PIR:S53487 >P1;S53487 porphobilinogen synthase (EC 4.2.1.24) precursor - Chlamydomonas reinhardtii N;Alternate names: delta-aminolevulinic acid dehydratase C;Species: Chlamydomonas reinhardtii C;Date: 14-Jul-1995 #sequence_revision 21-Jul-1995 #text_change 03-May-1996 C;Accession: S53487 R;Matters, G.L.; Beale, S.I. Plant Mol. Biol. 27, 607-617, 1995 A;Title: Structure and expression of the Chlamydomonas reinhardtii alad gene encoding the chlorophyll biosynthetic enzyme, delta-aminolevulinic acid dehydratase (porphobilinogen synthase). A;Reference number: S53487 A;Accession: S53487 A;Status: preliminary A;Molecule type: mRNA A;Residues: 1-390 A;Cross-references: EMBL:U19876 C;Superfamily: porphobilinogen synthase C;Keywords: carbon-oxygen lyase; hydro-lyase >S53487 MQMMQRNVVGQRPVAGSRRSLVVANVAEVTRPAVSTNGKHRTGVPEGTPIVTPQDLPSRP RRNRRSESFRASVREVNVSPANFILPIFIHEESNQNVPIASMPGINRLAYGKNVIDYVAE PRSYGVNQVVVFPKTPDHLKTQTAEEAFNKNGLSQRTIRLLKDSFPDLEVYTDVALDPYN SDGHDGIVSDAGVILNDETIEYLCRQAVSQAEAGADVVSPSDMMDGRVGAIRRALDREGF TNVSIMSYTAKYASAYYGPFRDALASAPKPGQAHRRIPPNKKTYQMDPANYREAIREAKA DEAEGADIMMVKPGMPYLDVVRLLRETSPLPVAVYHVSGEYAMLKAAAERGWLNEKDAVL EAMTCFRRAGGDLILTYYGIEASKWLAGEK PIR:A49925 >P1;A49925 delta-aminolevulinic acid dehydratase - Bradyrhizobium japonicum C;Species: Bradyrhizobium japonicum C;Date: 11-Nov-1994 #sequence_revision 11-Nov-1994 #text_change 03-May-1996 C;Accession: A49925 R;Chauhan, S.; O'Brian, M.R. J. Bacteriol. 175, 7222-7227, 1993 A;Title: Bradyrhizobium japonicum delta-aminolevulinic acid dehydratase is essential for symbiosis with soybean and contains a novel metal-binding domain. A;Reference number: A49925 A;Accession: A49925 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-353 A;Cross-references: GB:L24386 C;Genetics: A;Gene: hemB C;Superfamily: porphobilinogen synthase C;Keywords: heme biosynthesis; magnesium >A49925 MAIKYGRPIELREVSRRDGAAASPALDLAIRPRRNRKAEWARRMVRENVLTTDDLIWPLF LIDGNNKREQIASMPGVERLSVDQAVREAERAMKLTIPCIALFPYTDPSLRDEEGSEACN PNNLVCQAVRAIKKEFPEIGVLCDVALDPFTSHGHDGLIADGAILNDETVAVLVRQALVQ AEAGCDIIAPSDMMDGRVAAIREGLDQAGLIDVQIMAYAAKYASAFYGPFRDAIGSAKTL TGDKRTYQMDSANTDEALREVELDISEGADMVMVKPGMPYLDVVRRVKDTFAMPTFAYQV SGEYAMIAAAAGNGWLDGDRAMMESLLAFKRAGADGVLSYFAPKAAEKLRTQG PIR:A24724 >P1;A24724 porphobilinogen synthase (EC 4.2.1.24) - rat C;Species: Rattus norvegicus (Norway rat) C;Date: 05-Oct-1988 #sequence_revision 05-Oct-1988 #text_change 18-Jun-1993 C;Accession: A24724 R;Bishop, T.R.; Frelin, L.P.; Boyer, S.H. Nucleic Acids Res. 14, 10115, 1986 A;Title: Nucleotide sequence of rat liver delta-aminolevulinic acid dehydratase cDNA. A;Reference number: A24724; MUID:87117513 A;Accession: A24724 A;Molecule type: mRNA A;Residues: 1-330 C;Superfamily: porphobilinogen synthase C;Keywords: carbon-oxygen lyase; hydro-lyase; porphyrin biosynthesis >A24724 MHHQSVLHSGYFHPLLRAWQTTPSTVSATNLIYPIFVTDVPDDVQPIASLPGVARYGVNQ LEEMLRPLVEAGLRCVLIFGVPSRVPKDEQGSAADSEDSPTIEAVRLLRKTFPTLLVACD VCLCPYTSHGHCGLLSENGAFLAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKA ALLKHGLGNRVSVMSYSAKFASCFYGPFRDAAQSSPAFGDRRCYQLPPGARGLALRAVAR DIQEGADILMVKPGLPYLDMVQEVKDKHPELPLAVYQVSGEFAMLWHGAKAGAFDLRTAV LESMTAFRRAGADIIITYFAPQLLKWLKEE SWISSPROT:HEM2_YEAST ID HEM2_YEAST STANDARD; PRT; 342 AA. AC P05373; DT 01-NOV-1988 (REL. 09, CREATED) DT 01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) (PORPHOBILINOGEN DE SYNTHASE) (ALADH). GN HEM2 OR YGL040C. OS SACCHAROMYCES CEREVISIAE (BAKER'S YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 88059078. RA MYERS A.M., CRIVELLONE M.D., KOERNER T.J., TZAGOLOFF A.; RL J. BIOL. CHEM. 262:16822-16829(1987). RN [2] RP SEQUENCE FROM N.A. RA HEBLING U., HOFMANN B., DELIUS H.; RL SUBMITTED (MAY-1996) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [3] RP SEQUENCE OF 1-41 FROM N.A. RA FEUERMANN M., POTIER S., SOUCIET J.L.; RL SUBMITTED (MAY-1996) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER. CC -!- COFACTOR: ZINC. DR EMBL; J03493; G171664; -. DR EMBL; Z72562; E243278; -. DR PIR; A28465; A28465. DR LISTA; SC00431; HEM2. DR SGD; L0000761; HEM2. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; LYASE; ZINC. FT DOMAIN 130 143 ZINC-BINDING (BY SIMILARITY). FT ACT_SITE 263 263 FT CONFLICT 291 291 G -> D (IN REF. 1). SQ SEQUENCE 342 AA; 37740 MW; 708D318A CRC32; >HEM2_YEAST MHTAEFLETEPTEISSVLAGGYNHPLLRQWQSERQLTKNMLIFPLFISDNPDDFTEIDSL PNINRIGVNRLKDYLKPLVAKGLRSVILFGVPLIPGTKDPVGTAADDPAGPVIQGIKFIR EYFPELYIICDVCLCEYTSHGHCGVLYDDGTINRERSVSRLAAVAVNYAKAGAHCVAPSD MIDGRIRDIKRGLINANLAHKTFVLSYAAKFSGNLYGPFRDAACSAPSNGDRKCYQLPPA GRGLARRALERDMSEGADGIIVKPSTFYLDIMRDASEICKDLPICAYHVSGEYAMLHAAA EKGVVDLKTIAFESHQGFLRAGARLIITYLAPEFLDWLDEEN SWISSPROT:HEM2_SYNP7 ID HEM2_SYNP7 STANDARD; PRT; 326 AA. AC P43087; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) (PORPHOBILINOGEN DE SYNTHASE) (ALAD) (ALADH). GN HEMB. OS SYNECHOCOCCUS SP. (STRAIN PCC 7942) (ANACYSTIS NIDULANS R2). OC PROKARYOTA; GRACILICUTES; OXYPHOTOBACTERIA; OC CYANOBACTERIA (BLUE-GREEN ALGAE); CHROOCOCCALES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 94169298. RA JONES M.C., JENKINS J.M., SMITH A.G., HOWE C.J.; RL PLANT MOL. BIOL. 24:435-448(1994). CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: ZINC. DR EMBL; X70434; G471288; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; LYASE; ZINC. FT DOMAIN 116 129 ZINC-BINDING (BY SIMILARITY). FT ACT_SITE 251 251 BY SIMILARITY. SQ SEQUENCE 326 AA; 35659 MW; 98C29A4F CRC32; >HEM2_SYNP7 MFPTHRPRRLRSSETLRRMVRETTLTSADFIYPLFAVPGEGVAKEVTSMPGVYQLSIDKI VEEAKEVYDLGIPSIILFGIPTDKDNDATGAWHDCGIVQKAATAVKEAVPELIVAADTCL CEYTPHGHCGYLEVGDLSGRVLNDPTLELLRKTAVSQAKAGADIIAPSGMMDGFVATIRD ALDEAGFSDTPIMAYSAKYASAYYGPFRDAAESTPQFGDRRTYQMDPGNSREALKEVELD VAEGADIVMVKPALSYMDIICRIKETTDLPVAAYNVSGEYSMVKAARLNGWIDEERVVLE TLTSFKRAGADLILTYHAKDAARWLA SWISSPROT:HEM2_STRCO ID HEM2_STRCO STANDARD; PRT; 330 AA. AC P54919; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) (PORPHOBILINOGEN DE SYNTHASE) (ALAD) (ALADH). GN HEMB. OS STREPTOMYCES COELICOLOR. OC PROKARYOTA; FIRMICUTES; ACTINOMYCETALES; STREPTOMYCETACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=A3(2); RA PETRICEK M.; RL SUBMITTED (JAN-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + 2 CC H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: ZINC. DR EMBL; U19249; G625074; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW LYASE; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; ZINC. FT DOMAIN 124 137 ZINC-BINDING (BY SIMILARITY). FT ACT_SITE 255 255 BY SIMILARITY. SQ SEQUENCE 330 AA; 35437 MW; B239A8C3 CRC32; >HEM2_STRCO MTTYGSFPGARPRRLRTTPVMRRMVAETRLHPADFILPAFVREGVSEPVPIAAMPGVVQH TRDTLKKAAAEAVEAGVSGIMLFGVPEDGKKDAAGTAGTVPDGILQVALRDVRAEVGDEL LVMSDLCLDEFTDHGHCGVLDGQGRVDNDATLERYAEMAQVQADAGAHVVGPSGMMDGQI GVIRDALDQIGREDVAILAYTAKYASAFYGPFREAVGSSLKGDRKTYQQDSANARESLRE LALDLEEGADMVMVKPAGPYLDILAKVAEASDVPVAAYQISGEYSMIEAAAEKGWIDRDR AILESLTGIKRAGARNILTYWATEVARTLR SWISSPROT:HEM2_STAAU ID HEM2_STAAU STANDARD; PRT; 323 AA. AC P50915; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) (PORPHOBILINOGEN DE SYNTHASE) (ALAD) (ALADH). GN HEMB. OS STAPHYLOCOCCUS AUREUS. OC PROKARYOTA; FIRMICUTES; COCCI; MICROCOCCACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SA1959; RX MEDLINE; 95007251. RA KAFALA B., SASARMAN A.; RL CAN. J. MICROBIOL. 40:651-657(1994). CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + 2 CC H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: ZINC. DR EMBL; S72488; G632816; -. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; LYASE; ZINC. FT DOMAIN 115 128 ZINC-BINDING (BY SIMILARITY). FT ACT_SITE 248 248 BY SIMILARITY. SQ SEQUENCE 323 AA; 36453 MW; 71A0E3A0 CRC32; >HEM2_STAAU MKFDRHRRLRSSATMRDMVRENHVRKEDLIYPIFVVEKDDVKKEIKSLPGVYQISLNLLE SELKEAYDLGIRAIMFFGVPNSKDDIGTGAYIHDGVIQQATRIAKKMYDDLLIVADTCLC EYTDHGHCGVIDDHTHDVDNDKSLPLLVKTAISQVEAGADIIAPSNMMDGFVAEIRRGLD EAGYYNIPIMSYGVKYASSFFGPFRDAADSAPSFGDRKTYQMDPANRLEALRELESDLKE GCDMMIVKPALSYLDIVRDVKNHTNVPVVAYNVSGEYSMTKAAAQNGWIDEERVVMEQMV SMKRAGADMIITYCKDICRYLDN SWISSPROT:HEM2_SPIOL ID HEM2_SPIOL STANDARD; PRT; 433 AA. AC P24493; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE PRECURSOR (EC 4.2.1.24) DE (PORPHOBILINOGEN SYNTHASE) (ALDH) (ALAD). GN ALA1. OS SPINACIA OLERACEA (SPINACH). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; OC CARYOPHYLLALES; CHENOPODIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. AESTIVATO; RX MEDLINE; 92304405. RA SCHAUMBURG A., SCHNEIDER-POETSCH H.J.A.W.; RL Z. NATURFORSCH., C, BIOSCI. 47:77-84(1991). CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: MAGNESIUM. CC -!- SUBCELLULAR LOCATION: CHLOROPLAST. DR EMBL; X57842; G805062; -. DR PIR; A50000; A50000. DR PIR; S16786; S16786. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; LYASE; MAGNESIUM; KW CHLOROPLAST; TRANSIT PEPTIDE. FT TRANSIT 1 64 CHLOROPLAST. FT CHAIN 65 433 DELTA-AMINOLEVULINIC ACID DEHYDRATASE. FT ACT_SITE 354 354 BY SIMILARITY. SQ SEQUENCE 433 AA; 47321 MW; ECEA8465 CRC32; >HEM2_SPIOL MASTFNIPCNAGTIKNFNNSQRNLGFSSNLGINFAKTRFSNCGDSGRIPSQLVVRASERR DNLTQQKTGLSIEECEAAVVAGNAPSAPPVPPTPKAPSGTPSVSPLSLGRRPRRNRTSPV FRAAFQETTLSPANVVYPLFIHEGEEDTPIGAMPGCYRLGWRHGLVEEVAKARDVVVNSI VVFPKPDALKSPTGDEAYNENGLVPRTIRMLKDKFPDLIIYTDVALDPYYYDGHDGIVTQ HGVIMNDETVHQLCKQAVAQARAGADVVSPSDMMDGRVGAIRAALDAEGYSNVSIMSYTA KYASSFYGPFREALDSNPRFGDKKTYQMNPANYREALIETQEDESEGADILLVKPGLPYL DIIRLLRDNSDLPIAAYQVSGEYSMIKAGGVLKMIDEEKVMLESLLCLRRAGADIILTYF ALQAARCLCGEKR SWISSPROT:HEM2_SOYBN ID HEM2_SOYBN STANDARD; PRT; 412 AA. AC P43210; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE PRECURSOR (EC 4.2.1.24) DE (PORPHOBILINOGEN SYNTHASE) (ALADH). GN ALAD. OS GLYCINE MAX (SOYBEAN). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; FABALES; OC FABACEAE. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LEAF; RX MEDLINE; 94286747. RA KACZOR C.M., SMITH M.W., SANGWAN I., O'BRIAN M.R.; RL PLANT PHYSIOL. 104:1411-1417(1994). CC -!- FUNCTION: IS COMMITED TO PLANT TETRAPYRROLE SYNTHESIS. CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: MAGNESIUM. CC -!- SUBCELLULAR LOCATION: CHLOROPLAST. CC -!- TISSUE SPECIFICITY: LEAVES AND ROOT NODULES. DR EMBL; U04525; G468000; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; LYASE; MAGNESIUM; KW CHLOROPLAST; TRANSIT PEPTIDE. FT TRANSIT 1 48 CHLOROPLAST (POTENTIAL). FT CHAIN 49 412 DELTA-AMINOLEVULINIC ACID DEHYDRATASE. FT ACT_SITE 333 333 BY SIMILARITY. SQ SEQUENCE 412 AA; 45067 MW; 27D4D756 CRC32; >HEM2_SOYBN MASSIPNAPSAFNSQSYVGLRAPLRTFNFSSPQAAKIPRSQRLFVVRASDSEFEAAVVAG KVPPAPPVRPRPAAPVGTPVVPSLPLHRRPRRNRKSPALRSAFQETSISPANFVYPLFIH EGEEDTPIGAMPGCYRLGWRHGLVEEVAKARDVGVNSVVLFPKIPDALKSPTGDEAYNEN GLVPRTIRLLKDKYPDLVIYTDVALDPYSSDGHDGIVREDGVIMNDETVHQLCKQAVAQA QAGADVVSPSDMMDGRVGALRAALDAEGFQHVSIMSYTAKYASSFYGPFREALDSNPRFG DKKTYQMNPANYREALTEMREDESEGADILLVKPGLPYLDIIRLLRDNSPLPIAAYQVSG EYAMIKAAGALKMIDEEKVMMESLMCLRRAGADIILTYSALQAARCLCGEKR SWISSPROT:HEM2_SELMA ID HEM2_SELMA STANDARD; PRT; 417 AA. AC P45623; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE PRECURSOR (EC 4.2.1.24) DE (PORPHOBILINOGEN SYNTHASE) (ALDH) (ALAD). GN ALA2. OS SELAGINELLA MARTENSII (MARTENS'S SPIKE MOSS). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; LYCOPODIOPHYTA; ISOETOPSIDA. RN [1] RP SEQUENCE FROM N.A. RA SOLLBACH M., SCHNEIDER-POETSCH H.J.A.W.; RL SUBMITTED (SEP-1993) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: MAGNESIUM. CC -!- SUBCELLULAR LOCATION: CHLOROPLAST. DR EMBL; X75043; G404169; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; LYASE; MAGNESIUM; KW CHLOROPLAST; TRANSIT PEPTIDE. FT TRANSIT 1 40 CHLOROPLAST (POTENTIAL). FT CHAIN 41 417 DELTA-AMINOLEVULINIC ACID DEHYDRATASE. FT ACT_SITE 339 339 BY SIMILARITY. SQ SEQUENCE 417 AA; 45182 MW; 27B276C9 CRC32; >HEM2_SELMA MAALLVPGGGAAPGLVWRRRRAAVQCAAASPSSPDPSWRTNVVSDRVSVEPSPRTIHECE ADVVSGNPPAAPAAPAKAKAPPGTPVVKPLRLTSRPRRNRKSAALRDAFQETTLTPANFI LPLFIHEGEEDSPIGAMPGCSRLGWRHGLIDEVYKARDVGVNSVVLFPKIPDALKSSTGD EAYNPDGLVPRAIRTLKDKFPDLVIYTDVALDPYSSDGHDGIVREDGVIMNDETVHQLCK QAVAQAEAGADVVSPSDMMDGRVGAIRTALDEAGYYHVSIMAYTAKYASAFYEPFREELD SNPRFGDKKTYQMNPENYREALLEVHADESEGADILMVKPAMPYLHVIRLLRDTSALPIS AYQVSGEYSMIKAAASQGMLDEKKAILESLLCIKRAGADVILTYAALQAARWLCGEK SWISSPROT:HEM2_RHOCA ID HEM2_RHOCA STANDARD; PRT; 332 AA. AC P42504; DT 01-NOV-1995 (REL. 32, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) (PORPHOBILINOGEN DE SYNTHASE) (ALAD) (ALADH). GN HEMB. OS RHODOBACTER CAPSULATUS (RHODOPSEUDOMONAS CAPSULATA). OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; PURPLE BACTERIA; OC RHODOSPIRILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=PAS100; RX MEDLINE; 95303969. RA INDEST K., BIEL A.J.; RL PLANT PHYSIOL. 108:421-421(1995). CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN HEME BIOSYNTHESIS. CC -!- COFACTOR: MAGNESIUM (BY SIMILARITY). DR EMBL; U14593; G555920; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW HEME BIOSYNTHESIS; LYASE; MAGNESIUM. FT ACT_SITE 256 256 BY SIMILARITY. SQ SEQUENCE 332 AA; 35854 MW; D7E95440 CRC32; >HEM2_RHOCA MTLITPPFPTNRLRRMRRTEALRDLAQENRLSVKDLIWPIFITDVPGADVEISSMPGVVR RTMDGALKAAEGSRDAGHSRDLPVPLTDPAVKTETCEMAWQPDNFTNRVIAAMKQAVPEV AIMTDIALDPYNANGHDGLVRDGILLNDETTEALVKMALAQAAAGADILGPSDMMDGRVG AIRQAMEAAGHKDIAILSYAAKYASAFYGPFRDAVGASSALKGDKKTYQMNPANSAEALR NVARDIAEGADMVMVKPGMPYLDIVRQVKDAFGMPTYAYQVSGEYAMLMAAVQNGWLNHD KVMLESLMAFRRAGCDGVLTYFAPAAAKLIGA SWISSPROT:HEM2_RAT ID HEM2_RAT STANDARD; PRT; 330 AA. AC P06214; DT 01-JAN-1988 (REL. 06, CREATED) DT 01-JAN-1988 (REL. 06, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) (PORPHOBILINOGEN DE SYNTHASE) (ALADH). GN ALAD. 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; 87117513. RA BISHOP T.R., FRELIN L.P., BOYER S.H.; RL NUCLEIC ACIDS RES. 14:10115-10115(1986). CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER. CC -!- COFACTOR: ZINC. DR EMBL; X04959; G55626; -. DR PIR; A24724; A24724. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; LYASE; ZINC. FT DOMAIN 119 132 ZINC-BINDING (BY SIMILARITY). FT ACT_SITE 252 252 BY SIMILARITY. SQ SEQUENCE 330 AA; 36031 MW; C3920709 CRC32; >HEM2_RAT MHHQSVLHSGYFHPLLRAWQTTPSTVSATNLIYPIFVTDVPDDVQPIASLPGVARYGVNQ LEEMLRPLVEAGLRCVLIFGVPSRVPKDEQGSAADSEDSPTIEAVRLLRKTFPTLLVACD VCLCPYTSHGHCGLLSENGAFLAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKA ALLKHGLGNRVSVMSYSAKFASCFYGPFRDAAQSSPAFGDRRCYQLPPGARGLALRAVAR DIQEGADILMVKPGLPYLDMVQEVKDKHPELPLAVYQVSGEFAMLWHGAKAGAFDLRTAV LESMTAFRRAGADIIITYFAPQLLKWLKEE SWISSPROT:HEM2_PEA ID HEM2_PEA STANDARD; PRT; 398 AA. AC P30124; DT 01-APR-1993 (REL. 25, CREATED) DT 01-APR-1993 (REL. 25, LAST SEQUENCE UPDATE) DT 01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE DELTA-AMINOLEVULINIC ACID DEHYDRATASE PRECURSOR (EC 4.2.1.24) DE (PORPHOBILINOGEN SYNTHASE) (ALADH) (FRAGMENT). GN ALAD. OS PISUM SATIVUM (GARDEN PEA). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; FABALES; OC FABACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 91373313. RA BOESE Q.F., SPANO A.J., LI J., TIMKO M.P.; RL J. BIOL. CHEM. 266:17060-17066(1991). CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: MAGNESIUM. CC -!- SUBCELLULAR LOCATION: CHLOROPLAST. DR EMBL; M71235; G169031; -. DR PIR; A40966; A40966. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; LYASE; MAGNESIUM; KW CHLOROPLAST; TRANSIT PEPTIDE. FT NON_TER 1 1 FT TRANSIT 1 ? CHLOROPLAST. FT CHAIN ? 398 DELTA-AMINOLEVULINIC ACID DEHYDRATASE. FT ACT_SITE 319 319 BY SIMILARITY. SQ SEQUENCE 398 AA; 43815 MW; 7BC7F977 CRC32; >HEM2_PEA HTFVDLKSPFTLSNYLSFSSSKRRQPPSLFTVRASDSDFEAAVVAGKVPEAPPVPPTPAS PAGTPVVPSLPIQRRPRRNRRSPALRSAFQETTLSPANFVYPLFIHEGEEDTPIGAMPGC YRLGWRHGLLEEVAKARDVGVNSVVLFPKIPDALKTPTGDEAYNEDGLVPRSIRLLKDKY PDLIIYTDVALDPYSSDGHDGIVREDGVIMNDETVHQLCKQAVAQARAGADVVSPSDMMD GRVGAMRVALDAEGFQHVSIMSYTAKYASSFYGPFREALDSNPRFGDKKTYQMNPANYRE ALTEMREDESEGADILLVKPGLPYLDIIRLLRDNSPLPIAAYQVSGEYSMIKAGGALKMI DEEKVMMESLLCLRRAGADIILTYFALQAARTLCGEKR SWISSPROT:HEM2_MYCLE ID HEM2_MYCLE STANDARD; PRT; 329 AA. AC P46723; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) (PORPHOBILINOGEN DE SYNTHASE) (ALAD) (ALADH). GN HEMB OR B2168_C3_264. 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: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: ZINC (BY SIMILARITY). DR EMBL; U00018; G467062; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; LYASE; ZINC. FT DOMAIN 123 136 ZINC-BINDING (BY SIMILARITY). FT ACT_SITE 254 254 BY SIMILARITY. SQ SEQUENCE 329 AA; 34775 MW; DE1BA1B1 CRC32; >HEM2_MYCLE MSVSGYPRHRPRRLRSTPAMRRLVAQTSLEPRNLVLPMFVADGIDELRPIASMPGVVQHT RDSLRRAAVAAVDAGVGGLNLFGVPRDQDKDATGSAGVDPDGILNVALRDLAEDLGDATV LMADTCLDEFTDHGHCGVLDGQGRVDNDATVARYVELAVAQAESGANVVGPSGMMDGQIG ALRDGLDSAGYADVAILAYAAKFSSAFYGPFREAVSCSLSGDRRTYQQEPGNAREALREI KLDLDEGADIIMIKPASGYLDVVATAAGVSPVPVAAYQVSGEYAMICAAAANNWIDERAA VLESLTSIRRAGADIVFTYWAADVACWLS SWISSPROT:HEM2_MOUSE ID HEM2_MOUSE STANDARD; PRT; 330 AA. AC P10518; DT 01-JUL-1989 (REL. 11, CREATED) DT 01-JUL-1989 (REL. 11, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) (PORPHOBILINOGEN DE SYNTHASE) (ALADH). GN ALAD OR LV. OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BALB/C; RX MEDLINE; 89160346. RA BISHOP T.R., HODES Z.I., FRELIN L.P., BOYER S.H.; RL NUCLEIC ACIDS RES. 17:1775-1775(1989). CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER. CC -!- COFACTOR: ZINC. DR EMBL; X13752; G52952; -. DR PIR; S03187; S03187. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; LYASE; ZINC. FT DOMAIN 119 132 ZINC-BINDING (BY SIMILARITY). FT ACT_SITE 252 252 BY SIMILARITY. SQ SEQUENCE 330 AA; 36023 MW; 6A0998C6 CRC32; >HEM2_MOUSE MHHQSVLHSGYFHPLLRSWQTAASTVSASNLIYPIFVTDVPDDVQPIASLPGVARYGVNQ LEEMLRPLVEAGLRCVLIFGVPSRVPKDEQGSAADSEDSPTIEAVRLLRKTFPSLLVACD VCLCPYTSHGHCGLLSENGAFLAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKA ALLKHGLGNRVSVMSYSAKFASCFYGPFRDAAQSSPAFGDRRCYQLPPGARGLALRAVAR DIQEGADMLMVKPGLPYLDMVREVKDKHPELPLAVYQVSGEFAMLWHGAQAGAFDLRTAV LETMTAFRRAGADIIITYFAPQLLKWLKEE SWISSPROT:HEM2_METSC ID HEM2_METSC STANDARD; PRT; 320 AA. AC Q02250; DT 01-JUL-1993 (REL. 26, CREATED) DT 01-JUL-1993 (REL. 26, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) (PORPHOBILINOGEN DE SYNTHASE) (ALAD) (ALADH). GN HEMB OR ALADH. OS METHANOTHERMUS SOCIABILIS. OC ARCHAEBACTERIA; EURYARCHAEOTA; METHANOBACTERIALES; METHANOTHERMACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 93012970. RA BROCKL G., BERCHTOLD M., BEHR M., KONIG H.; RL GENE 119:151-152(1992). CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: ZINC. DR EMBL; M90083; G149788; -. DR PIR; JC1286; JC1286. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; LYASE; ZINC. FT DOMAIN 116 129 ZINC-BINDING (BY SIMILARITY). FT ACT_SITE 247 247 BY SIMILARITY. SQ SEQUENCE 320 AA; 35924 MW; 8139D263 CRC32; >HEM2_METSC MKFPYTRMRRLRKNSKIRSLVKETTLSKDDLIYPVFVKEGIKTKEKIPKMPGQYRYSVDE LIDEAKKLEEKGLKAILVFGIPKKKDKYGSSAYDPNGIVQKSVKLLKEETDLVVITDVCL CQYTEHGHCGIVKNKKIVNDETLKYLSKVALSHAEAGADVVAPSDMMDGRVKAIREELEK NGFDDVIIMSYSAKYASSFYEPFRSAVYSSPAFGDRSTYQMDPPNSLEALREVKLDIDEG ADIVMVKPALPYLDIIRLVKDTFGVPTAAYNVSGEYSMIKAAIDANYLSNKVIIETLLSI KRAGADLIITHFAPEIVEEI SWISSPROT:HEM2_HUMAN ID HEM2_HUMAN STANDARD; PRT; 330 AA. AC P13716; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) (PORPHOBILINOGEN DE SYNTHASE) (ALADH). GN ALAD. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 87017017. RA WETMUR J.G., BISHOP D.F., CANTELMO C., DESNICK R.J.; RL PROC. NATL. ACAD. SCI. U.S.A. 83:7703-7707(1986). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=LIVER; RX MEDLINE; 91334162. RA WETMUR J.; RL NUCLEIC ACIDS RES. 19:4307-4307(1991). RN [3] RP ACTIVE SITE. RX MEDLINE; 86323088. RA GIBBS P.N.B., JORDAN P.M.; RL BIOCHEM. J. 236:447-451(1986). RN [4] RP VARIANT ASN-59. RX MEDLINE; 91377738. RA WETMUR J.G., KAYA A.H., PLEWINSKA M., DESNICK R.J.; RL AM. J. HUM. GENET. 49:757-763(1991). RN [5] RP VARIANTS ARG-133 AND MET-275. RX MEDLINE; 91290050. RA PLEWINSKA M., THUNELL S., HOLMBERG L., WETMUR J.G., DESNICK R.J.; RL AM. J. HUM. GENET. 49:167-174(1991). RN [6] RP VARIANTS TRP-240 AND THR-274. RX MEDLINE; 92235256. RA ISHIDA N., FUJITA H., FUKUDA Y., NOGUCHI T., DOSS M., KAPPAS A., RA SASSA S.; RL J. CLIN. INVEST. 89:1431-1437(1992). CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER. CC -!- COFACTOR: ZINC. CC -!- DISEASE: DEFECTS IN ALAD ARE THE CAUSE OF ACUTE HEPATIC PORPHYRIA. CC -!- POLYMORPHISM: THERE ARE TWO COMMON ALLELES OF ALAD. INDIVIDUALS CC HETEROZYGOUS OR HOMOZYGOUS FOR THE 2ND ALLELE HAVE SIGNIFICANTLY CC HIGHER BLOOD LEAD LEVELS THAN DO 1ST ALLELE HOMOZYGOTES WHEN CC EXPOSED TO ENVIRONMENTAL LEAD. DR EMBL; M13928; G178329; -. DR EMBL; X64467; G28580; -. DR PIR; A26478; A26478. DR MIM; 125270; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; LYASE; ZINC; KW DISEASE MUTATION; POLYMORPHISM. FT DOMAIN 119 132 ZINC-BINDING (BY SIMILARITY). FT ACT_SITE 252 252 FT VARIANT 59 59 K -> N (IN ALLELE 2; 10% OF POPULATION). FT VARIANT 133 133 G -> R (IN ACUTE HEPATIC PORPHYRIA). FT VARIANT 240 240 R -> W (IN ACUTE HEPATIC PORPHYRIA). FT VARIANT 274 274 A -> T (IN ACUTE HEPATIC PORPHYRIA). FT VARIANT 275 275 V -> M (IN ACUTE HEPATIC PORPHYRIA). SQ SEQUENCE 330 AA; 36295 MW; 79FA73D2 CRC32; >HEM2_HUMAN MQPQSVLHSGYFHPLLRAWQTATTTLNASNLIYPIFVTDVPDDIQPITSLPGVARYGVKR LEEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKTFPNLLVACD VCLCPYTSHGHCGLLSENGAFRAEESRQRLAEVALAYAKAGCQVVAPSDMMDGRVEAIKE ALMAHGLGNRVSVMSYSAKFASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDR DVREGADMLMVKPGMPYLDIVREVKDKHPDLPLAVYHVSGEFAMLWHGAQAGAFDLKAAV LEAMTAFRRAGADIIITYYTPQLLQWLKEE SWISSPROT:HEM2_ECOLI ID HEM2_ECOLI STANDARD; PRT; 323 AA. AC P15002; DT 01-APR-1990 (REL. 14, CREATED) DT 01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) (PORPHOBILINOGEN DE SYNTHASE) (ALAD) (ALADH). GN HEMB OR NCF. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 89252914. RA LI J.-M., RUSSELL C.S., COSLOY S.D.; RL GENE 75:177-184(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 89112158. RA ECHELARD Y., DYMETRYSZYN J., DROLET M., SASARMAN A.; RL MOL. GEN. GENET. 214:503-508(1988). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=K12 / W3110; RA SIGURDSSON E., BACKMAN V.M., EGGERTSSON G.; RL SUBMITTED (AUG-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=K12; RA NASHIMOTO H., SAITO N.; RL SUBMITTED (NOV-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [5] RP CHARACTERIZATION, AND SEQUENCE OF 1-5; 95-134 AND 237-253. RX MEDLINE; 93176130. RA SPENCER P., JORDAN P.M.; RL BIOCHEM. J. 290:279-287(1993). CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER. CC -!- COFACTOR: ZINC. DR EMBL; M24488; G450371; -. DR EMBL; X17417; G41662; -. DR EMBL; M35121; -; NOT_ANNOTATED_CDS. DR EMBL; L44595; G1213559; -. DR EMBL; D64043; G1054579; ALT_INIT. DR PIR; JS0127; SYECPF. DR PIR; S10100; S10100. DR ECOGENE; EG10428; HEMB. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; LYASE; ZINC. FT INIT_MET 0 0 FT DOMAIN 116 129 ZINC-BINDING (BY SIMILARITY). FT ACT_SITE 246 246 BY SIMILARITY. FT CONFLICT 17 18 RA -> PR (IN REF. 1). FT CONFLICT 18 41 AMFEETTLSLNDLVLPIFVEEEID -> FT VCLKRQHLSLTTWCCRSLLKKKLT (IN REF. 2). FT CONFLICT 89 90 SD -> ER (IN REF. 1). FT CONFLICT 103 103 R -> P (IN REF. 1). FT CONFLICT 225 225 R -> P (IN REF. 2). FT CONFLICT 226 226 R -> A (IN REF. 1). FT CONFLICT 228 228 A -> G (IN REF. 1). FT CONFLICT 230 230 R -> A (IN REF. 1). FT CONFLICT 232 232 S -> Y (IN REF. 1). FT CONFLICT 240 240 A -> P (IN REF. 1). FT CONFLICT 253 253 D -> N (IN REF. 1). SQ SEQUENCE 323 AA; 35493 MW; 2C835AC7 CRC32; >HEM2_ECOLI TDLIQRPRRLRKSPALRAMFEETTLSLNDLVLPIFVEEEIDDYKAVEAMPGVMRIPEKHL AREIERIANAGIRSVMTFGISHHTDETGSDAWREDGLVARMSRICKQTVPEMIVMSDTCF CEYTSHGHCGVLCEHGVDNDATLENLGKQAVVAAAAGADFIAPSAAMDGQVQAIRQALDA AGFKDTAIMSYSTKFASSFYGPFREAAGSALKGDRKSYQMNPMNRREAIRESLLDEAQGA DCLMVKPAGAYLDIVRELRERTELPIGAYQVSGEYAMIKFAALAGAIDEEKVVLESLGSI KRAGADLIFSYFALDLAEKKILR SWISSPROT:HEM2_BRAJA ID HEM2_BRAJA STANDARD; PRT; 353 AA. AC P45622; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) (PORPHOBILINOGEN DE SYNTHASE) (ALAD) (ALADH). GN HEMB. OS BRADYRHIZOBIUM JAPONICUM. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC RHIZOBIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=I110; RX MEDLINE; 94042895. RA CHAUHAN S., O'BRIAN M.R.; RL J. BACTERIOL. 175:7222-7227(1993). CC -!- FUNCTION: REQUIRED FOR NODULE DEVELOPMENT. CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN HEME BIOSYNTHESIS. CC -!- COFACTOR: MAGNESIUM. DR EMBL; L24386; G416155; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW HEME BIOSYNTHESIS; LYASE; MAGNESIUM. FT ACT_SITE 275 275 BY SIMILARITY. SQ SEQUENCE 353 AA; 38582 MW; A5482A54 CRC32; >HEM2_BRAJA MAIKYGRPIELREVSRRDGAAASPALDLAIRPRRNRKAEWARRMVRENVLTTDDLIWPLF LIDGNNKREQIASMPGVERLSVDQAVREAERAMKLTIPCIALFPYTDPSLRDEEGSEACN PNNLVCQAVRAIKKEFPEIGVLCDVALDPFTSHGHDGLIADGAILNDETVAVLVRQALVQ AEAGCDIIAPSDMMDGRVAAIREGLDQAGLIDVQIMAYAAKYASAFYGPFRDAIGSAKTL TGDKRTYQMDSANTDEALREVELDISEGADMVMVKPGMPYLDVVRRVKDTFAMPTFAYQV SGEYAMIAAAAGNGWLDGDRAMMESLLAFKRAGADGVLSYFAPKAAEKLRTQG SWISSPROT:HEM2_BACSU ID HEM2_BACSU STANDARD; PRT; 324 AA. AC P30950; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) (PORPHOBILINOGEN DE SYNTHASE) (ALAD) (ALADH). GN HEMB. 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: 2 5-AMINOLEVULINATE = PORPHOBILINOGEN + CC 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: ZINC. DR EMBL; M57676; G143039; -. DR PIR; C42728; C42728. DR SUBTILIST; BG10344; HEMB. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; LYASE; ZINC. FT DOMAIN 117 130 ZINC-BINDING (BY SIMILARITY). FT ACT_SITE 248 248 BY SIMILARITY. SQ SEQUENCE 324 AA; 36209 MW; 78F1107D CRC32; >HEM2_BACSU MSQSFNRHRRLRTSKAMREMVKETRLHPSDFIYPIFVVEGLEGKKAVPSMPDVHHVSLDL LKDEVAELVKLGIQSVIVFGIPEEKDDCGTQAYHDHGIVQKAITEIKEHFPEMVVVADTC LCEYTDHGHCGLVKDGVILNDESLELLAQTAVSQAKAGADIIAPSNMMDGFVTVIREALD KEGFVNIPIMSYAVKYSSEFYGPFRDAANSTPQFGDRKTYQMDPANRMEALREAQSDVEE GADFLIVKPSLSYMDIMRDVKNEFTLPLVAYNVSGEYSMVKAAAQNGWIKEKEIVLEILT SMKRAGADLIITYHAKDAAKWLAE TREMBL:Q60178 ID Q60178 PRELIMINARY; PRT; 335 AA. AC Q60178; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) DE (PORPHOBILINOGEN SYNTHASE) (ALADH). GN MJ0643. 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: 2 5-AMINOLEVULINATE = CC PORPHOBILINOGEN + 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: ZINC. DR EMBL; U67512; G1591355; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; LYASE; ZINC. FT ACT_SITE 257 257 BY SIMILARITY. SQ SEQUENCE 335 AA; 37396 MW; 95C670FC CRC32; >Q60178 MFKINLGDFMLIRPRRLRKNQKIRDLVRETILTKNDLIMPIFVDENLKGNEKKEISSMPN QYRFSVEGAIEEAKEIADLGIPAVILFGIPKHKDEIASSAYDKNGVVQRTIRGIKEELGD ELLVIADCCLCEYTSHGHCGIVKDGKILNDATLPILAKIALSYADAGVDIVAPSDMMDGR VRAIREILEENGYDDVAIMSYSAKYASSFYGPFREAAESAPKFGDRKSYQMDIGNAREAL KEIALDIEEGADLILVKPALPYLDIIRMAKDRFDVPIGGYCVSGEYAMVEAAARNGWLDR EKVIYEILLSIKRAGADFIITYWAKEVAEIGLSQE TREMBL:Q59643 ID Q59643 PRELIMINARY; PRT; 337 AA. AC Q59643; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) DE (PORPHOBILINOGEN SYNTHASE) (ALADH). GN HEMB. OS PSEUDOMONAS AERUGINOSA. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC PSEUDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=PAO1; RA HUNGERER C., KITTEL T., ROEMLING U., JAHN D.; RL SUBMITTED (OCT-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = CC PORPHOBILINOGEN + 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: ZINC. DR EMBL; X91820; G1009431; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW LYASE; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; ZINC. FT ACT_SITE 260 260 BY SIMILARITY. SQ SEQUENCE 337 AA; 37037 MW; 9F3CED38 CRC32; >Q59643 MSFTPANRAYPYTRLRRNRRDDFSRRLVRENVLTVDDLILPVFVLDGVNQRESIPSMPGV ERLSIDQLLIEAEEWVALGIPALALFPVTPVEKKSLDAAEAYNPEGIAQRATRALRERFP ELGIITDVALDPFTTHGQDGILDDDGYVLNDVSIDVLVRQALSHAEAGAQVVAPSDMMDG RIGAIREALESAGHTNVRIMAYSAKYASAYYGPFRDAVGSASNLGKGNKATYQMDPANSD EALHEVAADLAEGADMVMVKPGMPYLDIVRRVKDEFRAPTFVYQVSGEYAMHMGAIQNGW LAESVILESLTAFKRAGADGILTYFAKQAAEQLRRGR TREMBL:Q59334 ID Q59334 PRELIMINARY; PRT; 328 AA. AC Q59334; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) DE (PORPHOBILINOGEN SYNTHASE) (ALADH). GN HEMB. OS CHLOROBIUM VIBRIOFORME. OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; GREEN BACTERIA; OC CHLOROBIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=F. THIOSULFATOPHILUM 8327; RA RHIE G., AVISSAR Y.J., BEALE S.I.; RL J. BIOL. CHEM. 271:8176-8182(1996). CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = CC PORPHOBILINOGEN + 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: ZINC. DR EMBL; U38348; G1033198; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW LYASE; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; ZINC. FT ACT_SITE 253 253 BY SIMILARITY. SQ SEQUENCE 328 AA; 36394 MW; 100BDE67 CRC32; >Q59334 MSQLDLLNIVHRPRRLRRTAALRNLVQENTLTVNDLVFPLFVMPGTNAVEEVSSMPGSFR FTIDRAVEECKELYDLGIQGIDLFGIPEQKTEDGSEAYNDNGILQQAIRAIKKAVPELCI MTDVALDPFTPFGHDGLVKDGIILNDETVEVLQKMAVSHAEAGADFVSPSDMMDGRIGAI REALDETDHSDVGILSYAAKYASSFYGPFRDALHSAPQFGDKSTYQMNPANTEEAMKEVE LDIVEGADIVMVKPGLAYLDIVWRTKERFDVPVAIYHVSGEYAMVKAAAAKGWIDEDRVM MESLLCMKRAGADIIFTYYAKEAAKKLR TREMBL:Q59295 ID Q59295 PRELIMINARY; PRT; 205 AA. AC Q59295; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) DE (PORPHOBILINOGEN SYNTHASE) (AMINOLEVULINATE DEHYDRATASE) (FRAGMENT). GN HEMB. OS CLOSTRIDIUM JOSUI. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=FERM P-9684; RX MEDLINE; 95394829. RA FUJINO E., FUJINO T., KARITA S., OHMIYA K.; RL J. BACTERIOL. 177:5169-5175(1995). CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = CC PORPHOBILINOGEN + 2 H(2)O. CC -!- COFACTOR: ZINC. DR EMBL; D28503; G556484; -. KW LYASE. FT NON_TER 205 205 SQ SEQUENCE 205 AA; 23172 MW; 1F438652 CRC32; >Q59295 MIKRPRRLRTNEVLRKAVRETRLSTDSLIWPLFIVEGKNIKKEISSLPGQYHFSPDMVGK AIEAALKADVKSVLLFGLPKHKDEKGSEAYNENGVLQQGIREIKQRYPQMQVITDICMCE YTSHGHCGILEGERVDNDRTLPYLEKIALSHVMAGADMIAPSDMMDGRIYALRSTLDKNG FTDIPIMSYAVKYASSFYGPFREAA TREMBL:Q43148 ID Q43148 PRELIMINARY; PRT; 401 AA. AC Q43148; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE PRECURSOR (EC 4.2.1.24) DE (PORPHOBILINOGEN SYNTHASE) (ALADH) (FRAGMENT). GN ALA 2. OS SELAGINELLA MARTENSII (MARTENS'S SPIKE MOSS). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; LYCOPODIOPHYTA; ISOETOPSIDA. RN [1] RP SEQUENCE FROM N.A. RA SCHAUMBURG A., SCHNEIDER-POETSCH H.J.A.W.; RL SUBMITTED (SEP-1991) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = CC PORPHOBILINOGEN + 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: ZINC. DR EMBL; X61652; G21226; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW TRANSIT PEPTIDE; LYASE; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; KW ZINC. FT NON_TER 1 1 FT TRANSIT <1 23 POTENTIAL. FT CHAIN 24 401 PORPHOBILINOGEN SYNTHASE. FT ACT_SITE 322 322 BY SIMILARITY. SQ SEQUENCE 401 AA; 43553 MW; 93CA7618 CRC32; >Q43148 RRRRAAIQCAAASPSSPDPSWRTNVVSDRVSVETSPRSIQECEADVVSGNPPAAPAAPAK AKAPSGTPVVKPLRLTSRPRRNRKSAALRDAFQETTLTPANFILPLFIHEGEEDSPIGAM PGCSRLGWRHGLIDEVYKARDVGVNSVVLFPKIPDALKSSTGDEAYNPNGLVPRAIRTLK DKFPDLVIYTDVALDPYSSDGHDGIVREDGVIMNDETVHQLCKQAVAQAEAGADVVSPSD IMDGRVGAIRTALDEAGYYHVWIMAYTAKYASALYEPFREALDSNPRFGDKKTYQMNPAN YREALLEVHADESEGADILMVKPAMPYLDVIRLLPDTSALPISAYQVSGEYSMIKAAASQ GMLVDEKKAILESLLCIKRAGADVILTYAALQAARWLCGEK TREMBL:Q43058 ID Q43058 PRELIMINARY; PRT; 430 AA. AC Q43058; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) DE (PORPHOBILINOGEN SYNTHASE) (ALADH). GN ALAD. OS PHYSCOMITRELLA PATENS (MOSS). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; BRYOPHYTA; BRYOPSIDA. RN [1] RP SEQUENCE FROM N.A. RA GWAREK M.A.; RL SUBMITTED (JUL-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = CC PORPHOBILINOGEN + 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: ZINC. DR EMBL; X89886; G927503; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW LYASE; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; ZINC. FT ACT_SITE 352 352 BY SIMILARITY. SQ SEQUENCE 430 AA; 46140 MW; 66F8262D CRC32; >Q43058 MVGVMMAAAATPGCRVSQALTACSSHEGLRRVAPVFGPGVVSVSAPCKLPRKLNVQAVAE PIAKSSPRTIEECEANVVAGNAPAAPPVPAKPSAPEGTPAISPLVMPARPRRNRRSPALR AAFQETTISPANFILPLFVHEGEQNAPIGAMPGCQRLGWRHGLIDEVYKARDVGVNSVVL FPKVPDALKSSTGDEAYNPDGLVPRCIRLLKAIPDLVIYTDVALDPYSSDGHDGIVREDG LIMNDETVHQLCKQAVAQAQAGADVVSPSDMMDGRVGAIRKALDLAGHQDVSIIAYTAKY ASAFYGPSREALDSNPRFGDKKTYQMNPANYREALIETRMDEAEGADILMVKPAMPYLDV IRLLRDNTALPISAYQVSGEYSMIRAGCRGMLDEKKAVLESLLSIRRAGADVILTYFAIQ AAQWLCAERV TREMBL:Q42836 ID Q42836 PRELIMINARY; PRT; 428 AA. AC Q42836; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE (EC 4.2.1.24) DE (PORPHOBILINOGEN SYNTHASE) (ALADH). GN ALAD. 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: 2 5-AMINOLEVULINATE = CC PORPHOBILINOGEN + 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: ZINC. DR EMBL; X92402; G1041423; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW LYASE; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; ZINC. FT ACT_SITE 347 347 BY SIMILARITY. SQ SEQUENCE 428 AA; 46212 MW; A410C92B CRC32; >Q42836 MASTVPFSPAKVQMFQATNCHGHAGFGSSFAVPRTGPRPRSVAVRVSSEQEAAATVRAPS GRSIEECEADAVAGRFPAPSCVCQTPKAPDGTPEIRPLDMAKRPRRNRRSPALRAAFQET SISPANLVLPLFIHEGEEDAPIGAMPGCFRLGWQHGLLAEVYKARDVGVNSFVLFPKVPD ALKSPTGVEAYNDNGLVPRTIRLLKDKFPDIIVYTDVALDPYSSDGHDGIVRKDGVILND ETVYQLCKQAVSQARAGADVVSPSNMMDGRVGAIRSALDAEGFNDVSIMSYTAKYASSFY GPFREALDSNPRFGDKKTYQMNPANYREALLETAADEAEGADILLVKPGLPYLDIIRLSR DNSALPIAAYQVSGEYSMIKAGGALNMIDEEKVMMESLMCLRRAGADVILTYFARQPPAV LCGMGTAK TREMBL:Q42682 ID Q42682 PRELIMINARY; PRT; 390 AA. AC Q42682; 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 DELTA-AMINOLEVULINIC ACID DEHYDRATASE PRECURSOR (EC 4.2.1.24) DE (PORPHOBILINOGEN SYNTHASE) (ALADH). GN ALAD. 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; 95201253. RA MATTERS G.L., BEALE S.I.; RL PLANT MOL. BIOL. 27:607-617(1995). CC -!- CATALYTIC ACTIVITY: 2 5-AMINOLEVULINATE = CC PORPHOBILINOGEN + 2 H(2)O. CC -!- PATHWAY: SECOND STEP IN PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: HOMOOCTAMER (BY SIMILARITY). CC -!- COFACTOR: ZINC. DR EMBL; U19876; G642579; -. DR PROSITE; PS00169; D_ALA_DEHYDRATASE. KW TRANSIT PEPTIDE; LYASE; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; KW ZINC. FT TRANSIT 1 24 POTENTIAL. FT CHAIN 25 390 DELTA-AMINOLEVULINIC ACID DEHYDRATASE. FT ACT_SITE 312 312 BY SIMILARITY. SQ SEQUENCE 390 AA; 43045 MW; 78FF3851 CRC32; >Q42682 MQMMQRNVVGQRPVAGSRRSLVVANVAEVTRPAVSTNGKHRTGVPEGTPIVTPQDLPSRP RRNRRSESFRASVREVNVSPANFILPIFIHEESNQNVPIASMPGINRLAYGKNVIDYVAE PRSYGVNQVVVFPKTPDHLKTQTAEEAFNKNGLSQRTIRLLKDSFPDLEVYTDVALDPYN SDGHDGIVSDAGVILNDETIEYLCRQAVSQAEAGADVVSPSDMMDGRVGAIRRALDREGF TNVSIMSYTAKYASAYYGPFRDALASAPKPGQAHRRIPPNKKTYQMDPANYREAIREAKA DEAEGADIMMVKPGMPYLDVVRLLRETSPLPVAVYHVSGEYAMLKAAAERGWLNEKDAVL EAMTCFRRAGGDLILTYYGIEASKWLAGEK TREMBLNEW:SPU83568_1 ID SPU83568_1 standard; PRT; 270 AA. AC U83568; DR EMBL; U83568; SPU83568. DE product: "delta-aminolevulinic acid dehydratase homolog"; DE Schizosaccharomyces pombe delta-aminolevulinic acid dehydratase DE homolog mRNA, partial cds. OS Schizosaccharomyces pombe (fission yeast) OC Eukaryotae; mitochondrial eukaryotes; Fungi; Ascomycota; OC Archaeascomycetes; Schizosaccharomycetales; OC Schizosaccharomycetaceae; Schizosaccharomyces. OG Plasmid pPV141 FT CDS <1..813 FT /EC_number="4.2.1.24" FT /codon_start=1 FT /product="delta-aminolevulinic acid dehydratase homolog" FT /db_xref="PID:g1791311" FT /translation="HRLEEFLGPLVKKGLRSVILFGVIESKKDYCGSMADSENGPVIKA FT VKEIRHLFPELVVACDVCLCEYTDHGHCGLLYEDGTINNAKSVERIAEVSGNYALAGAQ FT IISPSDCMDGRVKAIKQKLVELELSHKVCVISYSAKFASGFFGPFRAAANGAPKFGDRS FT CYQLPCNARGLAKRAILRDVREGADGIMVKPGTPYLDILAMASKLADDLPIATYQVSGE FT FAIIHAAAAAGVFELKRHVMETMDGFMRAGANIVLTYFTPELLEWLEY" SQ Sequence 270 BP; >SPU83568_1 HRLEEFLGPLVKKGLRSVILFGVIESKKDYCGSMADSENGPVIKAVKEIRHLFPELVVAC DVCLCEYTDHGHCGLLYEDGTINNAKSVERIAEVSGNYALAGAQIISPSDCMDGRVKAIK QKLVELELSHKVCVISYSAKFASGFFGPFRAAANGAPKFGDRSCYQLPCNARGLAKRAIL RDVREGADGIMVKPGTPYLDILAMASKLADDLPIATYQVSGEFAIIHAAAAAGVFELKRH VMETMDGFMRAGANIVLTYFTPELLEWLEY TREMBLNEW:ECAE143_12 ID ECAE143_12 standard; PRT; 335 AA. AC AE000143; DR EMBL; AE000143; ECAE143. SuspectSTRv DE gene: "hemB"; product: "delta-aminolevulinic acid dehydratase"; DE Escherichia coli from bases 379180 to 389460 (section 33 of 400) of DE the complete genome. OS Escherichia coli OC Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OG Chloroplast FT CDS complement(8798..9805) FT /gene="hemB" FT /EC_number="4.2.1.24" FT /note="f335; 100 pct identical to GB: ECOPS_9 ACCESSION: FT D85613; residues 13-335 are 100 pct identical to HEM2_ECOLI FT SW: P15002 (324 aa)" FT /codon_start=1 FT /product="delta-aminolevulinic acid dehydratase" FT /transl_table=11 FT /db_xref="PID:g1786566" FT /translation="MPLDSTNIRQTMTDLIQRPRRLRKSPALRAMFEETTLSLNDLVLP FT IFVEEEIDDYKAVEAMPGVMRIPEKHLAREIERIANAGIRSVMTFGISHHTDETGSDAW FT REDGLVARMSRICKQTVPEMIVMSDTCFCEYTSHGHCGVLCEHGVDNDATLENLGKQAV FT VAAAAGADFIAPSAAMDGQVQAIRQALDAAGFKDTAIMSYSTKFASSFYGPFREAAGSA FT LKGDRKSYQMNPMNRREAIRESLLDEAQGADCLMVKPAGAYLDIVRELRERTELPIGAY FT QVSGEYAMIKFAALAGAIDEEKVVLESLGSIKRAGADLIFSYFALDLAEKKILR" SQ Sequence 335 BP; >ECAE143_12 MPLDSTNIRQTMTDLIQRPRRLRKSPALRAMFEETTLSLNDLVLPIFVEEEIDDYKAVEA MPGVMRIPEKHLAREIERIANAGIRSVMTFGISHHTDETGSDAWREDGLVARMSRICKQT VPEMIVMSDTCFCEYTSHGHCGVLCEHGVDNDATLENLGKQAVVAAAAGADFIAPSAAMD GQVQAIRQALDAAGFKDTAIMSYSTKFASSFYGPFREAAGSALKGDRKSYQMNPMNRREA IRESLLDEAQGADCLMVKPAGAYLDIVRELRERTELPIGAYQVSGEYAMIKFAALAGAID EEKVVLESLGSIKRAGADLIFSYFALDLAEKKILR