ENZYME:4.1.1.37 ID 4.1.1.37 DE UROPORPHYRINOGEN DECARBOXYLASE. CA UROPORPHYRINOGEN-III = COPROPORPHYRINOGEN + 4 CO(2). CC -!- ACTS ON A NUMBER OF PORPHYRINOGENS. DI PORPHYRIA CUTANEA TARDA; MIM:176090. DI PORPHYRIA, HEPATOERYTHROPOIETIC; MIM:176100. PR PROSITE; PDOC00705; DR P32395, DCUP_BACSU; P29680, DCUP_ECOLI; P06132, DCUP_HUMAN; DR P46809, DCUP_MYCLE; P32362, DCUP_RAT ; P42503, DCUP_RHOCA; DR P32920, DCUP_RHOSH; P16891, DCUP_SYNP7; P54224, DCUP_SYNY3; DR P32347, DCUP_YEAST; PIR:S35595 >P1;S35595 uroporphyrinogen decarboxylase (EC 4.1.1.37) - Rhodobacter sphaeroides C;Species: Rhodobacter sphaeroides C;Date: 20-May-1994 #sequence_revision 20-May-1994 #text_change 20-May-1994 C;Accession: S35595 R;Jones, R.M.; Jordan, P.M. Biochem. J. 293, 703-712, 1993 A;Title: Purification and properties of the uroporphyrinogen decarboxylase from Rhodobacter sphaeroides. A;Reference number: S35595 A;Accession: S35595 A;Status: preliminary A;Residues: 1-27 >S35595 TMLRALKGETLPTPSIWLMRQAGPYLP PIR:A37215 >F1;A37215 uroporphyrinogen decarboxylase (EC 4.1.1.37) - human (fragment) C;Species: Homo sapiens (man) C;Date: 30-Dec-1991 #sequence_revision 30-Dec-1991 #text_change 23-Jun-1993 C;Accession: A37215 R;Garey, J.R.; Harrison, L.M.; Franklin, K.F.; Metcalf, K.M.; Radisky, E.S.; Kushner, J.P. J. Clin. Invest. 86, 1416-1422, 1990 A;Title: Uroporphyrinogen decarboxylase: a splice site mutation causes the deletion of exon 6 in multiple families with porphyria cutanea tarda. A;Reference number: A37215; MUID:91056138 A;Accession: A37215 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-161 A;Cross-references: GB:M60891 C;Keywords: carbon-carbon lyase; carboxy-lyase >A37215 GMEVTMVPSKGPSFPEPLREEQDLEALRDPEVVASELGYVFQAITLTRQRLAGRVPLIGF AGAPWTLMTYMVEGGGSSTMAQAKRWLYQRPQASHQLLRILTDALVPYLVGQVVAGAQLF ESHAGHLGPQLFNKFALPYIRDVAKQVKARLREAGLAPVPM PIR:A24411 >P1;A24411 uroporphyrinogen decarboxylase (EC 4.1.1.37) - human C;Species: Homo sapiens (man) C;Date: 31-Dec-1988 #sequence_revision 31-Dec-1988 #text_change 02-Jul-1996 C;Accession: A24411; I39205 R;Romeo, P.H.; Raich, N.; Dubart, A.; Beaupain, D.; Pryor, M.; Kushner, J.; Cohen-Solal, M.; Goossens, M. J. Biol. Chem. 261, 9825-9831, 1986 A;Title: Molecular cloning and nucleotide sequence of a complete human uroporphyrinogen decarboxylase cDNA. A;Reference number: A24411; MUID:86278017 A;Accession: A24411 A;Molecule type: mRNA A;Residues: 1-367 A;Note: the authors translated the codon GCG for residue 120 as Arg R;Romana, M.; Dubart, A.; Beaupain, D.; Chabret, C.; Goossens, M.; Romeo, P.H. Nucleic Acids Res. 15, 7343-7356, 1987 A;Title: Structure of the gene for human uroporphyrinogen decarboxylase. A;Reference number: I39205; MUID:88015599 A;Accession: I39205 A;Status: translation not shown; translated from GB/EMBL/DDBJ A;Molecule type: DNA A;Residues: 1-7 A;Cross-references: EMBL:X06048; NID:g37613; CDS_PID:g580607 C;Keywords: carbon-carbon lyase; carboxy-lyase; porphyrin biosynthesis >A24411 MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCR SPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPSKGPSFPEPLREEQDLEA LRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRW LYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDV AKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVT LQGNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKH SRLLRQN PIR:S23471 >P1;S23471 uroporphyrinogen decarboxylase (EC 4.1.1.37) - yeast (Saccharomyces cerevisiae) N;Alternate names: protein YD9609.03; protein YDR047w C;Species: Saccharomyces cerevisiae C;Date: 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 23-Aug-1996 C;Accession: S23471; S33965; S54033; S20190; S27348; S31312 R;Garey, J.R.; Labbe-Bois, R.; Chelstowska, A.; Rytka, J.; Harrison, L.; Kushner, J.; Labbe, P. Eur. J. Biochem. 205, 1011-1016, 1992 A;Title: Uroporphyrinogen decarboxylase in Saccharomyces cerevisiae. HEM12 gene sequence and evidence for two conserved glycines essential for enzymatic activity. A;Reference number: S23471 A;Accession: S23471 A;Molecule type: DNA A;Residues: 1-362 A;Cross-references: EMBL:X63721 R;Diflumeri, C.; Larocque, R.; Keng, T. Yeast 9, 613-623, 1993 A;Title: Molecular analysis of HEM6 (HEM12) in Saccharomyces cerevisiae, the gene for uroporphyrinogen decarboxylase. A;Reference number: S33965 A;Accession: S33965 A;Molecule type: DNA A;Residues: 1-362 A;Cross-references: EMBL:Z19089 R;Hunt, S.; Bowman, S.; Harris, D. submitted to the EMBL Data Library, May 1995 A;Reference number: S54031 A;Accession: S54033 A;Molecule type: DNA A;Residues: 1-362 A;Cross-references: EMBL:Z49209 C;Genetics: A;Gene: LISTA:HEM12; HEM6; POP3 A;Map position: 4R C;Keywords: carbon-carbon lyase; carboxy-lyase; porphyrin biosynthesis >S23471 MGNFPAPKNDLILRAAKGEKVERPPCWIMRQAGRYLPEYHEVKNNRDFFQTCRDAEIASE ITIQPVRRYRGLIDAAIIFSDILVIPQAMGMRVEMLEGKGPHFPEPLRNPEDLQTVLDYK VDVLKELDWAFKAITMTRIKLDGEVPLFGFCGGPWTLMVYMTEGGGSRLFRFAKQWINMY PELSHKLLQKITDVAVEFLSQQVVAGAQILQVFESWGGELSSVDFDEFSLPYLRQIAERV PKRLQELGIMEQIPMIVFAKGSWYALDKLCCSGFDVVSLDWSWDPREAVKINKNRVTLQG NLDPGVMYGSKEVITKKVKQMIEAFGGGKSRYIVNFGHGTHPFMDPDVIKFFLEECHRIG SK PIR:S55733 >P1;S55733 uroporphyrinogen decarboxylase - barley C;Species: Hordeum vulgare (barley) C;Date: 28-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 03-Nov-1995 C;Accession: S55733 R;Mock, H.P.; Trainotti, L.; Kruse, E.; Grimm, B. Plant Mol. Biol. 28, 245-256, 1995 A;Title: Isolation, sequencing and expression of cDNA sequences encoding uroporphyrinogen decarboxylase from tobacco and barley. A;Reference number: S55732 A;Accession: S55733 A;Status: preliminary A;Molecule type: mRNA A;Residues: 1-330 >S55733 VERPPVWLMRQAGRYMKSYQNLCEKYPLFRERSENVDLVVEISLQPWKVFKPDGVILFSD ILTPLPGMNIPFDIVKGKGPVIYDPLRTAAAVNEVREFVPEEWVPYVGQALNLLRGEVKN EAAVLGFVGAPFTLASYCVEGGSSKNFSKIKRMAFAEPAILHNLLQKFTTSMANYIKYQA DNGAQAVQIFDSWATELSPVDFEEFSLPYLKQIVDSVKETHPDLPLILYASGSGGLLERL PLTGVDVVSLDWTVDMAEGRKRLGSNIAVQGNVDPGVLFGSKEFITKRIYDTVQKAGSQG HVLNLGHGIKVGTPEENVAHFFEVAKGIRY PIR:S55732 >P1;S55732 uroporphyrinogen decarboxylase - common tobacco C;Species: Nicotiana tabacum (common tobacco) C;Date: 28-Oct-1995 #sequence_revision 03-Nov-1995 #text_change 03-Nov-1995 C;Accession: S55732 R;Mock, H.P.; Trainotti, L.; Kruse, E.; Grimm, B. Plant Mol. Biol. 28, 245-256, 1995 A;Title: Isolation, sequencing and expression of cDNA sequences encoding uroporphyrinogen decarboxylase from tobacco and barley. A;Reference number: S55732 A;Accession: S55732 A;Status: preliminary A;Molecule type: mRNA A;Residues: 1-391 >S55732 MMSCNYSFSSISPSSKSAFTSPSNFNLNPRLICCSAGGTVAEPKAINATQPLLLDAVRGK EVERPPVWLMRQAGRYMKSYQLLCEKYPLFRDRSENVDLVVEISLQPWKVFRPDGVILFS DILTPLSGMNIPFDIIKGKGPVIFDPLRTAADVEKVREFIPEKSVPYVGEALTILRKEVN NQAAVLGFVGAPFTLASYVVEGGSSKNFTKIKRLAFAEPKVLHALLQKFATSMAKYIRYQ ADSGAQAVQIFDSWATELSPVDFEEFSLPYLKQIVDSVKLTHPNLPLILYASGSGGLLER LPLTGVDVVSLDWTVDMADGRRRLGPNVAIQGNVDPGVLFGSKEFITNRINDTVKKAGKG KHILNLGHGIKVGTPEENFAHFFEIAKGLRY PIR:B47045 >P1;B47045 uroporphyrinogen decarboxylase (EC 4.1.1.37) - Bacillus subtilis C;Species: Bacillus subtilis C;Date: 04-Mar-1994 #sequence_revision 18-Nov-1994 #text_change 18-Nov-1994 C;Accession: B47045 R;Hansson, M.; Hederstedt, L. J. Bacteriol. 174, 8081-8093, 1992 A;Title: Cloning and characterization of the Bacillus subtilis hemEHY gene cluster, which encodes protoheme IX biosynthetic enzymes. A;Reference number: A47045; MUID:93094140 A;Contents: 3G18 A;Accession: B47045 A;Status: preliminary A;Molecule type: nucleic acid A;Residues: 1-353 A;Cross-references: NCBIN:119989; NCBIP:119991 A;Note: sequence extracted from NCBI backbone C;Keywords: carbon-carbon lyase; carboxy-lyase >B47045 MSKRETFNETFLKAARGEKADHTPVWYMRQAGRSQPEYRKLKEKYGLFEITHQPELCAYV TRLPVEQYGVDAAILYKDIMTPLPSIGVDVEIKNGIGPVIDQPIRSLADIEKLGQIDPEQ DVPYVLETIKLLVNEQLNVPLIGFSGAPFTLASYMIEGGPSKNYNKTKAFMYSMPDAWNL LMSKLADMIIVYVKAQIEAGAKAIQIFDSWVGALNQADYRTYIKPVMNRIFSELAKENVP LIMFGVGASHLAGDWHDLPLDVVGLDWRLGIDEARSKGITKTVQGNLDPSILLAPWEVIE QKTKEILDQGMESDGFIFNLGHGVFPDVSPEVLKKLTAFVHEYSQNKKMGQYS PIR:A56609 >P1;A56609 uroporphyrinogen decarboxylase homolog - Synechococcus sp. (PCC 7942) C;Species: Synechococcus sp. C;Date: 08-Jul-1995 #sequence_revision 03-Aug-1995 #text_change 11-Aug-1995 C;Accession: A56609; PQ0096; A30488 R;Kiel, J.A.; Ten Berge, A.M.; Venema, G. DNA Seq. 2, 415-418, 1992 A;Title: Nucleotide sequence of the Synechococcus sp. PCC7942 hemE gene encoding the homologue of mammalian uroporphyrinogen decarboxylase. A;Reference number: A56609; MUID:93076004 A;Accession: A56609 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-354 A;Cross-references: EMBL:Z11705; NCBIP:118919 A;Note: sequence extracted from NCBI backbone R;Kiel, J.A.K.W.; Boels, J.M.; Beldman, G.; Venema, G. Gene 89, 77-84, 1990 A;Title: Nucleotide sequence of the Synechococcus sp. PCC7942 branching enzyme gene (glgB): expression in Bacillus subtilis. A;Reference number: JQ0550; MUID:90323609 A;Accession: PQ0096 A;Molecule type: DNA A;Residues: 1-79 A;Cross-references: GB:M31544 C;Genetics: A;Gene: hemE C;Keywords: carbon-carbon lyase; carboxy-lyase; lyase; porphyrin biosynthesis >A56609 MVASSSLPRLLRAARGEVLDRPPVWMMRQAGRYMKVYRDLRDKYPGFRERSETPELAIEI SLQPFRAFKPDGVILFSDILTPLPGMGIPFDIIESKGPILEPPIRTAEQVAAVHDLDPEE ATPFIRPILETLRQEVGNEAAVLGFAGAPWTLAAYAIEGKSSKTYANIKHLAFSEPTILH ELLGKLADNIAIYLCHQIDCGAQVVQLFDSWAGQLSPIDYDTFALPYQQRVFQQVKAKHP EVPLILYISGSAGVLERMGQSGCDIVSVDWTVDLLDARRRLGPDIGLQGNIDPGVLFGSQ DFIRDRILDTVRKAGNQRHILNLGHGILPGTPEDNARHFFETAKNLDQLLAASH PIR:I40672 >F1;I40672 uroporphyrinogen decarboxylase homolog - Caulobacter crescentus (fragment) C;Species: Caulobacter crescentus C;Date: 12-Aug-1996 #sequence_revision 12-Aug-1996 #text_change 12-Aug-1996 C;Accession: I40672 R;Marczynski, G.T.; Shapiro, L. J. Mol. Biol. 226, 959-977, 1992 A;Title: Cell-cycle control of a cloned chromosomal origin of replication from Caulobacter crescentus. A;Reference number: I40672; MUID:92389343 A;Accession: I40672 A;Status: preliminary; translated from GB/EMBL/DDBJ A;Molecule type: DNA A;Residues: 1-294 A;Cross-references: EMBL:U13664; NID:g727240; CDS_PID:g727241 C;Genetics: A;Gene: hemE >I40672 MTSSSPILKQTPKFLSALEGQSHANPPVWFMRQAGRYLPEYRAVRATAPDFISFCFDPEK AAEVTLQPMRRFPFDASIVFADILLIPGALGQKVWFEAGEGPKLGDMPSVESMAEKAGEA GKALSLVGETLTRVRSALDPDKALIGFAGAPWTVATYMIEKGSSDRSGARTFAYQNPETL DALIQVLVDATIDYLAMQVDAGAQALKLFESWAEGLSEPLFEPLVTQPHIRIIEGLRARG VTVPIIGFPRGAGTLVEDYAARTPVQGVALDTSASAKLGQTIQKTKTIQGALDP PIR:JS0708 >P1;JS0708 uroporphyrinogen decarboxylase (EC 4.1.1.37) - Escherichia coli C;Species: Escherichia coli C;Date: 16-Sep-1992 #sequence_revision 16-Sep-1992 #text_change 15-Jun-1996 C;Accession: JN0894; JS0708 R;Nishimura, K.; Nakayashiki, T.; Inokuchi, H. Gene 133, 109-113, 1993 A;Title: Cloning and sequencing of the hemE gene encoding uroporphyrinogen III decarboxylase (UPD) from Escherichia coli K-12. A;Reference number: JN0894 A;Accession: JN0894 A;Status: nucleic acid sequence not shown A;Molecule type: DNA A;Residues: 1-353 A;Cross-references: GB:D12624 A;Experimental source: strain K-12 C;Comment: This enzyme catalyzes the decarboxylation of uroporphyrinogen III to coproporphyrinogen. C;Genetics: A;Gene: hemE A;Map position: 90 min C;Superfamily: uroporphyrinogen decarboxylase C;Keywords: carbon-carbon lyase; carboxy-lyase; lyase; porphyrin biosynthesis >JS0708 MTELKNDRYLRALLRQPVDVTPVWMMRQAGRYLPEYKATRAQAGDFMSLCKNAELACEVT LQPLRRYPLDARSSFRYLTVPIAMGLGSSILKPEKVRVLPRQITCKADVDKLPIPDPEDE LGYVMNAVRTIRRELKGEVPLIGFSGSPWTLATYMVEGGSSKAFTVIKKMMYADPQALHA LLDKLAKSVTLYLNAQIKAGAQAVMIFDTWGGVLTGRDYQQFSLYYMHKIVDGLLRENDG RRVPVTLFTKSATVAEAMAETGCDALGLDWTTDIADARRRVGNKVALQGNMDPSMLYAPP ARIEEEVATILAGFGHGEGHVFNLGHGIHQDVPPEHAGVFVEAVHRLSEQYHR SWISSPROT:DCUP_YEAST ID DCUP_YEAST STANDARD; PRT; 362 AA. AC P32347; DT 01-OCT-1993 (REL. 27, CREATED) DT 01-OCT-1993 (REL. 27, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE UROPORPHYRINOGEN DECARBOXYLASE (EC 4.1.1.37) (UPD). GN HEM12 OR HEM6 OR POP3 OR YD9609.03. OS SACCHAROMYCES CEREVISIAE (BAKER'S YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 92249304. RA GAREY J.R., LABBE-BOIS R., CHELSTOWSKA A., RYTKA J., HARRISON L., RA KUSHNER J., LABBE P.; RL EUR. J. BIOCHEM. 205:1011-1016(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 93348774. RA DIFLUMERI C., LAROCQUE R., KENG T.; RL YEAST 9:613-623(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA HUNT S., BOWMAN S., HARRIS D., BARRELL B., RAJANDREAM M.A.; RL SUBMITTED (MAY-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [4] RP MUTANTS. RX MEDLINE; 93111946. RA CHELSTOWSKA A., ZOADEK T., GAREY J.R., KUSHNER J., RYTKA J., RA LABBE-BOIS R.; RL BIOCHEM. J. 288:753-757(1992). CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN III = COPROPORPHYRINOGEN + CC 4 CO(2). CC -!- PATHWAY: PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. DR EMBL; X63721; G3767; -. DR EMBL; Z19089; G4776; -. DR EMBL; Z49209; G798900; -. DR PIR; S23471; S23471. DR PIR; S20190; S20190. DR PIR; S31312; S31312. DR LISTA; SC00428; HEM12. DR SGD; L0000764; HEM12. DR PROSITE; PS00906; UROD_1. DR PROSITE; PS00907; UROD_2. KW LYASE; DECARBOXYLASE; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS. FT MUTAGEN 33 33 G->D: INACTIVATION. FT MUTAGEN 300 300 G->D: INACTIVATION. FT VARIANT 59 59 S -> F (IN HEM12-6 AND HEM12-12). FT VARIANT 62 62 T -> I (IN HEM12-14). FT VARIANT 107 107 L -> S (IN HEM12-3 AND HEM12-13). FT VARIANT 215 215 S -> N (IN HEM12-2 AND HEM12-11). SQ SEQUENCE 362 AA; 41349 MW; 1F6A47C9 CRC32; >DCUP_YEAST MGNFPAPKNDLILRAAKGEKVERPPCWIMRQAGRYLPEYHEVKNNRDFFQTCRDAEIASE ITIQPVRRYRGLIDAAIIFSDILVIPQAMGMRVEMLEGKGPHFPEPLRNPEDLQTVLDYK VDVLKELDWAFKAITMTRIKLDGEVPLFGFCGGPWTLMVYMTEGGGSRLFRFAKQWINMY PELSHKLLQKITDVAVEFLSQQVVAGAQILQVFESWGGELSSVDFDEFSLPYLRQIAERV PKRLQELGIMEQIPMIVFAKGSWYALDKLCCSGFDVVSLDWSWDPREAVKINKNRVTLQG NLDPGVMYGSKEVITKKVKQMIEAFGGGKSRYIVNFGHGTHPFMDPDVIKFFLEECHRIG SK SWISSPROT:DCUP_SYNY3 ID DCUP_SYNY3 STANDARD; PRT; 350 AA. AC P54224; 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 UROPORPHYRINOGEN DECARBOXYLASE (EC 4.1.1.37). GN HEME OR SLR0536. OS SYNECHOCYSTIS SP. (STRAIN PCC 6803). OC PROKARYOTA; GRACILICUTES; OXYPHOTOBACTERIA; OC CYANOBACTERIA (BLUE-GREEN ALGAE); CHROOCOCCALES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 96127529. RA KANEKO T., TANAKA A., SATO S., KOTANI H., SAZUKA T., MIYAJIMA N., RA SUGIURA M., TABATA S.; RL DNA RES. 2:153-166(1995). CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN III = COPROPORPHYRINOGEN + 4 CC CO(2). CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. DR EMBL; D64006; G1001337; -. KW LYASE; DECARBOXYLASE; PORPHYRIN BIOSYNTHESIS. SQ SEQUENCE 350 AA; 39152 MW; 0C627308 CRC32; >DCUP_SYNY3 MTEANDLPYLLRVARGEVVKRPPVWMMRQAGRYMKVYRDLRDKYPSFRERSENPDLAIEI SLQPWQAFQPDGVIMFSDILTPLPGIGIPFDIIESKGPIIDPPIRTQAQVDQLHALDPES SLPFIKTILGTLRKEVGNQSTVLGFVGAPWTLAAYAIEGKSSKDYKVIKQMAFSEPAILH SFLDKIAEAIAVYVRYQIDCGAQVVQLFDSWAGQLSPQDYDTFALPYQQKVVKLVKEIHP DTPLILYISGSAGILERMGKSGVDIVSVDWTVDMADARQRLGKEMKVQGNMDPGVLFGSQ DFIKERILDTVRKAGQGGHIFNLGHGVLVGTPEDNVRFFFETAKQVDQLL SWISSPROT:DCUP_SYNP7 ID DCUP_SYNP7 STANDARD; PRT; 354 AA. AC P16891; DT 01-AUG-1990 (REL. 15, CREATED) DT 01-APR-1993 (REL. 25, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE UROPORPHYRINOGEN DECARBOXYLASE (EC 4.1.1.37) (UPD). GN HEME. 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; 93076004. RA KIEL J.A.K.W., TEN BERGE A.M., VENEMA G.; RL DNA SEQ. 2:415-418(1992). RN [2] RP SEQUENCE OF 1-79 FROM N.A. RX MEDLINE; 90323609. RA KIEL J.A.K.W., BOELS J.M., BELDMAN G., VENEMA G.; RL GENE 89:77-84(1990). CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN III = COPROPORPHYRINOGEN + CC 4 CO(2). CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. DR EMBL; Z11705; G48040; -. DR EMBL; M31544; G142136; -. DR PIR; PQ0096; PQ0096. DR PROSITE; PS00906; UROD_1. DR PROSITE; PS00907; UROD_2. KW LYASE; DECARBOXYLASE; PORPHYRIN BIOSYNTHESIS. SQ SEQUENCE 354 AA; 39278 MW; A7197ACA CRC32; >DCUP_SYNP7 MVASSSLPRLLRAARGEVLDRPPVWMMRQAGRYMKVYRDLRDKYPGFRERSETPELAIEI SLQPFRAFKPDGVILFSDILTPLPGMGIPFDIIESKGPILEPPIRTAEQVAAVHDLDPEE ATPFIRPILETLRQEVGNEAAVLGFAGAPWTLAAYAIEGKSSKTYANIKHLAFSEPTILH ELLGKLADNIAIYLCHQIDCGAQVVQLFDSWAGQLSPIDYDTFALPYQQRVFQQVKAKHP EVPLILYISGSAGVLERMGQSGCDIVSVDWTVDLLDARRRLGPDIGLQGNIDPGVLFGSQ DFIRDRILDTVRKAGNQRHILNLGHGILPGTPEDNARHFFETAKNLDQLLAASH SWISSPROT:DCUP_RHOSH ID DCUP_RHOSH STANDARD; PRT; 27 AA. AC P32920; DT 01-OCT-1993 (REL. 27, CREATED) DT 01-OCT-1993 (REL. 27, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE UROPORPHYRINOGEN DECARBOXYLASE (EC 4.1.1.37) (UPD) (FRAGMENT). GN HEME. OS RHODOBACTER SPHAEROIDES (RHODOPSEUDOMONAS SPHAEROIDES). OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; PURPLE BACTERIA; OC RHODOSPIRILLACEAE. RN [1] RP SEQUENCE. RC STRAIN=NCIB 8253; RX MEDLINE; 93356732. RA JONES R.M., JORDAN P.M.; RL BIOCHEM. J. 293:703-712(1993). CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN III = COPROPORPHYRINOGEN + CC 4 CO(2). CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. CC -!- SUBUNIT: MONOMER. DR PIR; S35595; S35595. DR PROSITE; PS00906; UROD_1. DR PROSITE; PS00907; UROD_2. KW LYASE; DECARBOXYLASE; PORPHYRIN BIOSYNTHESIS. FT NON_TER 27 27 SQ SEQUENCE 27 AA; 3042 MW; 08D21AC1 CRC32; >DCUP_RHOSH TMLRALKGETLPTPSIWLMRQAGPYLP SWISSPROT:DCUP_RHOCA ID DCUP_RHOCA STANDARD; PRT; 344 AA. AC P42503; 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 UROPORPHYRINOGEN DECARBOXYLASE (EC 4.1.1.37) (UPD). GN HEME. 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; 95303970. RA INEICHEN G., BIEL A.J.; RL PLANT PHYSIOL. 108:423-423(1995). CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN III = COPROPORPHYRINOGEN + CC 4 CO(2). CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. CC -!- SUBUNIT: MONOMER (BY SIMILARITY). DR EMBL; U16796; G567081; -. DR PROSITE; PS00906; UROD_1. DR PROSITE; PS00907; UROD_2. KW LYASE; DECARBOXYLASE; PORPHYRIN BIOSYNTHESIS. SQ SEQUENCE 344 AA; 37498 MW; DECFA0DB CRC32; >DCUP_RHOCA MTDKTILRALKGEVLPTPPVWLMRQAGRYLPEYRATRAQAGDFLSLCYTPDLAAEVTLQP IRRYGFDAAILFADILLLPQALGLDLWFETGEGPRMSTVTSMEGVKGLKGKDDIHDKLAP VYETCKILSRELPKETTFIGFAGMPWTVATYMIAGRGSKDQAAAHKFKDTDRAAFSALID AVTVATIEYLSKQVEAGCEVVKLFDSWAGSLKGQDFEDFAVEPARVITAEMKRRFPGLPV IAFPREAGQGYIGFAEKTGADCVAIDNSVSPDWAAENVQKGKTCVQGNLDPSYMVTGGQE LVEATKKVVAAFKNGPHIFNLGHGITPEANPDNVTLLMETIRKG SWISSPROT:DCUP_RAT ID DCUP_RAT STANDARD; PRT; 364 AA. AC P32362; DT 01-OCT-1993 (REL. 27, CREATED) DT 01-OCT-1993 (REL. 27, LAST SEQUENCE UPDATE) DT 01-OCT-1993 (REL. 27, LAST ANNOTATION UPDATE) DE UROPORPHYRINOGEN DECARBOXYLASE (EC 4.1.1.37) (URO-D) (FRAGMENT). GN UROD. OS RATTUS NORVEGICUS (RAT). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 88015587. RA ROMANA M., LE BOULCH P., ROMEO P.-H.; RL NUCLEIC ACIDS RES. 15:7211-7211(1987). CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN III = COPROPORPHYRINOGEN + CC 4 CO(2). CC -!- PATHWAY: PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. DR EMBL; Y00350; E10786; ALT_SEQ. DR PROSITE; PS00906; UROD_1. DR PROSITE; PS00907; UROD_2. KW LYASE; DECARBOXYLASE; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS. FT NON_TER 1 1 SQ SEQUENCE 364 AA; 40452 MW; 94805E19 CRC32; >DCUP_RAT NGLGLQNFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCRSPE ACCELTLEPVRRFPLDAAIIFSDILVVPQALAMEVTMVPGKGPSFPEPLREERDLERLRD PAAVASELGYVFQAITLTRQQLAGRVPLIGFAGAPWTLMTYMVEGGSFKTMAQAKRWLYQ KPVASHKLLGILTHALVPYLIGQVAAGAQALQLFESHAGHLGSELFSKFALPYIRDVAKR VKAGLQKAGLTRMPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKAREPVGKTVTLQG ELDPCALYASEEEIGRLVQQMLNDFGPQRYIANLGHGLYPDMDPEHVGAFLDAVHKHSRL LRQN SWISSPROT:DCUP_MYCLE ID DCUP_MYCLE STANDARD; PRT; 382 AA. AC P46809; 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 UROPORPHYRINOGEN DECARBOXYLASE (EC 4.1.1.37) (UPD). GN HEME. OS MYCOBACTERIUM LEPRAE. OC PROKARYOTA; FIRMICUTES; ACTINOMYCETALES; MYCOBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RA SMITH D.R., ROBISON K.; RL SUBMITTED (SEP-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN III = COPROPORPHYRINOGEN + CC 4 CO(2). CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. DR EMBL; U15181; G699194; -. DR PROSITE; PS00906; UROD_1. DR PROSITE; PS00907; UROD_2. KW LYASE; DECARBOXYLASE; PORPHYRIN BIOSYNTHESIS. SQ SEQUENCE 382 AA; 40851 MW; 078FECAD CRC32; >DCUP_MYCLE MLRSDVGYARPIVRGSTGPVAVLRSMSTRRELLESPYLAAVSGRKPCRVPVWFMRQAGRS LPEYRALRERYSMLAACFEPEVACEITLQPLRRYDVDAAILFSDIVVPLCAAGIDLDIVP DVGPVIGDPVRTATDIHAMKPLEPQAIQPIFQAISLLVAALGDVPLIGFAGAPFTLASYL VEGGPSRNHPRTKAMMLAEPASWHTLMDKLTDLTLGFLLGQIDAGVDAIQVFDSWAGTLS LSDYRQYVLPHSARIFATVAEHGVPMTHFGVGTADLLGAMSAAVRSGEKPGHQAVVGVDW RTSLTDAAARVEPCTALQGNLDPVVLLAGWPAVERVARTVVDDGRRAVVAGAAGHVFNLG HGVLPETDPGVLSELVSFIHSL SWISSPROT:DCUP_HUMAN ID DCUP_HUMAN STANDARD; PRT; 367 AA. AC P06132; DT 01-JAN-1988 (REL. 06, CREATED) DT 01-JAN-1988 (REL. 06, LAST SEQUENCE UPDATE) DT 01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE UROPORPHYRINOGEN DECARBOXYLASE (EC 4.1.1.37) (URO-D). GN UROD. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RX MEDLINE; 86278017. RA ROMEO P.-H., RAICH N., DUBART A., BEAUPAIN D., PRYOR M., KUSHNER J., RA COHEN-SOLAL M., GOOSSENS M.; RL J. BIOL. CHEM. 261:9825-9831(1986). RN [2] RP SEQUENCE OF 1-7 FROM N.A. RX MEDLINE; 88015599. RA ROMANA M., DUBART A., BEAUPAIN D., CHABRET C., GOOSSENS M., RA ROMEO P.-H.; RL NUCLEIC ACIDS RES. 15:7343-7356(1987). RN [3] RP VARIANT HEP LYS-167. RX MEDLINE; 91284956. RA ROMANA M., GRANDCHAMP B., DUBART A., AMSELEM S., CHABRET C., RA NORDMANN Y., GOOSSENS M., ROMEO P.H.; RL EUR. J. CLIN. INVEST. 21:225-229(1991). RN [4] RP VARIANT PCT VAL-281. RX MEDLINE; 89150444. RA GAREY J.R., HANSEN J.L., HARRISON L.M., KENNEDY J.B., KUSHNER J.P.; RL BLOOD 73:892-895(1989). RN [5] RP VARIANT PCT GLU-281. RX MEDLINE; 87042763. RA DE VERNEUIL H., GRANDCHAMP B., BEAUMONT C., PICAT C., NORDMANN Y.; RL SCIENCE 234:732-734(1986). RN [6] RP VARIANT HEP GLY-292. RX MEDLINE; 92340083. RA DE VERNEUIL H., BOURGEOIS F., DE ROOIJ F., SIERSEMA P.D., WILSON J.H., RA GRANDCHAMP B., NORDMANN Y.; RL HUM. GENET. 89:548-552(1992). CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN III = COPROPORPHYRINOGEN + CC 4 CO(2). CC -!- PATHWAY: PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- SUBUNIT: MONOMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- DISEASE: ABNORMAL UROPORPHYRINOGEN DECARBOXYLASE ACTIVITY IS CC ASSOCIATED WITH PORPHYRIA CUTANEA TARDA (PCT) AND CC HEPATOERYTHROPOIETIC PORPHYRIA (HEP). DR EMBL; M14016; G340181; -. DR EMBL; X06048; G580607; -. DR PIR; A24411; A24411. DR MIM; 176090; -. DR MIM; 176100; -. DR PROSITE; PS00906; UROD_1. DR PROSITE; PS00907; UROD_2. KW LYASE; DECARBOXYLASE; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; KW ACETYLATION; DISEASE MUTATION. FT MOD_RES 1 1 ACETYLATION. FT VARIANT 167 167 E -> K (IN HEP). FT VARIANT 281 281 G -> E (IN PCT AND HEP). FT VARIANT 281 281 G -> V (IN PCT). FT VARIANT 292 292 R -> G (IN HEP). FT CONFLICT 103 103 S -> G (IN AA SEQUENCE). SQ SEQUENCE 367 AA; 40732 MW; 990643EE CRC32; >DCUP_HUMAN MEANGLGPQGFPELKNDTFLRAAWGEETDYTPVWCMRQAGRYLPEFRETRAAQDFFSTCR SPEACCELTLQPLRRFPLDAAIIFSDILVVPQALGMEVTMVPSKGPSFPEPLREEQDLEA LRDPEVVASELGYVFQAITLTRQRLAGRVPLIGFAGAPWTLMTYMVEGGGSSTMAQAKRW LYQRPQASHQLLRILTDALVPYLVGQVVAGAQALQLFESHAGHLGPQLFNKFALPYIRDV AKQVKARLREAGLAPVPMIIFAKDGHFALEELAQAGYEVVGLDWTVAPKKARECVGKTVT LQGNLDPCALYASEEEIGQLVKQMLDDFGPHRYIANLGHGLYPDMDPEHVGAFVDAVHKH SRLLRQN SWISSPROT:DCUP_ECOLI ID DCUP_ECOLI STANDARD; PRT; 354 AA. AC P29680; DT 01-APR-1993 (REL. 25, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE UROPORPHYRINOGEN DECARBOXYLASE (EC 4.1.1.37) (UPD). GN HEME. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 94040783. RA NISHIMURA K., INOKUCHI H.; RL GENE 133:109-113(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE; 94089392. RA BLATTNER F.R., BURLAND V.D., PLUNKETT G. III, SOFIA H.J., RA DANIELS D.L.; RL NUCLEIC ACIDS RES. 21:5408-5417(1993). CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN III = COPROPORPHYRINOGEN + CC 4 CO(2). CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. DR EMBL; D12624; G216564; -. DR EMBL; U00006; G409791; -. DR PIR; JS0708; JS0708. DR ECOGENE; EG11543; HEME. DR PROSITE; PS00906; UROD_1. DR PROSITE; PS00907; UROD_2. KW LYASE; DECARBOXYLASE; PORPHYRIN BIOSYNTHESIS. FT CONFLICT 72 78 AILFSDI -> RSSFRY (IN REF. 1). FT CONFLICT 83 83 D -> I (IN REF. 1). FT CONFLICT 89 103 LYFEAGEGPRFTSPV -> SSILKPEKVRVLPRQI FT (IN REF. 1). FT CONFLICT 251 256 GGGQWL -> SATVA (IN REF. 1). SQ SEQUENCE 354 AA; 39248 MW; A9638BF5 CRC32; >DCUP_ECOLI MTELKNDRYLRALLRQPVDVTPVWMMRQAGRYLPEYKATRAQAGDFMSLCKNAELACEVT LQPLRRYPLDAAILFSDILTVPDAMGLGLYFEAGEGPRFTSPVTCKADVDKLPIPDPEDE LGYVMNAVRTIRRELKGEVPLIGFSGSPWTLATYMVEGGSSKAFTVIKKMMYADPQALHA LLDKLAKSVTLYLNAQIKAGAQAVMIFDTWGGVLTGRDYQQFSLYYMHKIVDGLLRENDG RRVPVTLFTKGGGQWLEAMAETGCDALGLDWTTDIADARRRVGNKVALQGNMDPSMLYAP PARIEEEVATILAGFGHGEGHVFNLGHGIHQDVPPEHAGVFVEAVHRLSEQYHR SWISSPROT:DCUP_BACSU ID DCUP_BACSU STANDARD; PRT; 353 AA. AC P32395; DT 01-OCT-1993 (REL. 27, CREATED) DT 01-OCT-1993 (REL. 27, LAST SEQUENCE UPDATE) DT 01-FEB-1995 (REL. 31, LAST ANNOTATION UPDATE) DE UROPORPHYRINOGEN DECARBOXYLASE (EC 4.1.1.37) (UPD). GN HEME. OS BACILLUS SUBTILIS. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 93094140. RA HANSSON M., HEDERSTEDT L.; RL J. BACTERIOL. 174:8081-8093(1992). CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN III = COPROPORPHYRINOGEN + CC 4 CO(2). CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. DR EMBL; M97208; G143043; -. DR PIR; B47045; B47045. DR SUBTILIST; BG10429; HEME. DR PROSITE; PS00906; UROD_1. DR PROSITE; PS00907; UROD_2. KW LYASE; DECARBOXYLASE; PORPHYRIN BIOSYNTHESIS. SQ SEQUENCE 353 AA; 39646 MW; F7B59F2A CRC32; >DCUP_BACSU MSKRETFNETFLKAARGEKADHTPVWYMRQAGRSQPEYRKLKEKYGLFEITHQPELCAYV TRLPVEQYGVDAAILYKDIMTPLPSIGVDVEIKNGIGPVIDQPIRSLADIEKLGQIDPEQ DVPYVLETIKLLVNEQLNVPLIGFSGAPFTLASYMIEGGPSKNYNKTKAFMYSMPDAWNL LMSKLADMIIVYVKAQIEAGAKAIQIFDSWVGALNQADYRTYIKPVMNRIFSELAKENVP LIMFGVGASHLAGDWHDLPLDVVGLDWRLGIDEARSKGITKTVQGNLDPSILLAPWEVIE QKTKEILDQGMESDGFIFNLGHGVFPDVSPEVLKKLTAFVHEYSQNKKMGQYS TREMBL:Q59269 ID Q59269 PRELIMINARY; PRT; 294 AA. AC Q59269; 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 UROPORPHYRINOGEN DECARBOXYLASE (EC 4.1.1.37) (FRAGMENT). GN HEME. OS CAULOBACTER CRESCENTUS. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; BUDDING AND/OR APPENDAGED. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NA1000; RX MEDLINE; 92389343. RA MARCZYNSKI G.T., SHAPIRO L.; RL J. MOL. BIOL. 226:959-977(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=NA1000; RA MARCZYNSKI G.T.; RL SUBMITTED (AUG-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN III = CC COPROPORPHYRINOGEN + 4 CO(2). CC -!- PATHWAY: PORPHYRIN AND HEME BIOSYNTHESIS. DR EMBL; U13664; G727241; -. DR PROSITE; PS00906; UROD_1. KW LYASE; DECARBOXYLASE; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS. FT NON_TER 294 294 SQ SEQUENCE 294 AA; 31638 MW; B4BFFBC6 CRC32; >Q59269 MTSSSPILKQTPKFLSALEGQSHANPPVWFMRQAGRYLPEYRAVRATAPDFISFCFDPEK AAEVTLQPMRRFPFDASIVFADILLIPGALGQKVWFEAGEGPKLGDMPSVESMAEKAGEA GKALSLVGETLTRVRSALDPDKALIGFAGAPWTVATYMIEKGSSDRSGARTFAYQNPETL DALIQVLVDATIDYLAMQVDAGAQALKLFESWAEGLSEPLFEPLVTQPHIRIIEGLRARG VTVPIIGFPRGAGTLVEDYAARTPVQGVALDTSASAKLGQTIQKTKTIQGALDP TREMBL:Q42967 ID Q42967 PRELIMINARY; PRT; 391 AA. AC Q42967; 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 UROPORPHYRINOGEN DECARBOXYLASE (EC 4.1.1.37). GN DCUP. OS NICOTIANA TABACUM (COMMON TOBACCO). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; OC SOLANALES; SOLANACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SR1; TISSUE=LEAF; RX MEDLINE; 95322587. RA MOCK H.P., TRAINOTTI L., KRUSE E., GRIMM B.; RL PLANT MOL. BIOL. 28:245-256(1995). CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN III = CC COPROPORPHYRINOGEN + 4 CO(2). CC -!- PATHWAY: PORPHYRIN AND HEME BIOSYNTHESIS. DR EMBL; X82833; G1009429; -. DR PROSITE; PS00906; UROD_1. KW LYASE; DECARBOXYLASE; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS. SQ SEQUENCE 391 AA; 43116 MW; E99D8203 CRC32; >Q42967 MMSCNYSFSSISPSSKSAFTSPSNFNLNPRLICCSAGGTVAEPKAINATQPLLLDAVRGK EVERPPVWLMRQAGRYMKSYQLLCEKYPLFRDRSENVDLVVEISLQPWKVFRPDGVILFS DILTPLSGMNIPFDIIKGKGPVIFDPLRTAADVEKVREFIPEKSVPYVGEALTILRKEVN NQAAVLGFVGAPFTLASYVVEGGSSKNFTKIKRLAFAEPKVLHALLQKFATSMAKYIRYQ ADSGAQAVQIFDSWATELSPVDFEEFSLPYLKQIVDSVKLTHPNLPLILYASGSGGLLER LPLTGVDVVSLDWTVDMADGRRRLGPNVAIQGNVDPGVLFGSKEFITNRINDTVKKAGKG KHILNLGHGIKVGTPEENFAHFFEIAKGLRY TREMBL:Q42855 ID Q42855 PRELIMINARY; PRT; 330 AA. AC Q42855; 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 UROPORPHYRINOGEN DECARBOXYLASE (EC 4.1.1.37) (FRAGMENT). GN DCUP. OS HORDEUM VULGARE (BARLEY). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; MONOCOTYLEDONEAE; OC CYPERALES; GRAMINEAE. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LEAF; RX MEDLINE; 95322587. RA MOCK H.P., TRAINOTTI L., KRUSE E., GRIMM B.; RL PLANT MOL. BIOL. 28:245-256(1995). CC -!- CATALYTIC ACTIVITY: UROPORPHYRINOGEN III = CC COPROPORPHYRINOGEN + 4 CO(2). CC -!- PATHWAY: PORPHYRIN AND HEME BIOSYNTHESIS. DR EMBL; X82832; G1016347; -. DR PROSITE; PS00906; UROD_1. KW LYASE; DECARBOXYLASE; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS. FT NON_TER 1 1 SQ SEQUENCE 330 AA; 36667 MW; 96271C57 CRC32; >Q42855 VERPPVWLMRQAGRYMKSYQNLCEKYPLFRERSENVDLVVEISLQPWKVFKPDGVILFSD ILTPLPGMNIPFDIVKGKGPVIYDPLRTAAAVNEVREFVPEEWVPYVGQALNLLRGEVKN EAAVLGFVGAPFTLASYCVEGGSSKNFSKIKRMAFAEPAILHNLLQKFTTSMANYIKYQA DNGAQAVQIFDSWATELSPVDFEEFSLPYLKQIVDSVKETHPDLPLILYASGSGGLLERL PLTGVDVVSLDWTVDMAEGRKRLGSNIAVQGNVDPGVLFGSKEFITKRIYDTVQKAGSQG HVLNLGHGIKVGTPEENVAHFFEVAKGIRY TREMBLNEW:ECAE473_9 ID ECAE473_9 standard; PRT; 354 AA. AC AE000473; DR EMBL; AE000473; ECAE473. SuspectSTRv DE gene: "hemE"; product: "uroporphyrinogen decarboxylase"; DE Escherichia coli from bases 4186952 to 4205241 (section 363 of 400) DE of the complete genome. OS Escherichia coli OC Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OG Chloroplast FT CDS 8078..9142 FT /gene="hemE" FT /EC_number="4.1.1.37" FT /note="o354; 99 pct identical amino acid sequence and equal FT length to DCUP_ECOLI SW: P29680; CG Site No. 644" FT /codon_start=1 FT /product="uroporphyrinogen decarboxylase" FT /transl_table=11 FT /db_xref="PID:g1790430" FT /translation="MTELKNDRYLRALLXQPVDVTPVWMMRQAGRYLPEYKATRAQAGD FT FMSLCKNAELACEVTLQPLRRYPLDAAILFSDILTVPDAMGLGLYFEAGEGPRFTSPVT FT CKADVDKLPIPDPEDELGYVMNAVRTIRRELKGEVPLIGFSGSPWTLATYMVEGGSSKA FT FTVIKKMMYADPQALHALLDKLAKSVTLYLNAQIKAGAQAVMIFDTWGGVLTGRDYQQF FT SLYYMHKIVDGLLRENDGRRVPVTLFTKGGGQWLEAMAETGCDALGLDWTTDIADARRR FT VGNKVALQGNMDPSMLYAPPARIEEEVATILAGFGHGEGHVFNLGHGIHQDVPPEHAGV FT FVEAVHRLSEQYHR" SQ Sequence 354 BP; >ECAE473_9 MTELKNDRYLRALLXQPVDVTPVWMMRQAGRYLPEYKATRAQAGDFMSLCKNAELACEVT LQPLRRYPLDAAILFSDILTVPDAMGLGLYFEAGEGPRFTSPVTCKADVDKLPIPDPEDE LGYVMNAVRTIRRELKGEVPLIGFSGSPWTLATYMVEGGSSKAFTVIKKMMYADPQALHA LLDKLAKSVTLYLNAQIKAGAQAVMIFDTWGGVLTGRDYQQFSLYYMHKIVDGLLRENDG RRVPVTLFTKGGGQWLEAMAETGCDALGLDWTTDIADARRRVGNKVALQGNMDPSMLYAP PARIEEEVATILAGFGHGEGHVFNLGHGIHQDVPPEHAGVFVEAVHRLSEQYHR TREMBLNEW:SSSLLLH_46 ID SSSLLLH_46 standard; PRT; 350 AA. AC D64006; DR EMBL; D64006; SSSLLLH. DE gene: "hemE"; product: "uroporphyrinogen decarboxylase"; DE Synechocystis sp. PCC6803 complete genome, 25/27, 3138604-3270709. OS Synechocystis sp. OC Eubacteria; Cyanobacteria; Chroococcales; Synechocystis. OG Mitochondrion FT CDS 60128..61180 FT /gene="hemE" FT /note="ORF_ID:slr0536" FT /codon_start=1 FT /product="uroporphyrinogen decarboxylase" FT /transl_table=11 FT /db_xref="PID:g1001337" FT /db_xref="SWISS-PROT:P54224" FT /translation="MTEANDLPYLLRVARGEVVKRPPVWMMRQAGRYMKVYRDLRDKYP FT SFRERSENPDLAIEISLQPWQAFQPDGVIMFSDILTPLPGIGIPFDIIESKGPIIDPPI FT RTQAQVDQLHALDPESSLPFIKTILGTLRKEVGNQSTVLGFVGAPWTLAAYAIEGKSSK FT DYKVIKQMAFSEPAILHSFLDKIAEAIAVYVRYQIDCGAQVVQLFDSWAGQLSPQDYDT FT FALPYQQKVVKLVKEIHPDTPLILYISGSAGILERMGKSGVDIVSVDWTVDMADARQRL FT GKEMKVQGNMDPGVLFGSQDFIKERILDTVRKAGQGGHIFNLGHGVLVGTPEDNVRFFF FT ETAKQVDQLL" SQ Sequence 350 BP; >SSSLLLH_46 MTEANDLPYLLRVARGEVVKRPPVWMMRQAGRYMKVYRDLRDKYPSFRERSENPDLAIEI SLQPWQAFQPDGVIMFSDILTPLPGIGIPFDIIESKGPIIDPPIRTQAQVDQLHALDPES SLPFIKTILGTLRKEVGNQSTVLGFVGAPWTLAAYAIEGKSSKDYKVIKQMAFSEPAILH SFLDKIAEAIAVYVRYQIDCGAQVVQLFDSWAGQLSPQDYDTFALPYQQKVVKLVKEIHP DTPLILYISGSAGILERMGKSGVDIVSVDWTVDMADARQRLGKEMKVQGNMDPGVLFGSQ DFIKERILDTVRKAGQGGHIFNLGHGVLVGTPEDNVRFFFETAKQVDQLL TREMBLNEW:SYNHEME_1 ID SYNHEME_1 standard; PRT; 354 AA. AC Z11705; DR EMBL; Z11705; SYNHEME. DE gene: "hemE"; product: "putative uroporphyrinogen decarboxylase"; DE Synechococcus sp. hemE gene for putative uroporphyrinogen DE decarboxylase OS Synechococcus sp. OC Eubacteria; Cyanobacteria; Chroococcales; Synechococcus. OG Mitochondrion FT CDS 54..1118 FT /EC_number="4.1.1.37" FT /product="putative uroporphyrinogen decarboxylase" FT /gene="hemE" FT /note="nucleotides 2420-2709 of Genbank accession number FT M31544 (presented in citation 2) overlap with nt 1-290 in FT the sequence presented here" FT /citation=([1],[2]) FT /db_xref="PID:g48040" FT /db_xref="SWISS-PROT:P16891" FT /translation="MVASSSLPRLLRAARGEVLDRPPVWMMRQAGRYMKVYRDLRDKYP FT GFRERSETPELAIEISLQPFRAFKPDGVILFSDILTPLPGMGIPFDIIESKGPILEPPI FT RTAEQVAAVHDLDPEEATPFIRPILETLRQEVGNEAAVLGFAGAPWTLAAYAIEGKSSK FT TYANIKHLAFSEPTILHELLGKLADNIAIYLCHQIDCGAQVVQLFDSWAGQLSPIDYDT FT FALPYQQRVFQQVKAKHPEVPLILYISGSAGVLERMGQSGCDIVSVDWTVDLLDARRRL FT GPDIGLQGNIDPGVLFGSQDFIRDRILDTVRKAGNQRHILNLGHGILPGTPEDNARHFF FT ETAKNLDQLLAASH" SQ Sequence 354 BP; >SYNHEME_1 MVASSSLPRLLRAARGEVLDRPPVWMMRQAGRYMKVYRDLRDKYPGFRERSETPELAIEI SLQPFRAFKPDGVILFSDILTPLPGMGIPFDIIESKGPILEPPIRTAEQVAAVHDLDPEE ATPFIRPILETLRQEVGNEAAVLGFAGAPWTLAAYAIEGKSSKTYANIKHLAFSEPTILH ELLGKLADNIAIYLCHQIDCGAQVVQLFDSWAGQLSPIDYDTFALPYQQRVFQQVKAKHP EVPLILYISGSAGVLERMGQSGCDIVSVDWTVDLLDARRRLGPDIGLQGNIDPGVLFGSQ DFIRDRILDTVRKAGNQRHILNLGHGILPGTPEDNARHFFETAKNLDQLLAASH TREMBLNEW:ANGLGB_2 ID ANGLGB_2 standard; PRT; 79 AA. AC M31544; DR EMBL; M31544; ANGLGB. DE gene: "hemE"; product: "uroporphyrinogen decarboxylase"; DE Synechococcus PCC6301 branching enzyme (glgB) gene, complete cds, DE and urophorphyrinogen decarboxylase (hemE) gene, 5' end. OS Synechococcus PCC6301 OC Eubacteria; Cyanobacteria; Chroococcales; Synechococcus. OG Mitochondrion FT CDS 2473..>2709 FT /gene="hemE" FT /EC_number="4.1.1.37" FT /codon_start=1 FT /product="uroporphyrinogen decarboxylase" FT /transl_table=11 FT /db_xref="PID:g142136" FT /db_xref="SWISS-PROT:P16891" FT /translation="MVASSSLPRLLRAARGEVLDRPPVWMMRQAGRYMKVYRDLRDKYP FT GFRERSETPELAIEISLQPFRAFKPDGVILFSDI" SQ Sequence 79 BP; >ANGLGB_2 MVASSSLPRLLRAARGEVLDRPPVWMMRQAGRYMKVYRDLRDKYPGFRERSETPELAIEI SLQPFRAFKPDGVILFSDI