PIR:CEECME >P1;CEECME UDP-N-acetylmuramoylalanine--D-glutamate ligase (EC 6.3.2.9) - Escherichia coli N;Alternate names: UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase C;Species: Escherichia coli C;Date: 30-Jun-1991 #sequence_revision 30-Jun-1991 #text_change 06-Dec-1996 C;Accession: S08396; S07581; S40598; S19573; B32581 R;Ikeda, M.; Wachi, M.; Ishino, F.; Matsuhashi, M. Nucleic Acids Res. 18, 1058, 1990 A;Title: Nucleotide sequence involving murD and an open reading frame ORF-Y spacing murF and ftsW in Escherichia coli. A;Reference number: S08395; MUID:90192099 A;Accession: S08396 A;Molecule type: DNA A;Residues: 1-438 R;Mengin-Lecreulx, D.; van Heijenoort, J. Nucleic Acids Res. 18, 183, 1990 A;Title: Nucleotide sequence of the murD gene encoding the UDP-MurNAc-L-Ala-D-Glu synthetase of Escherichia coli. A;Reference number: S07581; MUID:90174916 A;Accession: S07581 A;Molecule type: DNA A;Residues: 1-27,'A',29-72,84-173,'T',175-275,'RV',278-438 A;Cross-references: EMBL:X51584 R;Yura, T.; Mori, H.; Nagai, H.; Nagata, T.; Ishihama, A.; Fujita, N.; Isono, K.; Mizobuchi, K.; Nakata, A. submitted to the EMBL Data Library, December 1992 A;Reference number: S40531 A;Accession: S40598 A;Molecule type: DNA A;Residues: 1-438 A;Cross-references: EMBL:D10483 R;Pratviel-Sosa, F.; Mengin-Lecreulx, D.; van Heijenoort, J. Eur. J. Biochem. 202, 1169-1176, 1991 A;Title: Over-production, purification and properties of the uridine diphosphate N-acetylmuramoyl-L-alanine: D-glutamate ligase from Escherichia coli. A;Reference number: S19573; MUID:92111492 A;Accession: S19573 A;Molecule type: protein A;Residues: 2-20 R;Ikeda, M.; Sato, T.; Wachi, M.; Jung, H.K.; Ishino, F.; Kobayashi, Y.; Matsuhashi, M. J. Bacteriol. 171, 6375-6378, 1989 A;Title: Structural similarity among Escherichia coli FtsW and RodA proteins and Bacillus subtilis SpoVE protein, which function in cell division, cell elongation, and spore formation, respectively. A;Reference number: A32581; MUID:90036736 A;Accession: B32581 A;Molecule type: DNA A;Residues: 376-438 A;Note: the authors translated the codon ATG for residue 407 as Trp C;Genetics: A;Gene: murD A;Map position: 2 min C;Superfamily: UDP-N-acetylmuramate--alanine ligase C;Keywords: ligase; peptidoglycan biosynthesis >CEECME MADYQGKNVVIIGLGLTGLSCVDFFLARGVTPRVMDTRMTPPGLDKLPEAVERHTGSLND EWLMAADLIVASPGIALAHPSLSAAADAGIEIVGDIELFCREAQAPIVAITGSNGKSTVT TLVGEMAKAAGVNVGVGGNIGLPALMLLDDECELYVLELSSFQLETTSSLQAVAATILNV TEDHMDRYPFGLQQYRAAKLRIYENAKVCVVNADDALTMPIRGADERCVSFGVNMGDYHL NHQQGETWLRVKGEKVLNVKEMKLSGQHNYTNALAALALADAAGLPRASSLKALTTFTGL PHRFEVVLEHNGVRWINDSKATNVGSTEAALNGLHVDGTLHLLLGGDGKSADFSPLARYL NGDNVRLYCFGRDGAQLAALRPEVAEQTETMEQAMRLLAPRVQPGDMVLLSPACASLDQF KNFEQRGNEFARLAKELG SWISSPROT:HEM1_YEAST ID HEM1_YEAST STANDARD; PRT; 548 AA. AC P09950; DT 01-MAR-1989 (REL. 10, CREATED) DT 01-MAR-1989 (REL. 10, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE 5-AMINOLEVULINIC ACID SYNTHASE, MITOCHONDRIAL PRECURSOR (EC 2.3.1.37) DE (DELTA-AMINOLEVULINATE SYNTHASE) (DELTA-ALA SYNTHETASE). GN HEM1 OR YDR232W OR YD9934.16. OS SACCHAROMYCES CEREVISIAE (BAKER'S YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 86192482. RA URBAN-GRIMAL D., VOLLAND C., GARNIER T., DEHOUX P., LABBE-BOIS R.; RL EUR. J. BIOCHEM. 156:511-519(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA MURPHY L., HARRIS D., BARRELL B., RAJANDREAM M.A.; RL SUBMITTED (MAR-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [3] RP SEQUENCE OF 1-2 FROM N.A. RX MEDLINE; 88097438. RA KENG T., GUARENTE L.; RL PROC. NATL. ACAD. SCI. U.S.A. 84:9113-9117(1987). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; J03556; E18676; -. DR EMBL; M26329; G171662; -. DR EMBL; Z48612; G728687; -. DR PIR; A24870; SYBYAL. DR LISTA; SC00427; HEM1. DR SGD; L0000760; HEM1. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; MITOCHONDRION; KW TRANSIT PEPTIDE; PYRIDOXAL PHOSPHATE. FT TRANSIT 1 ? MITOCHONDRION. FT CHAIN ? 548 5-AMINOLEVULINIC ACID SYNTHASE. FT BINDING 337 337 PYRIDOXAL PHOSPHATE (PROBABLE). FT DOMAIN 26 62 ALA-RICH. FT DOMAIN 54 62 POLY ALA. SQ SEQUENCE 548 AA; 59362 MW; B21AAA85 CRC32; >HEM1_YEAST MQRSIFARFGNSSAAVSTLNRLSTTAAPHAKNGYATATGAGAAAATATASSTHAAAAAAA AANHSTQESGFDYEGLIDSELQKKRLDKSYRYFNNINRLAKEFPLAHRQREADKVTVWCS NDYLALSKHPEVLDAMHKTIDKYGCGAGGTRNIAGHNIPTLNLEAELATLHKKEGALVFS SCYVANDAVLSLLGQKMKDLVIFSDELNHASMIVGIKHANVKKHIFKHNDLNELEQLLQS YPKSVPKLIAFESVYSMAGSVADIEKICDLADKYGALTFLDEVHAVGLYGPHGAGVAEHC DFESHRASGIATPKTNDKGGAKTVMDRVDMITGTLGKSFGSVGGYVAASRKLIDWFRSFA PGFIFTTTLPPSVMAGATAAIRYQRCHIDLRTSQQKHTMYVKKAFHELGIPVIPNPSHIV PVLIGNADLAKQASDILINKHQIYVQAINFPTVARGTERLRITPTPGHTNDLSDILINAV DDVFNELQLPRVRDWESQGGLLGVGESGFVEESNLWTSSQLSLTNDDLNPNVRDPIVKQL EVSSGIKQ SWISSPROT:HEM1_RHOSH ID HEM1_RHOSH STANDARD; PRT; 407 AA. AC Q04512; DT 01-OCT-1993 (REL. 27, CREATED) DT 01-OCT-1993 (REL. 27, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE 5-AMINOLEVULINIC ACID SYNTHASE 1 (EC 2.3.1.37) (DELTA-AMINOLEVULINATE DE SYNTHASE) (DELTA-ALA SYNTHETASE). GN HEMA. OS RHODOBACTER SPHAEROIDES (RHODOPSEUDOMONAS SPHAEROIDES). OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; PURPLE BACTERIA; OC RHODOSPIRILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=2.4.1; RX MEDLINE; 93224451. RA NEIDLE E.L., KAPLAN S.; RL J. BACTERIOL. 175:2292-2303(1993). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; L07490; G151937; -. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; PYRIDOXAL PHOSPHATE; KW MULTIGENE FAMILY. FT BINDING 248 248 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 407 AA; 44616 MW; 1797F0D5 CRC32; >HEM1_RHOSH MDYNLALDTALNRLHTEGRYRTFIDIERRKGAFPKAMWRKPDGSEKEITVWCGNDYLGMG QHPVVLGAMHEALDSTGAGSGGTRNISGTTLYHKRLEAELADLHGKEAALVFSSAYIAND ATLSTLPQLIPGLVIVSDKLNHASMIEGIRRSGTEKHIFKHNDLDDLRRILTSIGKDRPI LVAFESVYSMDGDFGRIEEICDIADEFGALKYIDEVHAVGMYGPRGGGVAERDGLMDRID IINGTLGKAYGVFGGYIAASSKMCDAVRSYAPGFIFSTSLPPVVAAGAAASVRHLKGDVE LREKHQTQARILKMRLKGLGLPIIDHGSHIVPVHVGDPVHCKMISDMLLEHFGIYVQPIN FPTVPRGTERLRFTPSPVHDSGMIDHLVKAMDVLWQHCALNRAEVVA SWISSPROT:HEM1_RHOCA ID HEM1_RHOCA STANDARD; PRT; 401 AA. AC P18079; DT 01-NOV-1990 (REL. 16, CREATED) DT 01-NOV-1990 (REL. 16, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE 5-AMINOLEVULINIC ACID SYNTHASE (EC 2.3.1.37) (DELTA-AMINOLEVULINATE DE SYNTHASE) (DELTA-ALA SYNTHETASE). GN HEMA. OS RHODOBACTER CAPSULATUS (RHODOPSEUDOMONAS CAPSULATA). OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; PURPLE BACTERIA; OC RHODOSPIRILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SB1003; RX MEDLINE; 90340288. RA HORNBERGER U., LIEBETANZ R., TICHY H.V., DREWS G.; RL MOL. GEN. GENET. 221:371-378(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=SB1003; RX MEDLINE; 91250108. RA WRIGHT M.S., ECKERT J.J., BIEL S.W., BIEL A.J.; RL FEMS MICROBIOL. LETT. 62:339-342(1991). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; X53309; G46029; -. DR EMBL; X53864; E264664; -. DR PIR; S10528; S10528. DR PIR; S16149; S16149. DR PIR; S16880; S16880. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; PYRIDOXAL PHOSPHATE. FT BINDING 248 248 PYRIDOXAL PHOSPHATE (PROBABLE). SQ SEQUENCE 401 AA; 43575 MW; E73D6BE0 CRC32; >HEM1_RHOCA MDYNLALDKAIQKLHDEGRYRTFIDIEREKGAFPKAQWNRPDGGKQDITVWCGNDYLGMG QHPVVLAAMHEALEAVGAGSGGTRNISGTTAYHRRLEAEIADLHGKEAALVFSSAYIAND ATLSTLRLLFPGLIIYSDSLNHASMIEGIKRNAGPKRIFRHNDVAHLRELIAADDPAAPK LIAFESVYSMDGDFGPIKEICDIADEFGALTYIDEVHAVGMYGPRGAGVAERDGLMHRID IFNGTLAKAYGVFGGYIAASAKMVDAVRSYAPGFIFSTSLPPAIAAGAQASIAFLKTAEG QKLRDAQQMHAKVLKMRLKALGMPIIDHGSHIVPVVIGDPVHTKAVSDMLLSDYGVYVQP INFPTVPRGTERLRFTPSPVHDLKQIDGLVHAMDLLWARCA SWISSPROT:HEM1_RHIME ID HEM1_RHIME STANDARD; PRT; 76 AA. AC P08080; DT 01-AUG-1988 (REL. 08, CREATED) DT 01-AUG-1988 (REL. 08, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE 5-AMINOLEVULINIC ACID SYNTHASE (EC 2.3.1.37) (DELTA-AMINOLEVULINATE DE SYNTHASE) (DELTA-ALA SYNTHETASE) (FRAGMENT). GN HEMA. OS RHIZOBIUM MELILOTI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC RHIZOBIACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 85297790. RA LEONG S.A., WILLIAMS P.H., DITTA G.S.; RL NUCLEIC ACIDS RES. 13:5965-5976(1985). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; X02853; G46262; -. DR PIR; A24077; A24077. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; PYRIDOXAL PHOSPHATE. FT NON_TER 76 76 SQ SEQUENCE 76 AA; 8699 MW; 6EF9F1DE CRC32; >HEM1_RHIME MMMDFESFFKNELDGLHQEGRYRVFADLARHRGSFPKATRYTADGAQEVTVWCSNDYLGM GQCPIVTEAMKNAIDE SWISSPROT:HEM1_RAT ID HEM1_RAT STANDARD; PRT; 642 AA. AC P13195; 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 5-AMINOLEVULINIC ACID SYNTHASE MITOCHONDRIAL PRECURSOR, NONSPECIFIC DE (EC 2.3.1.37) (DELTA-AMINOLEVULINATE SYNTHASE) (DELTA-ALA SYNTHETASE) DE (ALAS-H). OS RATTUS NORVEGICUS (RAT). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RX MEDLINE; 88186809. RA SRIVASTAVA G., BORTHWICK I.A., MAGUIRE D.J., ELFERINK C.J., RA BAWDEN M.J., MERCER J.F.B., MAY B.K.; RL J. BIOL. CHEM. 263:5202-5209(1988). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RX MEDLINE; 89034050. RA YAMAMOTO M., KURE S., ENGEL J.D., HIRAGA K.; RL J. BIOL. CHEM. 263:15973-15979(1988). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- THERE ARE TWO DELTA-ALA SYNTHETASE IN VERTEBRATES: AN ERYTHROID- CC SPECIFIC FORM AND ONE (HOUSEKEEPING) WHICH IS EXPRESSED IN ALL CC TISSUES. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; J03190; G203068; -. DR EMBL; J04044; G202860; -. DR PIR; A28191; SYRTAL. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; MITOCHONDRION; KW TRANSIT PEPTIDE; PYRIDOXAL PHOSPHATE; MULTIGENE FAMILY. FT TRANSIT 1 56 MITOCHONDRION. FT CHAIN 57 642 5-AMINOLEVULINIC ACID SYNTHASE. FT BINDING 447 447 PYRIDOXAL PHOSPHATE (PROBABLE). FT CONFLICT 118 136 ARRAAASSARPVWSFRRTW -> FT SQTGSSVFRKASLELQEDV (IN REF. 2). FT CONFLICT 144 144 T -> K (IN REF. 2). FT CONFLICT 195 195 V -> S (IN REF. 2). FT CONFLICT 244 245 NN -> KK (IN REF. 2). FT CONFLICT 251 251 S -> C (IN REF. 2). FT CONFLICT 377 377 V -> L (IN REF. 2). FT CONFLICT 587 587 Y -> F (IN REF. 2). SQ SEQUENCE 642 AA; 71128 MW; FE31E64C CRC32; >HEM1_RAT METVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRTVSTSAAQCQQVKE TPPANEKEKTAKAAVQQAPDESQMAQTPDGTQLPPGHPSPSTSQSSGSKCPFLAAQLARR AAASSARPVWSFRRTWQEMHAVRTEVAQSPVLPSLVNAKRDGEGPSPLLKNFQDIMRKQR PERVSHLLQDNLPKVVSTFQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDS LITNNQVSVWSSNDYLGMSRHPRVCGAVIETVKQHGAGAGGTRNISGTSKFHVELEQELA DLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH NDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGL YGASGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSLLIDTVRSYAAGFIFTTSLP PMLLAGALESVRILKSNEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVADAA KNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLEKLLLTWKRVG LELKPHSSAECNFCRRPLHFEVMSEREKAYFSGMSKMVSAQA SWISSPROT:HEM1_PARDE ID HEM1_PARDE STANDARD; PRT; 409 AA. AC P43089; 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 5-AMINOLEVULINIC ACID SYNTHASE (EC 2.3.1.37) (DELTA-AMINOLEVULINATE DE SYNTHASE) (DELTA-ALA SYNTHETASE). GN HEMA. OS PARACOCCUS DENITRIFICANS. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC UNCERTAIN. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=PD 1222; RX MEDLINE; 95014024. RA PAGE M.D., FERGUSON S.J.; RL J. BACTERIOL. 176:5919-5928(1994). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; U12508; G537435; -. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; PYRIDOXAL PHOSPHATE. FT BINDING 248 248 PYRIDOXAL PHOSPHATE (PROBABLE). SQ SEQUENCE 409 AA; 44596 MW; 075D09C2 CRC32; >HEM1_PARDE MDYSAALDQAIGKLHEEGRYRTFIDIERRKGAYPTAVWTRPDGTETRITVWCGNDYLGMG QHPVVLAAMHEALDATGAGSGGTRNISGTTVYHKRLEAELADLHGKEAALVFSSVYIAND ATLSTLRKLFPGLIIYSDELNHASMIEGIKRSTAPKRIFRHNDVGHLRELLAADDPEAPK LIAFESIYSMDGDFAPIKEICDLADEFNALTYLDEVHAVGMYGPRGGGVAERDGLSHRID IFNGTLAKAFGVFGGYIGFGARMVDAIRSYAPGFIFTTSLPPAVAAGVAASIAFLKTAEG QFVRDQQQLNGRLLKMRLRGAGMPVMDHGSHIVPVHVGNPVHCKALSDMLLADFSIYVQP INFPTVPRGTERLRFTASPVHDPKQIDHLVKAMDSLWSQCKLNRSTSAA SWISSPROT:HEM1_OPSTA ID HEM1_OPSTA STANDARD; PRT; 627 AA. AC P43091; 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 5-AMINOLEVULINIC ACID SYNTHASE MITOCHONDRIAL PRECURSOR, NONSPECIFIC DE (EC 2.3.1.37) (DELTA-AMINOLEVULINATE SYNTHASE) (DELTA-ALA SYNTHETASE) DE (ALAS-H). OS OPSANUS TAU (OYSTER TOADFISH). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA; OC OSTEICHTHYES; ACTINOPTERYGII; BATRACHOIDIFORMES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RA CORNELL N.W.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- THERE ARE TWO DELTA-ALA SYNTHETASE IN VERTEBRATES: AN ERYTHROID- CC SPECIFIC FORM AND ONE (HOUSEKEEPING) WHICH IS EXPRESSED IN ALL CC TISSUES. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; L35915; G532630; -. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; MITOCHONDRION; KW TRANSIT PEPTIDE; PYRIDOXAL PHOSPHATE; MULTIGENE FAMILY. FT TRANSIT 1 58 MITOCHONDRION (POTENTIAL). FT CHAIN 59 627 5-AMINOLEVULINIC ACID SYNTHASE. FT BINDING 432 432 PYRIDOXAL PHOSPHATE (PROBABLE). SQ SEQUENCE 627 AA; 69691 MW; 7502AC87 CRC32; >HEM1_OPSTA MDVIVRRCPFLARVPQAFFQQSKKSLAVYAQRCPFMMELASKPMAPSLARALCSSSSSQQ KIEDTMSTGEVLKPKAEAKLPVGLATPPSNEAVAPKCPFLAAEMGQNNSNVVRQVGVEFQ EDVEEIRTVQKEVSPAQLEQPSLIGKTMGEEGHQKNLMKSLLKQRPKRVSHLLQDNLPGS FTRFYYDNFFEKKIEEKKSDHTYRVFKTVNRLANEFPMADDFTGSLEDKREVSVWCSNDY LGMSRHPRVAQAIMETLRKHGSGAGGTRNISGTSKFHVELEQELADLHRKDAALLFTSCF VANDSTLFTLAKMLPGCEIYSDAGNHASMIQGIRNSGAKKFIFRHNDVAHLRELLEKGDP TKPKIVAFETVHSMDGAVCPLEEMCDLAHEFGAITFVDEVHAVGLYGPRGGGIGDRDGIM HKMDIISGTLGKAFGCVGGYIASTATLVDTVRSYAAGFIFTTSLPPMLLAGAKQSIQILK GEEGCTLRRKHQRNVKLLRQMLMDSGLPVVHCPSHIIPIRVSDAEKNTKVCDLMMSHHNI YVQAINYPTVARGDELLRIAPTPHHTPEMMKYFVDRLVQTWKEVGLELKPHSSAECTFCQ QPLHFEVMNEREKSYFSGLSHLVSVCA SWISSPROT:HEM1_HUMAN ID HEM1_HUMAN STANDARD; PRT; 640 AA. AC P13196; DT 01-JAN-1990 (REL. 13, CREATED) DT 01-AUG-1991 (REL. 19, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE 5-AMINOLEVULINIC ACID SYNTHASE MITOCHONDRIAL PRECURSOR, NONSPECIFIC DE (EC 2.3.1.37) (DELTA-AMINOLEVULINATE SYNTHASE) (DELTA-ALA SYNTHETASE) DE (ALAS-H). GN ALAS1 OR ALASH. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RX MEDLINE; 91088347. RA BISHOP D.F.; RL NUCLEIC ACIDS RES. 18:7187-7188(1990). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RX MEDLINE; 88040476. RA BAWDEN M.J., BORTHWICK I.A., HEALY H.M., MORRIS C.P., MAY B.K., RA ELLIOTT W.H.; RL NUCLEIC ACIDS RES. 15:8563-8563(1987). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- THERE ARE TWO DELTA-ALA SYNTHETASE IN VERTEBRATES: AN ERYTHROID- CC SPECIFIC FORM AND ONE (HOUSEKEEPING) WHICH IS EXPRESSED IN ALL CC TISSUES. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -!- CAUTION: REF.2 SEQUENCE WAS INCORRECT IN MANY PLACES. DR EMBL; X56351; G28583; -. DR EMBL; Y00451; G599830; ALT_SEQ. DR PIR; A27834; SYHUAL. DR PIR; S13682; S13682. DR MIM; 125290; -. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; MITOCHONDRION; KW TRANSIT PEPTIDE; PYRIDOXAL PHOSPHATE; MULTIGENE FAMILY. FT TRANSIT 1 56 MITOCHONDRION. FT CHAIN 57 640 5-AMINOLEVULINIC ACID SYNTHASE. FT BINDING 445 445 PYRIDOXAL PHOSPHATE (PROBABLE). SQ SEQUENCE 640 AA; 70580 MW; 7B1D99CD CRC32; >HEM1_HUMAN MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKE TPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGS SVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPE RVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLI TKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADL HGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHND VSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYG ARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPM LLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKN TEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFLENLLVTWKQVGLE LKPHSSAECNFCRRPLHFEVMSEREKSYFSGLSKLVSAQA SWISSPROT:HEM1_EMENI ID HEM1_EMENI STANDARD; PRT; 648 AA. AC P38092; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE 5-AMINOLEVULINIC ACID SYNTHASE, MITOCHONDRIAL PRECURSOR (EC 2.3.1.37) DE (DELTA-AMINOLEVULINATE SYNTHASE) (DELTA-ALA SYNTHETASE). GN HEMA. OS EMERICELLA NIDULANS (ASPERGILLUS NIDULANS). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; PLECTOMYCETES; EUROTIALES. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=R153; RX MEDLINE; 93306758. RA BRADSHAW R.E., DIXON S.W.C., RAITT D.C., PILLAR T.M.; RL CURR. GENET. 23:501-507(1993). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; X64170; G2361; -. DR PIR; S31846; S31846. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; MITOCHONDRION; KW TRANSIT PEPTIDE; PYRIDOXAL PHOSPHATE. FT TRANSIT 1 ? MITOCHONDRION. FT CHAIN ? 648 5-AMINOLEVULINIC ACID SYNTHASE. FT BINDING 412 412 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 648 AA; 69045 MW; 57D93FB7 CRC32; >HEM1_EMENI MEALLQQSRAMCPFLKRSSPNTLRSLATATRPSTSPGGGTMTNLQRIARRCPVMSKALAV QSARMTGTKRFTSSAAGVPGAGAGTPKPTRGSPGKRALHSTGGNGANMSTEFHKGAQQIH PGLSNATRSHVGASATVSGPTPRAPVAAPFDYDAFYNAELQKKHQDKSYRYFNNINRLAQ EFPRAHTASKDEKVTVWCSNDYLGMGRNPEVLATMHKTLDTYGAGAGGTRNISGHNQHAV SLENTLAKLHGKEAALVFSSCFVANDATLATLGSKMPDCVILSDSLNHASMIQGIRHSGR KKMVFKHNDLVDLETKLASLPLHVPKIIAFESVYSMCGSIAPIEAICDLADKYGAITFLD EVHAVGMYGPHGAGVAEHLDYEIYASQDTANPLSTKGTVMDRINIITGTLGKAYGCVGGY IAGSAALVDTIRSLAPGFIFTTSLPPATMAGADTAIRYQARHQQDRILQQLHTRAVKQSF KDLDIPVIPNPSHIVPLLVGDAELAKQASDKLLEEHGIYVQAINYPTVPRGEERLRITPT PGHTQELRDHLVEAVNTVWNDLGIKRASDWKAMGGFVGVGVEAAELENQPIWTDAQLNMR PDETLEAAVEREFQAAVPGMKAGGAKAKPVGSIAANPIGASIPVAAAA SWISSPROT:HEM1_CHICK ID HEM1_CHICK STANDARD; PRT; 635 AA. AC P07997; DT 01-AUG-1988 (REL. 08, CREATED) DT 01-JAN-1990 (REL. 13, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE 5-AMINOLEVULINIC ACID SYNTHASE MITOCHONDRIAL PRECURSOR, NONSPECIFIC DE (EC 2.3.1.37) (DELTA-AMINOLEVULINATE SYNTHASE) (DELTA-ALA SYNTHETASE) DE (ALAS-H). GN ALASN. OS GALLUS GALLUS (CHICKEN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; AVES; NEOGNATHAE; OC GALLIFORMES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RX MEDLINE; 86148479. RA MAGUIRE D.J., DAY A.R., BORTHWICK I.A., SRIVASTAVA G., WIGLEY P.L., RA MAY B.K., ELLIOTT W.H.; RL NUCLEIC ACIDS RES. 14:1379-1391(1986). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RX MEDLINE; 85257679. RA BORTHWICK I.A., SRIVASTAVA G., DAY A.R., PIROLA B.A., SNOSWELL M.A., RA MAY B.K., ELLIOTT W.H.; RL EUR. J. BIOCHEM. 150:481-484(1985). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE; 89128863. RA RIDDLE R.D., YAMAMOTO M., ENGEL J.D.; RL PROC. NATL. ACAD. SCI. U.S.A. 86:792-796(1989). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- THERE ARE TWO DELTA-ALA SYNTHETASE IN VERTEBRATES: AN ERYTHROID- CC SPECIFIC FORM AND ONE (HOUSEKEEPING) WHICH IS EXPRESSED IN ALL CC TISSUES. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; X02827; G63608; -. DR EMBL; X03517; G763098; -. DR EMBL; X03627; G763098; JOINED. DR PIR; A23538; SYCHAL. DR PIR; B31452; B31452. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; MITOCHONDRION; KW TRANSIT PEPTIDE; PYRIDOXAL PHOSPHATE; MULTIGENE FAMILY. FT TRANSIT 1 56 MITOCHONDRION. FT CHAIN 57 635 5-AMINOLEVULINIC ACID SYNTHASE. FT BINDING 440 440 PYRIDOXAL PHOSPHATE (PROBABLE). FT CONFLICT 53 53 S -> A (IN REF. 2 AND 3). SQ SEQUENCE 635 AA; 69948 MW; BA6F1FAF CRC32; >HEM1_CHICK MEAVVRRCPFLARVSQAFLQKAGPSLLFYAQHCPKMMEAAPPAAARGLATSASRGQQVEE TPAAQPEAKKAKEVAQQNTDGSQPPAGHPPAAAVQSSATKCPFLAAQMNHKSSNVFCKAS LELQEDVKEMQVDRKGKEFAKIPTNSVVRNTEAEGEEQSGLLKKFKDIMLKQRPESVSHL LQDNLPKSVSTFQYDQFFEKKIDEKKKDHTYRVFKTVNRKAQIFPMADDYSDSLITKKEV SVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLEKELADLHGKDA ALLFSSCFVANDSTLFTLAKMLPGCEIYSDSGNHASMIQGIRNSRVPKHIFRHNDVNHLR ELLKKSDPSTPKIVAFETVHSMDGAVCPLEELCDVAHEHGAITFVDEVHAVGLYGARGGG IGDRDGVMHKMDIISGTLGKAFACVGGYISSTSALIDTVRSYAAGFIFTTSLPPMLLAGA LESVRTLKSAEGQVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPIRVADAAKNTEICD KLMSQHSIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSYFLEKLLATWKDVGLELKPHS SAECNFCRRPLHFEVMSERERSYFSGMSKLLSVSA SWISSPROT:HEM1_BRAJA ID HEM1_BRAJA STANDARD; PRT; 409 AA. AC P08262; DT 01-AUG-1988 (REL. 08, CREATED) DT 01-AUG-1988 (REL. 08, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE 5-AMINOLEVULINIC ACID SYNTHASE (EC 2.3.1.37) (DELTA-AMINOLEVULINATE DE SYNTHASE) (DELTA-ALA SYNTHETASE). GN HEMA. OS BRADYRHIZOBIUM JAPONICUM. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC RHIZOBIACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 87277426. RA MCCLUNG C.R., SOMERVILLE J.E., GUERINOT M.L., CHELM B.K.; RL GENE 54:133-139(1987). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; M16751; G152097; -. DR PIR; A27478; SYZJAL. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; PYRIDOXAL PHOSPHATE. FT BINDING 247 247 PYRIDOXAL PHOSPHATE (PROBABLE). SQ SEQUENCE 409 AA; 44602 MW; A6BCC382 CRC32; >HEM1_BRAJA MDYSQFFNSALDRLHTERRYRVFADLERMAGRFPHAIWHSPKGKRDVVIWCSNDYLGMGQ HPKVVGAMVETATRVGTGAGGTRNIAGTHHPLVQLEAELADLHGKEAALLFTSGYVSNQT GIATIAKLIPNCLILSDELNHNSMIEGIRQSGCERQVFRHNDLADLEALLKAAGANRPKL IACESLYSMDGDVAPLAKICDLAEKYNAMTYVDEVHAVGMYGPRGGGIAERDGVMHRIDI LEGTLAKAFGCLGGYIAANGRIIDAVRSYAPGFIFTTALPPAICSAATAAIKHLKTSSWE RERHQDRAARVKAILNAAGLPVMSSDTHIVPLFIGDAEKCKQASDLLLEEHGIYIQPINY PTVAKGSERLRITPSPYHDDGLIDQLAEALLQVWDRLGLPLKQKSLAAE SWISSPROT:HEM1_AGRRD ID HEM1_AGRRD STANDARD; PRT; 405 AA. AC P26505; DT 01-AUG-1992 (REL. 23, CREATED) DT 01-AUG-1992 (REL. 23, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE 5-AMINOLEVULINIC ACID SYNTHASE (EC 2.3.1.37) (DELTA-AMINOLEVULINATE DE SYNTHASE) (DELTA-ALA SYNTHETASE). GN HEMA. OS AGROBACTERIUM RADIOBACTER. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC RHIZOBIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 4718; RX MEDLINE; 91238701. RA DROLET M., SASARMAN A.; RL MOL. GEN. GENET. 226:250-256(1991). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR PIR; S15996; S15996. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; PYRIDOXAL PHOSPHATE. FT BINDING 248 248 PYRIDOXAL PHOSPHATE (PROBABLE). SQ SEQUENCE 405 AA; 44411 MW; CA56DA45 CRC32; >HEM1_AGRRD MDFEAFFTTELQSLHSEGRYRVFADIERQQGNFPRATRYNANGQRKDVTVWCSNDYLGMG QNPKVIEAMKAAIDHCGAGAGGTRNISGTNHYHVLLEQELADLHGKESALIFTSGYVSNW ATLGTLGQKIPGLIIFSDALNHASMIEGIRYGRCERVIWKHNDLEDLEAKLKAADPNAPK LIAFESVYSMDGDIAPIKEICDLADRYGAMTYLDEVHAVGMYGPRGGGIAEREGLMDRLT IIEGTLGKAFGVMGGYITGSTAVCDFIRSFASGFIFTTALPPSLAAGAIASIQHLKASPF ERARHQDRVRKLRGLLDARGIPHMDNPSHIVPVMVGDAAKCKWISDILLDSHGVYVQPIN YPTVPRKTERLRITPTPLHSDADIEHLVGALHQLWSHCALARAVA SWISSPROT:HEM0_RHOSH ID HEM0_RHOSH STANDARD; PRT; 407 AA. AC Q06965; 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 5-AMINOLEVULINIC ACID SYNTHASE 2 (EC 2.3.1.37) (DELTA-AMINOLEVULINATE DE SYNTHASE) (DELTA-ALA SYNTHETASE). GN HEMT. OS RHODOBACTER SPHAEROIDES (RHODOPSEUDOMONAS SPHAEROIDES). OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; PURPLE BACTERIA; OC RHODOSPIRILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=2.4.1; RX MEDLINE; 93224451. RA NEIDLE E.L., KAPLAN S.; RL J. BACTERIOL. 175:2292-2303(1993). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -!- CAUTION: EXPRESSED IN THE MUTANT STRAIN HEMA1 BUT EXPRESSION IN CC THE WILD TYPE STRAIN HAS NOT BEEN PROVEN. DR EMBL; L07489; G151939; -. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; PYRIDOXAL PHOSPHATE; KW MULTIGENE FAMILY. FT BINDING 248 248 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 407 AA; 44332 MW; C9292EBC CRC32; >HEM0_RHOSH MEFSQHFQKLIDDMRLDGRYRTFAELERIAGEFPTALWHGPDGQARRVTVWCSNDYLGMG QNAEVLAAMHRSIDLSGAGTGGTRNISGTNRQHVALEAELADLHGKESALIFTSGWISNL AALGTLGKILPECAIFSDALNHNSMIEGIRRSGAERFIFHHNDPVHLDRLLSSVDPARPK IVAFESVYSMDGDIAPIAEICDVAERHGALTYLDEVHAVGLYGPRGGGISDRDGLADRVT IIEGTLAKAFGVMGGYVSGPSLLMDVIRSMSDSFIFTTSICPHLAAGALAAVRHVKAHPD ERRRQAENAVRLKVLLQKAGLPVLDTPSHILPVMVGEAHLCRSISEALLARHAIYVQPIN YPTVARGQERFRLTPTPFHTTSHMEALVEALLAVGRDLGWAMSRRAA SWISSPROT:HEM0_OPSTA ID HEM0_OPSTA STANDARD; PRT; 582 AA. AC P43090; 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 5-AMINOLEVULINIC ACID SYNTHASE MITOCHONDRIAL PRECURSOR, ERYTHROID- DE SPECIFIC (EC 2.3.1.37) (DELTA-AMINOLEVULINATE SYNTHASE) (DELTA-ALA DE SYNTHETASE) (ALAS-E). OS OPSANUS TAU (OYSTER TOADFISH). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; PISCES; GNATHOSTOMATA; OC OSTEICHTHYES; ACTINOPTERYGII; BATRACHOIDIFORMES. RN [1] RP SEQUENCE FROM N.A. RA HELLMICH H.L., CORNELL N.W.; RL SUBMITTED (XXX-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- THERE ARE TWO DELTA-ALA SYNTHETASE IN VERTEBRATES: AN ERYTHROID- CC SPECIFIC FORM AND ONE (HOUSEKEEPING) WHICH IS EXPRESSED IN ALL CC TISSUES. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; L02632; G213491; -. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; MITOCHONDRION; KW TRANSIT PEPTIDE; PYRIDOXAL PHOSPHATE; MULTIGENE FAMILY. FT TRANSIT 1 ? MITOCHONDRION (POTENTIAL). FT CHAIN ? 582 5-AMINOLEVULINIC ACID SYNTHASE. FT BINDING 386 386 PYRIDOXAL PHOSPHATE (PROBABLE). SQ SEQUENCE 582 AA; 64531 MW; FDFAC5A4 CRC32; >HEM0_OPSTA MAAFLHHCPFLKSMPKPALRRRVPALLSLADRCPVIVHQVCISRLHILETKLDVSPTQPK RQRLSLLDQKRLFAQTATQVAVSVSKGCPFVSSQIGMVRASPEVQEDVQADLKSPVLPTP PQTGITQLLKDNMVGPSFDYDNFFNEKIAEKKRDHTYRVFKTVNRNAVVFPFAEDYSVSD RQGSQVSVWCSNDYLGMSRHPRVLEAIREVLERHGAGAGGTRNISGTSKYHVTLEKELAH LHQKDAALVFSSCFVANDSTLFTLAKMLPGCHIYSDAGNHASMIQGIRNSGAKRFIFRHN DSRHLEELLQQSDPKTPKIVAFETVHSMDGAICPLEELCDVAHRHGALTFVDEVHAVGLY GAHGAGVGERDNVMHKIDIVSGTLGKAFGCVGGYVASSAALVDTVRSFAAGFIFTTSLPP MILAGALESVRVLKSPEGQLLRRAHQRNVKYMRQLLMDKGLPVVNCPSHIIPIRVGNAEL NTKVCDSLLEKHNIYVQAINYPTVPRGQELLRLAPSPHHHPAMMEYFVDKLVEVWQEAGL LLNGPATVSCTFCDRPLHFDLMSEWEKSYFGNMEPQYITMSA SWISSPROT:HEM0_MOUSE ID HEM0_MOUSE STANDARD; PRT; 572 AA. AC P08680; DT 01-JAN-1988 (REL. 06, CREATED) DT 01-AUG-1991 (REL. 19, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE 5-AMINOLEVULINIC ACID SYNTHASE MITOCHONDRIAL PRECURSOR, ERYTHROID- DE SPECIFIC (EC 2.3.1.37) (DELTA-AMINOLEVULINATE SYNTHASE) (DELTA-ALA DE SYNTHETASE) (ALAS-E). OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RX MEDLINE; 87163516. RA SCHOENHAUT D.S., CURTIS P.J.; RL GENE 48:55-63(1986). RN [2] RP PYRIDOXAL-PHOSPHATE BINDING SITE. RX MEDLINE; 94093402. RA FERREIRA G.C., NEAME P.J., DAILEY H.A.; RL PROTEIN SCI. 2:1959-1965(1993). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- TISSUE SPECIFICITY: ERYTHROID-SPECIFIC. CC -!- THERE ARE TWO DELTA-ALA SYNTHETASE IN VERTEBRATES: AN ERYTHROID- CC SPECIFIC FORM AND ONE (HOUSEKEEPING) WHICH IS EXPRESSED IN ALL CC TISSUES. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; M15268; G387096; ALT_INIT. DR PIR; A29040; SYMSAL. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; MITOCHONDRION; KW TRANSIT PEPTIDE; PYRIDOXAL PHOSPHATE; MULTIGENE FAMILY. FT TRANSIT 1 ?49 MITOCHONDRION (POTENTIAL). FT CHAIN ?50 572 5-AMINOLEVULINIC ACID SYNTHASE. FT BINDING 376 376 PYRIDOXAL PHOSPHATE. FT MUTAGEN 376 376 K->A,H: ABOLISHES ENZYME ACTIVITY. SQ SEQUENCE 572 AA; 63230 MW; 681D276A CRC32; >HEM0_MOUSE MVAAAMLLWSCPVLSQGPTGLLGKVAKTYQFLFSIGRCPILATQGPTCSQIHLKATKAGG ELQDRKSKIVQRAAPEVQEDVKTFKTDLLSTMDSTTRSHSFPSFQEPEQTEGAVPHLIQN NMTGSQAFGYDQFFRDKIMEKKQDHTYRVFKTVNRWANAYPFAQHFSEASMASKDVSVWC SNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLF SSCFVANDSTLFTLAKLLPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPGHLKKLLE KSDPKTPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGAWGAGIGER DGIMHKLDIISGTLGKAFGCVGGYIASTWDLVDMVRSYAAGFIFTTSLPPMMLSGALESV RLLKGEEGQALRWAHQRNVKHMRQLLMDRGFPVIPCPSHIIPIRVGNAALNSKICDLLLS KHSIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTEVGLPLQDVSVAAC NFCHRPVHFELMSEWERSYFGNMGPQYVTTYA SWISSPROT:HEM0_HUMAN ID HEM0_HUMAN STANDARD; PRT; 587 AA. AC P22557; DT 01-AUG-1991 (REL. 19, CREATED) DT 01-AUG-1991 (REL. 19, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE 5-AMINOLEVULINIC ACID SYNTHASE MITOCHONDRIAL PRECURSOR, ERYTHROID- DE SPECIFIC (EC 2.3.1.37) (DELTA-AMINOLEVULINATE SYNTHASE) (DELTA-ALA DE SYNTHETASE) (ALAS-E). GN ALAS2 OR ALASE OR ASB. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RX MEDLINE; 91088347. RA BISHOP D.F.; RL NUCLEIC ACIDS RES. 18:7187-7188(1990). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RX MEDLINE; 91266919. RA COX T.C., BAWDEN M.J., MARTIN A., MAY B.K.; RL EMBO J. 10:1891-1902(1991). RN [3] RP VARIANT XLSA SER-388. RX MEDLINE; 94150519. RA COX T.C., BOTTOMLEY S.S., WILEY J.S., BAWDEN M.J., MATTHEWS C.S., RA MAY B.K.; RL NEW ENGL. J. MED. 330:675-679(1994). RN [4] RP VARIANT XLSA ASN-476. RX MEDLINE; 92237301. RA COTTER P.D., BAUMANN M., BISHOP D.F.; RL PROC. NATL. ACAD. SCI. U.S.A. 89:4028-4032(1992). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- TISSUE SPECIFICITY: ERYTHROID-SPECIFIC. CC -!- THERE ARE TWO DELTA-ALA SYNTHETASE IN VERTEBRATES: AN ERYTHROID- CC SPECIFIC FORM AND ONE (HOUSEKEEPING) WHICH IS EXPRESSED IN ALL CC TISSUES. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -!- DISEASE: DEFECTS IN ALAS2 ARE THE CAUSE OF X-LINKED SIDEROBLASTIC CC ANEMIA (XLSA). DR EMBL; X56352; G28586; ALT_INIT. DR PIR; S13683; S13683. DR PIR; S16347; S16347. DR MIM; 301300; -. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; MITOCHONDRION; KW TRANSIT PEPTIDE; PYRIDOXAL PHOSPHATE; MULTIGENE FAMILY; KW DISEASE MUTATION. FT TRANSIT 1 ?49 MITOCHONDRION. FT CHAIN ?50 587 5-AMINOLEVULINIC ACIS SYNTHASE. FT BINDING 391 391 PYRIDOXAL PHOSPHATE (PROBABLE). FT VARIANT 388 388 T -> S (IN XLSA). FT VARIANT 476 476 I -> N (IN XLSA). SQ SEQUENCE 587 AA; 64693 MW; 8B93335F CRC32; >HEM0_HUMAN MVTAAMLLQCCPVLARGPTSLLGKVVKTHQFLFGIGRCPILATQGPNCSQIHLKATKAGG DSPSWAKGHCPFMLSELQDGKSKIVQKAAPEVQEDVKAFKTDLPSSLVSVSLRKPFSGPQ EQEQISGKVTHLIQNNMPGNYVFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQH FFEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELE QELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKF VFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVH AVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT TSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRV GNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAW TAVGLPLQDVSVAACNFCRRPVHFELMSEWERSYFGNMGPQYVTTYA SWISSPROT:HEM0_CHICK ID HEM0_CHICK STANDARD; PRT; 513 AA. AC P18080; 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 5-AMINOLEVULINIC ACID SYNTHASE MITOCHONDRIAL PRECURSOR, ERYTHROID- DE SPECIFIC (EC 2.3.1.37) (DELTA-AMINOLEVULINATE SYNTHASE) (DELTA-ALA DE SYNTHETASE) (ALAS-E). GN ALASE. OS GALLUS GALLUS (CHICKEN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; AVES; NEOGNATHAE; OC GALLIFORMES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=ERYTHROID; RX MEDLINE; 89128863. RA RIDDLE R.D., YAMAMOTO M., ENGEL J.D.; RL PROC. NATL. ACAD. SCI. U.S.A. 86:792-796(1989). CC -!- CATALYTIC ACTIVITY: SUCCINYL-COA + GLYCINE = 5-AMINOLEVULINATE + CC COA + CO(2). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST AND RATE-LIMITING STEP IN HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL MATRIX. CC -!- TISSUE SPECIFICITY: ERYTHROID-SPECIFIC. CC -!- THERE ARE TWO DELTA-ALA SYNTHETASE IN VERTEBRATES: AN ERYTHROID- CC SPECIFIC FORM AND ONE (HOUSEKEEPING) WHICH IS EXPRESSED IN ALL CC TISSUES. CC -!- SIMILARITY: BELONGS TO CLASS-II OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. DR EMBL; M24367; G517499; -. DR PIR; A31452; SYCHLE. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2. KW HEME BIOSYNTHESIS; TRANSFERASE; ACYLTRANSFERASE; MITOCHONDRION; KW TRANSIT PEPTIDE; PYRIDOXAL PHOSPHATE; MULTIGENE FAMILY. FT TRANSIT 1 18 MITOCHONDRION (POTENTIAL). FT CHAIN 19 513 5-AMINOLEVULINIC ACID SYNTHASE. FT BINDING 323 323 PYRIDOXAL PHOSPHATE (PROBABLE). SQ SEQUENCE 513 AA; 54777 MW; 945858E2 CRC32; >HEM0_CHICK MAAFLRCPLLARHPPLARAFATGARCPFMGFAHRAAPELQEDVERPQIPAVEVLEELLRD GGAALNRTVRDCMDEDAFPYEEQFQAQLGALRRTHTYRVVTAVGRRADAPPLGTRGTAPH TSVELWCSSDYLGLSRHPAVLRAARAALDAHGLGAGGTRNIGGTSPLHGALERALALLHR QPRAALFSSCFAANDTALDTLARILPGCQVYSDAGNHASMIQGIRRRGVPKFIFRHNDPH HLEQLLGRSPPGVPKIVAFESLHSMDGSIAPLEELCDVAHAYGALTFVDEVHAVGLYGAR GAGIAERDGVQHKVDVVSGTLGKALGAVGGYIAGSEALVDAVRSLGPGFIFTTALPPQRG GGALAALQVVGSAEGAALRRAHQRHAKHLRVLLRDRGLPALPSHIVPVRWDAEANTRLSR ALLEEHGLYVQAINHPTVPRGQELLLRIAPTPHHSPPMLENLADKLSECWGAVGLPREDP PGPSCSSCHRPLHLSLLSPLERDQFGVRGAAAG