNITHINE + 2-OXOGLUTARATE = CC N-ACETYL-L-GLUTAMATE 5-SEMIALDEHYDE + L-GLUTAMATE. CC -!- COFACTOR: PYRIDOXAL-PHOSPHATE. DR EMBL; X86157; E146164; -. KW TRANSFERASE; AMINOTRANSFERASE. SQ SEQUENCE 389 AA; 41103 MW; 2752EEE1 CRC32; >Q59282 MSTLETWPQVIINTYGTPPVELVSGKGATVTDDQGNVYIDLLAGIAVNALGHAHPAIIEA VTNQIGQLGHVSNLFASRPVVEVAEELIKRFSLDDATLAAQTRVFFCNSGAEANEAAFKI ARLTGRSRILAAVHGFHGRTMGSLALTGQPDKREAFLPMPSGVEFYPYGDTDYLRKMVET NPTDVAAIFLEPIQGETGVVPAPEGFLKAVRELCDEYGILMITDEVQTGVGRTGDFFAHQ HDGVVPDVVTMAKGLGGGLPIGACLALRAAELMTPGKHGTTFGGNPVACAAAKAVLSVVD DAFCAEVARKQLFKELLAKVDGVVDVRGRGLMLGVVLERDVAKQAVLDGFKHGVILNAPA DNIIRLTPPLVITDEEIADAVKAIAETIA TREMBL:Q58020 ID Q58020 PRELIMINARY; PRT; 445 AA. AC Q58020; 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 GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE. GN MJ0603. 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., RA GOCAYNE J.D., KERLAVAGE A.R., DOUGHERTY B.A., TOMB J.F., RA ADAMS M.D., REICH C.I., OVERBEEK R., KIRKNESS E.F., RA WEINSTOCK K.G., MERRICK J.M., GLODEK A., SCOTT J.L., RA GEOGHAGEN N.S.M., WEIDMAN J.F., FUHRMANN J.L., PRESLEY E.A., RA NGUYEN D., UTTERBACK T.R., KELLEY J.M., PETERSON J.D., SADOW P.W., RA HANNA M.C., COTTON M.D., HURST M.A., ROBERTS K.M., KAINE B.P., RA BORODOVSKY M., KLENK H.P., FRASER C.M., SMITH H.O., WOESE C.R., RA VENTER J.C.; RL SCIENCE 273:1058-1073(1996). DR EMBL; U67508; G1591312; -. KW TRANSFERASE; AMINOTRANSFERASE. SQ SEQUENCE 445 AA; 49682 MW; 6782D643 CRC32; >Q58020 MVNSSPLWKKLMRKCKGENMALKMDKSKELFEEAKKYLVGGVNSPVRYFKPYPFFVEKAK DCYLFDVDGNCYIDYCLAYGPMVLGHANDAVIKAVKEQLELGSAYGCPTEKEIILAKEVV KRVPCAEMVRFVNSGTEATMSAIRLARGVTGRKKIIKFDGAYHGAHDYVLVKSGSGALTH GHPNSPGIPEETTKNTILIPFNDEDAVKKAINENKDEIACIIVEPIMGNVGCILPKEGYL EFLREITEENDILLIFDEVITGFRLAKGGAQEYFGVVPDIATLGKILGGGFPIGAIVGRR ELMEQFSPLGAIYQAGTFNGNPISITAGIATLKQLDDRFYKETARTAKILADTLRELADK HNIKAKVYNIASMFQIYFNDKEVVNYEIAKQSDTEKFMKYFWRLLEKGVFVPPSQFECCF TSIKHDDEVVDKTIKAMEDVFEGLE TREMBL:Q56470 ID Q56470 PRELIMINARY; PRT; 76 AA. AC Q56470; 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 GLUTAMATE SEMIALDEHYDE AMINOTRANSFERASE (FRAGMENT). OS UNIDENTIFIED ARCHAEON 4B7. OC PROKARYOTA; BACTERIA; MENDOSICUTES; ARCHAEOBACTERIA; CRENARCHAEOTA; OC UNCLASSIFIED CRENARCHAEOTA. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 96146502. RA STEIN J.L., MARSH T.L., WU K.Y., SHIZUYA H., DELONG E.F.; RL J. BACTERIOL. 178:591-599(1996). DR EMBL; U40241; G1127769; -. KW TRANSFERASE; AMINOTRANSFERASE. FT NON_TER 1 1 FT NON_TER 76 76 SQ SEQUENCE 76 AA; 8445 MW; 38BDD433 CRC32; >Q56470 ATQEYLKGIQEMVKTNNALFMLDEIVTGFRFRYGCIYSKMKLDPDIVTLGKIIGGGFPIG VICGKDEIMEHANTSL TREMBL:Q42522 ID Q42522 PRELIMINARY; PRT; 472 AA. AC Q42522; 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 GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE (EC 5.4.3.8) DE (GLUTAMATE-1-SEMIALDEHYDE 2,1-AMINOMUTASE). GN GSA2. OS ARABIDOPSIS THALIANA (MOUSE-EAR CRESS). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; OC CAPPARALES; CRUCIFERAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=COLUMBIA; RA PAEK N.C., TAYLOR B.H., SMITH J.D.; RL PLANT PHYSIOL. 108:1342-1342(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=COLUMBIA; RA BERRY-LOWE S.L.; RL SUBMITTED (JUN-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: (S)-4-AMINO-5-OXOPENTANOATE = CC 5-AMINOLEVULINATE. DR EMBL; U10278; G498914; -. KW TRANSFERASE; AMINOTRANSFERASE; ISOMERASE. SQ SEQUENCE 472 AA; 50105 MW; D03AB2B8 CRC32; >Q42522 MAATLTGSGIALGFSSSAKFSKRASSSSNRRCIKMSVSVEEKTKKFTLQKSEEAFNAAKN LMPGGVNSPVRAFKSVGGQPVVMDSAKGSRIRDIDGNEYIDYVGSWGPAIIGHADDEVLA ALAETMKKGTSFGAPCLLENVLAEMVISAVPSIEMVRFVNSGTEACMGVLRLARAFTGKQ KFIKFEGCYHGHAKSFLVKAGSGVATLGLPDSPGVPKAATSDTLTAPYNDIAAVEKLFEA NKGEIAAIILEPVVGNSGFITPKPEFIEGIRRITKDNGALLILDEVMTGFRLAYGGAQEY FGITPDLTTLGKIIGGGLPVGAYGGRRDIMEMVAPAGPMYQAGTLSGNPLAMTAGIHTLK RLSQPGTYEYLDKITKELTNGILEAGKKTGHAMCGGYISGMFGFFFTEGPVYDFSDAKKS DTEKFGKFFRGMLEEGVYLAPSQFEAGFTSLAHTSEDIQFTIAAAEKVLSRL TREMBL:Q39567 ID Q39567 PRELIMINARY; PRT; 99 AA. AC Q39567; 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 GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE (FRAGMENT). GN GSA. OS CHLAMYDOMONAS REINHARDTII. OC EUKARYOTA; PLANTA; PHYCOPHYTA; CHLOROPHYTA (GREEN ALGAE); OC CHLOROPHYCEAE; VOLVOCALES; CHLAMYDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CC124; RX MEDLINE; 94207187. RA MATTERS G.L., BEALE S.I.; RL PLANT MOL. BIOL. 24:617-629(1994). DR EMBL; U03633; G424153; -. KW TRANSFERASE; AMINOTRANSFERASE. FT NON_TER 99 99 SQ SEQUENCE 99 AA; 10791 MW; FF6B747D CRC32; >Q39567 MQMQLNAKTVQGAFKAQRPRSVRGNVAVRAVAAPPKLVTKRSEEIFKEAQELLPGGVNSP VRAFRSVGGGPIVFDRVKGAYCWDVDGNKYIDYVGSWGP TREMBL:Q39566 ID Q39566 PRELIMINARY; PRT; 463 AA. AC Q39566; 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 GLUTAMATE-1-SEMIALDEHYDE AMINOTRANSFERASE PRECURSOR. GN GSA. OS CHLAMYDOMONAS REINHARDTII. OC EUKARYOTA; PLANTA; PHYCOPHYTA; CHLOROPHYTA (GREEN ALGAE); OC CHLOROPHYCEAE; VOLVOCALES; CHLAMYDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NO-; RX MEDLINE; 94207187. RA MATTERS G.L., BEALE S.I.; RL PLANT MOL. BIOL. 24:617-629(1994). DR EMBL; U03632; G424151; -. KW SIGNAL; TRANSFERASE; AMINOTRANSFERASE. FT SIGNAL 1 30 POTENTIAL. FT CHAIN 31 463 POTENTIAL. SQ SEQUENCE 463 AA; 49228 MW; 6F6590EF CRC32; >Q39566 MQMQLNAKTVQGAFKAQRPRSVRGNVAVRAVAAPPKLVTKRSEEIFKEAQELLPGGVNSP VRAFRSVGGGPIVFDRVKGAYCWDVDGNKYIDYVGSWGPAICGHGNDEVNNALKAQIDKG TSFGAPCELENVLAKMVIDRVPSVEMVRFVSSGTEACLSVLRLMRAYTGREKVLKFTGCY HGHADSFLVKAGSGVITLGLPDSPGVPKSTAAATLTATYNNLDSVRELFAANKGEIAGVI LEPVVGNSGFIVPTKEFLQGLREICTAEGAVLCFDEVMTGFRIAKGCAQEHFGITPDLTT MGKVIGGGMPVGAYGGKKEIMKMVAPAGPMYQAGTLSGNPMAMTAGIKTLEILGRPGAYE HLEKVTKRLIDGIMAAAKEHSHEITGGNISGMFGFFFCKGPVTCFEDALAADTAKFARFH RGMLEEGVYLAPSQFEAGFTSLAHSEADVDATIAAARRVFARI TREMBL:Q29591 ID Q29591 PRELIMINARY; PRT; 62 AA. AC Q29591; 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 ORNITHINE--OXO-ACID TRANSAMINASE (EC 2.6.1.13) DE (ORNITHINE--OXO-ACID AMINOTRANSFERASE) (ORNITHINE AMINOTRANSFERASE) DE (ORNITHINE KETOACID AMINOTRANSFERASE) (FRAGMENT). OS SUS SCROFA (PIG). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; ARTIODACTYLA. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=SMALL INTESTINE; RA WINTEROE A.K., FREDHOLM M., DAVIES W.; RL SUBMITTED (AUG-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: L-ORNITHINE + A 2-OXO ACID = CC L-GLUTAMATE 5-SEMIALDEHYDE + A L-AMINO ACID. CC -!- COFACTOR: PYRIDOXAL-PHOSPHATE. DR EMBL; F14762; G972345; -. KW TRANSFERASE; AMINOTRANSFERASE. FT NON_TER 62 62 SQ SEQUENCE 62 AA; 6764 MW; BC130F8F CRC32; >Q29591 MFSKLAHLQTVAVLRRGVHSTVASATSVATKRTVQGPPSSDYIFEREAKYGAHNYHPLPV AL