ENZYME:4.3.1.8 ID 4.3.1.8 DE HYDROXYMETHYLBILANE SYNTHASE. AN PORPHOBILINOGEN DEAMINASE. AN PRE-UROPORPHYRINOGEN SYNTHASE. CA 4 PORPHOBILINOGEN + H(2)O = HYDROXYMETHYLBILANE + 4 NH(3). CF DIPYRROMETHANE. CC -!- IN THE PRESENCE OF A SECOND ENZYME, EC 4.2.1.75 (UROPORPHYRINOGEN- CC III SYNTHASE), OFTEN CALLED CO-SYNTHASE, THE PRODUCT IS CYCLIZED TO CC FORM UROPORPHYRINOGEN-III. DI ACUTE INTERMITTENT PORPHYRIA; MIM:176000. PR PROSITE; PDOC00461; DR P16616, HEM3_BACSU; P28464, HEM3_CHLVI; P06983, HEM3_ECOLI; DR P40129, HEM3_ERWCH; P13446, HEM3_EUGGR; P08397, HEM3_HUMAN; DR P22907, HEM3_MOUSE; Q11173, HEM3_MYCTU; P19356, HEM3_RAT ; DR Q09899, HEM3_SCHPO; P28789, HEM3_YEAST; P30527, HEM3_YERIN; DR P46355, HEM3_YERPE; PDBFINDER:1PDA ID : 1PDA Header : LYASE(PORPHYRIN) Date : 1992-11-17 Compound : Porphobilinogen deaminase Enzyme-Code : 4.3.1.8 Source : (escherichia coli) Author : G.V.Louie Author : P.D.Brownlie Author : R.Lambert Author : J.B.Cooper Author : T.L.Blundell Author : S.P.Wood Author : M.J.Warren Author : S.C.Woodcock Author : P.M.Jordan Exp-Method : X Resolution : 1.76 R-Factor : 0.188 Ref-Prog : X-PLOR/PROLSQ HSSP-N-Align : 12 T-Frac-Helix : 0.37 T-Frac-Beta : 0.24 T-Nres-Prot : 296 T-Water-Mols : 249 HET-Groups : 2 Het-Id : 314 Natom : 30 Name : DIPYROMETHANE COFACTOR Het-Id : 315 Natom : 4 Name : ACETATE ION Chain : _ Sec-Struc : 296 Helix : 109 i,i+3 : 12 Beta : 71 Para-Hb : 26 Anti-Hb : 64 Amino-Acids : 296 Break : 1 Substrate : 34 Water-Mols : 249 Sequence : DNVLRIATRQSPLALWQAHYVKDKLMASHPGLVVELVPMVTRGDVIGKGLFVKELEVALLENRAD IAVHSMKDVPVEFPQGLGLVTICEREDPRDAFVSNNYDSLDALPAGSIVGTSSLRRQCQLAERRP DLIIRSLRGNVGTRLSKLDNGEYDAIILAVAGLKRLGLESRIRAALPPEISLPAVGQGAVGIECR LDDSRTRELLAALNHHETALRVTAERAMNTRLEGGCQVPIGSYAELIDGEIWLRALVGAPDGSQI IRGERRGAPQDAEQMGISLAEELLNNGAREILAEVY PIR:S13475 >P1;S13475 hydroxymethylbilane synthase (EC 4.3.1.8) - garden pea C;Species: Pisum sativum (garden pea) C;Date: 21-Nov-1993 #sequence_revision 21-Nov-1993 #text_change 21-Nov-1993 C;Accession: S13475 R;Spano, A.J.; Timko, M.P. Biochim. Biophys. Acta 1076, 29-36, 1991 A;Title: Isolation, characterization and partial amino acid sequence of a chloroplast-localized porphobilinogen deaminase from pea (Pisum sativum L.). A;Reference number: S13475; MUID:91098265 A;Accession: S13475 A;Status: preliminary A;Residues: 1-17 >S13475 SLAVEQQTQCQDQXTAG PIR:B48359 >F1;B48359 porphobilinogen deaminase HemC - Chlorobium vibrioforme (fragment) C;Species: Chlorobium vibrioforme C;Date: 19-Nov-1993 #sequence_revision 18-Nov-1994 #text_change 04-Dec-1994 C;Accession: B48359 R;Majumdar, D.; Avissar, Y.J.; Wyche, J.H.; Beale, S.I. Arch. Microbiol. 156, 281-289, 1991 A;Title: Structure and expression of the Chlorobium vibrioforme hemA gene. A;Reference number: A48359; MUID:92171712 A;Accession: B48359 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-43 A;Cross-references: NCBIN:86184; NCBIP:86187 A;Note: sequence extracted from NCBI backbone >B48359 MNISLKLVKTTGDVLLDSPLSKIGDMGLFTKDIEKHLLAGEID PIR:S30695 >P1;S30695 porphobilinogen deaminase - Escherichia coli C;Species: Escherichia coli C;Date: 02-Dec-1993 #sequence_revision 01-Sep-1995 #text_change 04-Oct-1996 C;Accession: S30695; S19283 R;Daniels, D.L.; Plunkett III, G.; Burland, V.; Blattner, F.R. Science 257, 771-778, 1992 A;Title: Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes. A;Reference number: S30660 A;Accession: S30695 A;Status: preliminary; nucleic acid sequence not shown; translation not shown A;Molecule type: DNA A;Residues: 1-320 A;Cross-references: EMBL:M87049 A;Note: the nucleotide sequence was submitted to the EMBL Data Library, November 1992 R;Jordan, P.M.; Woodcock, S.C. Biochem. J. 280, 445-449, 1991 A;Title: Mutagenesis of arginine residues in the catalytic cleft of Escherichia coli porphobilinogen deaminase that affects dipyrromethane cofactor assembly and tetrapyrrole chain initiation and elongation. A;Reference number: S19283; MUID:92082485 A;Accession: S19283 A;Status: preliminary A;Molecule type: DNA A;Residues: 8-57,'T',59-143,'A',145-192,'A',194-271,'A',273-306,'R',308-320 C;Superfamily: hydroxymethylbilane synthase >S30695 MIMTVTSMLDNVLRIATRQSPLALWQAHYVKDKLMASHPGLVVELVPMVTRGDVILDXPL AKVGGKGLFVKELEVALLENRADIAVHSMKDVPVEFPQGLGLVTICEREDPRDAFVSNNY DSLDALPAGSIVGTSSLRRQCQLGERRPDLIIRSLRGNVGTRLSKLDNGEYDAIILAVAG LKRLGLESRIRAGLPPEISLPAVGQGAVGIECRLDDSRTRELLAALNHHETALRVTAERA MNTRLEGGCQVPIGSYAELIDGEIWLRALVGRPDGSQIIRGERRGAPQDAEQMGISLAEE LLNNGAXEILAEVYNGDAPA PIR:S25071 >P1;S25071 hydroxymethylbilane synthase (EC 4.3.1.8) - yeast (Saccharomyces cerevisiae) N;Alternate names: porphobilinogen deaminase; pre-uroporphyrinogen synthase; protein D1057; protein YDL205c C;Species: Saccharomyces cerevisiae C;Date: 30-Sep-1993 #sequence_revision 30-Sep-1993 #text_change 23-Aug-1996 C;Accession: S25071; S67764; S20129 R;Keng, T.; Richard, C.; Larocque, R. Mol. Gen. Genet. 234, 233-243, 1992 A;Title: Structure and regulation of yeast HEM3, the gene for porphobilinogen deaminase. A;Reference number: S25071 A;Accession: S25071 A;Molecule type: DNA A;Residues: 1-327 A;Cross-references: EMBL:Z11745 R;Schmidt, E.R.; Bahr, A.; Kraemer, C.; Hankeln, T.; Moeller-Rieker, S. submitted to the Protein Sequence Database, July 1996 A;Reference number: S67756 A;Accession: S67764 A;Molecule type: DNA A;Residues: 1-327 A;Cross-references: EMBL:Z74253 A;Experimental source: strain S288C C;Genetics: A;Gene: LISTA:HEM3 A;Map position: 4L C;Superfamily: hydroxymethylbilane synthase C;Keywords: ammonia-lyase; carbon-nitrogen lyase; porphyrin biosynthesis >S25071 MGPETLHIGGRKSKLAVIQSNHVLKLIEEKYPDYDCKVFTLQTLGDQIQFKPLYSFGGKA LWTKELEDHLYHDDPSKKLDLIVHSLKDMPTLLPEGFELGGITKRVDPTDCLVMPFYSAY KSLDDLPDGGIVGTSSVRRSAQLKRKYPHLKFESVRGNIQTRLQKLDDPKSPYQCIILAS AGLMRMGLENRITQRFHSDTMYHAVGQGALGIEIRKGDTKMMKILDEICDLNATICCLSE RALMRTLEGGCSVPIGVESKYNEETKKLLLKAIVVDVEGTEAVEDEIEMLIENVKEDSMA CGKILAERMIADGAKKILDEINLDRIK PIR:S50762 >P1;S50762 hydroxymethylbilane synthase (EC 4.3.1.8) precursor - Arabidopsis thaliana C;Species: Arabidopsis thaliana (mouse-ear cress) C;Date: 14-Jul-1995 #sequence_revision 03-Nov-1995 #text_change 03-May-1996 C;Accession: S50762; S34147; S34382 R;Lim, S.H.; Witty, M.; Wallace-Cook, A.D.M.; Ilag, L.I.; Smith, A.G. Plant Mol. Biol. 26, 863-872, 1994 A;Title: Porphobilinogen deaminase is encoded by a single gene in Arabidopsis thaliana and is targeted to the chloroplasts. A;Reference number: S50762 A;Accession: S50762 A;Status: nucleic acid sequence not shown; translation not shown A;Molecule type: DNA A;Residues: 1-382 A;Cross-references: EMBL:X73535 A;Note: the nucleotide sequence was submitted to the EMBL Data Library, June 1993 C;Genetics: A;Gene: hemC A;Genome: nuclear A;Introns: 82/2; 217/3; 286/3; 346/1 C;Superfamily: hydroxymethylbilane synthase C;Keywords: ammonia-lyase; carbon-nitrogen lyase; chloroplast F;1-62/Domain: transit peptide (chloroplast) #status predicted F;63-382/Product: hydroxymethylbilane synthase #status predicted >S50762 MDIASSSLSQAHKVVLTRQPSSRVNTCSLGSVSAIGFSLPQISSPALGKCRRKQSSSGFV KACVAVEQKTRTAIIRIGTRGSPLALAQAYETREKLKKKHPELVEDGAIHIEIIKTTGDK ILSQPLADIGGKGLFTKEIDEALINGHIDIAVHSMKDVPTYLPEKTILPCNLPREDVRDA FICLTAATLAELPAGSVVGTASLRRKSQILHKYPALHVEENFRGNVQTRLSKLQGGKVQA TLLALAGLKRLSMTENVASILSLDEMLPAVAQGAIGIACRTDDDKMATYLASLNHEETRL AISCERAFLETLDGSCRTPIAGYASKDEEGNCIFRGLVASPDGTKVLETSRKGPYVYEDM VKMGKDAGQELLSRAGPGFFGN PIR:JQ2278 >P1;JQ2278 hydroxymethylbilane synthase (EC 4.3.1.8) precursor - garden pea chloroplast N;Alternate names: porphobilinogen deaminase C;Species: chloroplast Pisum sativum (garden pea) C;Date: 30-Sep-1993 #sequence_revision 20-Aug-1994 #text_change 20-Aug-1994 C;Accession: JQ2278; PQ0748 R;Witty, M.; Wallace-Cook, A.D.M.; Albrecht, H.; Spano, A.J.; Michel, H.; Shabanowitz, J.; Hunt, D.F.; Timko, M.P.; Smith, A.G. Plant Physiol. 103, 139-147, 1993 A;Title: Structure and expression of chloroplast-localized porphobilinogen deaminase from pea (Pisum sativum L.) isolated by redundant polymerase chain reaction. A;Reference number: JQ2278 A;Accession: JQ2278 A;Molecule type: DNA A;Residues: 1-369 A;Accession: PQ0748 A;Molecule type: protein A;Residues: 47-63;108-119;125-143;166-172;219-226;274-286;323-332;339-349 C;Comment: This enzyme catalyzes the polymerization of four porphobilinogen monopyrrole units into the linear tetrapyrrole hydroxymethylbilane necessary for the formation of chlorophyll and heme in plant cells. C;Genetics: A;Genome: chloroplast C;Superfamily: hydroxymethylbilane synthase C;Keywords: ammonia-lyase; carbon-nitrogen lyase; chlorophyll biosynthesis; chloroplast; porphyrin biosynthesis F;1-46/Domain: signal sequence #status predicted F;47-369/Product: hydroxymethylbilane synthase #status predicted >JQ2278 MEMTLYSSSSFSLPSAPSNPSLSLFTSSFRFSSFKTSPFSKCRIRASLAVEQQTQQNKTA LIRIGTRGSPLALAQAHETRDKLMASHTELAEEGAIQIVIIKTTGDKILSQPLADIGGKG LFTKEIDEALINGDIDIAVHSMKDVPTYLPEETILPCNLPREDVRDAFISLSAASLADLP AGSVIGTASLRRKSQILHRYPSLTVQDNFRGNVQTRLRKLSEGVVKATLLALAGLKRLNM TENVTSTLSIDDMLPAVAQGAIGIACRSNDDKMAEYLASLNHEETRLAISCERAFLTTLD GSCRTPIAGYASRDKDGNCLFRGLVASPDGTRVLETSRIGSYTYEDMMKIGKDAGEELLS RAGPGFFNS PIR:IBEC >P1;IBEC hydroxymethylbilane synthase (EC 4.3.1.8) - Escherichia coli N;Alternate names: porphobilinogen deaminase; pre-uroporphyrinogen synthase C;Species: Escherichia coli C;Date: 31-Mar-1988 #sequence_revision 31-Mar-1988 #text_change 26-Apr-1996 C;Accession: A25512; S02226; S01306; S24974 R;Thomas, S.D.; Jordan, P.M. Nucleic Acids Res. 14, 6215-6226, 1986 A;Title: Nucleotide sequence of the hemC locus encoding porphobilinogen deaminase of Escherichia coli K12. A;Reference number: A25512; MUID:86312890 A;Accession: A25512 A;Molecule type: DNA A;Residues: 1-313 A;Cross-references: GB:X04242; GB:M35827 A;Experimental source: strain K12 A;Note: the authors translated the codon GCA for residue 241 as Gly and GGG for residue 261 as Ala R;Alefounder, P.R.; Abell, C.; Battersby, A.R. Nucleic Acids Res. 16, 9871, 1988 A;Title: The sequence of hemC, hemD and two additional E. coli genes. A;Reference number: S01693; MUID:89041586 A;Accession: S02226 A;Status: translation not shown A;Molecule type: DNA A;Residues: 1-240,'G',242-260,'A',262-313 A;Cross-references: EMBL:X12614 R;Jordan, P.M.; Thomas, S.D.; Warren, M.J. Biochem. J. 254, 427-435, 1988 A;Title: Purification, crystallization and properties of porphobilinogen deaminase from a recombinant strain of Escherichia coli K12. A;Reference number: S01306; MUID:89025710 A;Accession: S01306 A;Molecule type: protein A;Residues: 1-10 R;Glaser, P.; Sismeiro, O.; Danchin, A. submitted to the EMBL Data Library, June 1992 A;Reference number: S24974 A;Accession: S24974 A;Molecule type: DNA A;Residues: 1-89 A;Cross-references: EMBL:X66782 C;Genetics: A;Gene: hemC A;Map position: 85 min C;Function: A;Description: catalyzes the stepwise polymerization of four molecules of porphobilinogen to hydroxymethylbilane (uroporphyrinogen precursor) and four molecules of ammonia A;Pathway: porphyrin biosynthesis A;Note: acting with uroporphyrinogen-III synthase (cosynthase), which cyclizes hydroxymethylbilane, this enzyme produces uroporphyrinogen III the precursor for porphyrins C;Superfamily: hydroxymethylbilane synthase C;Keywords: ammonia-lyase; carbon-nitrogen lyase; porphyrin biosynthesis >IBEC MLDNVLRIATRQSPLALWQAHYVKDKLMASHPGLVVELVPMVTRGDVILDTPLAKVGGKG LFVKELEVALLENRADIAVHSMKDVPVEFPQGLGLVTICEREDPRDAFVSNNYDSLDALP AGSIVGTSSLRRQCQLAERRPDLIIRSLRGNVGTRLSKLDNGEYDAIILAVAGLKRLGLE SRIRAALPPEISLPAVGQGAVGIECRLDDSRTRELLAALNHHETALRVTAERAMNTRLEG ACQVPIGSYAELIDGEIWLRGLVGAPDGSQIIRGERRGAPQDAEQMGISLAEELLNNGAR EILAEVYNGDAPA PIR:IBEG >P1;IBEG hydroxymethylbilane synthase (EC 4.3.1.8) precursor - Euglena gracilis N;Alternate names: porphobilinogen deaminase; pre-uroporphyrinogen synthase C;Species: Euglena gracilis C;Date: 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 26-Apr-1996 C;Accession: S06109 R;Sharif, A.L.; Smith, A.G.; Abell, C. Eur. J. Biochem. 184, 353-359, 1989 A;Title: Isolation and characterisation of a cDNA clone for a chlorophyll synthesis enzyme from Euglena gracilis. The chloroplast enzyme hydroxymethylbilane synthase (porphobilinogen deaminase) is synthesised with a very long transit peptide in Euglena. A;Reference number: S06109; MUID:90005485 A;Accession: S06109 A;Molecule type: mRNA A;Residues: 1-480 A;Cross-references: GB:X15743 A;Note: part of this sequence, including the amino end of the mature protein, was confirmed by protein sequencing A;Note: 175-Ala was also found C;Function: A;Description: catalyzes the stepwise polymerization of four molecules of porphobilinogen to hydroxymethylbilane (uroporphyrinogen precursor) and four molecules of ammonia A;Pathway: porphyrin biosynthesis A;Note: acting with uroporphyrinogen-III synthase (cosynthase), which cyclizes hydroxymethylbilane, this enzyme produces uroporphyrinogen III the precursor for porphyrins C;Superfamily: hydroxymethylbilane synthase C;Keywords: ammonia-lyase; carbon-nitrogen lyase; chlorophyll biosynthesis; chloroplast; porphyrin biosynthesis F;1-139/Domain: transit peptide (chloroplast) #status predicted F;140-480/Product: hydroxymethylbilane synthase #status experimental >IBEG MYCGRYETIGETRGNSLNVFIGAAAGFVAAVALINSGLATSFYSTPVRAVPQVIVPSSLA ASSQLPVVPKETNIQVNSAQILYPDSTVKGQERTITILGVCSFLSASLFYIWKQFGMKAR TTKPADLQEVSGGRIWSLASTTGSNIGAGKTVRVATRKSPLAMWQAEFIQSELERLWPGI TVELQPMSTRGDKILDSPLAKVGGKGLFVKELETALLENRSDIAVHSTKDVPMELPEGLV LGVICKRHDPCDAIVFPKGSNLKSLEDLPHGARVGTSSLRRQCQLLLKRPDLKFLELRGN VNTRLAKLDSGDYDAIILAAAGLKRLGFSDRVLPGETNIIDPNVMCPAAGQGALSIELRT NDPEIAALLEPLHHIPDAVTVACERAMNRRLNGGCQVPISGFAQLKDGQLRMEARVGSVT GKGPLIIQSKTFRLPWSGRTWPQLQKESEALGVEVADMLLADGAQAYLDEAYASRTLGWA PIR:IBMSN >P1;IBMSN hydroxymethylbilane synthase (EC 4.3.1.8), nonerythropoietic - mouse N;Alternate names: porphobilinogen deaminase; pre-uroporphyrinogen synthase N;Contains: hydroxymethylbilane synthase, erythropoietic C;Species: Mus musculus (house mouse) C;Date: 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 26-Apr-1996 C;Accession: A36513 R;Beaumont, C.; Porcher, C.; Picat, C.; Nordmann, Y.; Grandchamp, B. J. Biol. Chem. 264, 14829-14834, 1989 A;Title: The mouse porphobilinogen deaminase gene. Structural organization, sequence, and transcriptional analysis. A;Reference number: A36513; MUID:89359283 A;Accession: A36513 A;Molecule type: DNA A;Residues: 1-361 A;Cross-references: GB:J04981 C;Function: A;Description: catalyzes the stepwise polymerization of four molecules of porphobilinogen to hydroxymethylbilane (uroporphyrinogen precursor) and four molecules of ammonia A;Pathway: porphyrin biosynthesis A;Note: acting with uroporphyrinogen-III synthase (cosynthase), which cyclizes hydroxymethylbilane, this enzyme produces uroporphyrinogen III the precursor for porphyrins C;Superfamily: hydroxymethylbilane synthase C;Keywords: alternative splicing; ammonia-lyase; carbon-nitrogen lyase; porphyrin biosynthesis F;1-361/Product: hydroxymethylbilane synthase, nonerythropoietic #status predicted F;18-361/Product: hydroxymethylbilane synthase, erythropoietic #status predicted >IBMSN MSGNGGAATTAEENGSKMRVIRVGTRKSQLARIQTETVVAMLKALYPGIQFEIIAMSTTG DKIVDTALSKIGEKSLFTKELENALEKNEVDLVVHSLKDVPTILPPGFTIGAICKRQNPC DAVVFHPKFIGKTLETLPEKSAVGTSSLRRVAQLQRKFPNLEFKSIRGNLNTRLRKLDEL QEFSAIVLAVAGLQRMGWQNRVGQILHPEECMYAVGQGALAVEVRAKDQDILDLVSVLHD PETLLRCIAERAFLRHLEGGCSVPVAVHTVIKDGQLYLTGGVWSLDGSDSMQETMQATIQ VPVQQEDGPEDDPQLVGITARNIPRGAQLAAENLGISLASLLLNKGAKNILDVARQLNDV R PIR:IBRTE >P1;IBRTE hydroxymethylbilane synthase (EC 4.3.1.8), erythropoietic - rat N;Alternate names: porphobilinogen deaminase; pre-uroporphyrinogen synthase C;Species: Rattus norvegicus (Norway rat) C;Date: 30-Sep-1992 #sequence_revision 30-Sep-1992 #text_change 26-Apr-1996 C;Accession: S00746 R;Stubnicer, A.C.; Picat, C.; Grandchamp, B. Nucleic Acids Res. 16, 3102, 1988 A;Title: Rat porphobilinogen deaminase cDNA: nucleotide sequence of the erythropoietic form. A;Reference number: S00746; MUID:88217524 A;Accession: S00746 A;Status: translation not shown A;Molecule type: mRNA A;Residues: 1-344 A;Cross-references: EMBL:X06827 C;Function: A;Description: catalyzes the stepwise polymerization of four molecules of porphobilinogen to hydroxymethylbilane (uroporphyrinogen precursor) and four molecules of ammonia A;Pathway: porphyrin biosynthesis A;Note: acting with uroporphyrinogen-III synthase (cosynthase), which cyclizes hydroxymethylbilane, this enzyme produces uroporphyrinogen III the precursor for porphyrins C;Superfamily: hydroxymethylbilane synthase C;Keywords: alternative splicing; ammonia-lyase; carbon-nitrogen lyase; porphyrin biosynthesis >IBRTE MRVIRVGTRKSQLARIQTDTVVAMLKTLYPGIQFEIIAMSTTGDKILDTALSKIGEKSLF TKELENALEKNEVDLVVHSLKDVPTILPPGFTIGAICKRENPCDAVVFEGKFIGKTLETL PEKSAVGTSSLRRVAQLQRKFPHLEFKSIRGNLNTRLRKLDEQLEFSAIILAVAGLQRMG WQNRVGQILHPEECMYAVGQGALAVEVRAKDQDILDLVGVLHDPETLLRCIAERDFLRHL EGGCSVPVAVHTVMKDGQLYLTGGVWSLDGSDSMQETMQATIQVPVQQEDGPEDDPQLVG ITARNIPRGAQLAAENLGISLASLLLNKGAKNILDVARQLNDVR PIR:IBHUN >P1;IBHUN hydroxymethylbilane synthase (EC 4.3.1.8), housekeeping (long) form - human N;Alternate names: porphobilinogen ammonia-lyase (polymerizing); porphobilinogen deaminase; pre-uroporphyrinogen synthase N;Contains: hydroxymethylbilane synthase, erythroid-specific (short) form C;Species: Homo sapiens (man) C;Date: 31-Mar-1988 #sequence_revision 02-Jul-1996 #text_change 06-Sep-1996 C;Accession: A45012; I60851; A26416; A25508; A60438; I60127 R;Yoo, H.W.; Warner, C.A.; Chen, C.H.; Desnick, R.J. Genomics 15, 21-29, 1993 A;Title: Hydroxymethylbilane synthase: complete genomic sequence and amplifiable polymorphisms in the human gene. A;Reference number: A45012; MUID:93162658 A;Accession: A45012 A;Status: preliminary; translation not shown; translated from GB/EMBL/DDBJ A;Molecule type: DNA A;Residues: 1-361 A;Cross-references: GB:M95623; NID:g292384; CDS_PID:g292386 A;Accession: I60851 A;Status: translation not shown; translated from GB/EMBL/DDBJ A;Molecule type: DNA A;Residues: 18-361 A;Cross-references: GB:M95623; NID:g292384; CDS_PID:g292385 R;Grandchamp, B.; De Verneuil, H.; Beaumont, C.; Chretien, S.; Walter, O.; Nordmann, Y. Eur. J. Biochem. 162, 105-110, 1987 A;Title: Tissue-specific expression of porphobilinogen deaminase: two isoenzymes from a single gene. A;Reference number: A26416; MUID:87133520 A;Accession: A26416 A;Molecule type: mRNA A;Residues: 1-176,'L',178-209,'K',211-361 A;Cross-references: GB:X04808 R;Raich, N.; Romeo, P.H.; Dubart, A.; Beaupain, D.; Cohen-Solal, M.; Goossens, M. Nucleic Acids Res. 14, 5955-5968, 1986 A;Title: Molecular cloning and complete primary sequence of human erythrocyte porphobilinogen deaminase. A;Reference number: A25508; MUID:86312872 A;Accession: A25508 A;Molecule type: mRNA A;Residues: 18-176,'L',178-348,'T',350-361 A;Cross-references: GB:X04217 R;Lannfelt, L.; Wetterberg, L.; Lilius, L.; Thunell, S.; Joernvall, H.; Pavlu, B.; Wielburski, A.; Gellerfors, P. Scand. J. Clin. Lab. Invest. 49, 677-684, 1989 A;Title: Porphobilinogen deaminase in human erythrocytes: purification of two forms with apparent molecular weights of 40 kDa and 42 kDa. A;Reference number: A60438 A;Accession: A60438 A;Molecule type: protein A;Residues: 18-36 A;Note: this amino-terminal sequence represents a form from erythropoietic tissues R;Chretien, S.; Dubart, A.; Beaupain, D.; Raich, N.; Grandchamp, B.; Rosa, J.; Goossens, M.; Romeo, P.H. Proc. Natl. Acad. Sci. U.S.A. 85, 6-10, 1988 A;Title: Alternative transcription and splicing of the human porphobilinogen deaminase gene result either in tissue-specific or in housekeeping expression. A;Reference number: I60127; MUID:88124819 A;Accession: I60127 A;Status: translation not shown; translated from GB/EMBL/DDBJ A;Molecule type: DNA A;Residues: 1-11 A;Cross-references: GB:M18799; NID:g189641; CDS_PID:g189644 C;Genetics: A;Gene: GDB:HMBS; PBGD A;Cross-references: GDB:120528 A;Map position: 11q23.3-11q23.3 A;Introns: 11/3; 29/3; 54/1; 70/3; 89/2; 115/2; 141/2; 166/3; 204/3; 217/3; 257/3; 275/3; 304/3 C;Function: A;Description: catalyzes the stepwise polymerization of four molecules of porphobilinogen to hydroxymethylbilane (uroporphyrinogen precursor) and four molecules of ammonia A;Pathway: porphyrin biosynthesis A;Note: acting with uroporphyrinogen-III synthase (cosynthase), which cyclizes hydroxymethylbilane, this enzyme produces uroporphyrinogen III the precursor for porphyrins C;Superfamily: hydroxymethylbilane synthase C;Keywords: alternative initiators; alternative splicing; ammonia-lyase; carbon-nitrogen lyase; porphyrin biosynthesis F;1-361/Product: hydroxymethylbilane synthase, nonerythropoietic #status predicted F;18-361/Product: hydroxymethylbilane synthase, erythropoietic #status experimental >IBHUN MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTG DKILDTALSKIGEKSLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPH DAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKMDEQ QEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHD PETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIH VPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNLGISLANLLLSKGAKNILDVARQLNDA H SWISSPROT:HEM3_YERPE ID HEM3_YERPE STANDARD; PRT; 183 AA. AC P46355; 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 PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (PBG) (HYDROXYMETHYLBILANE DE SYNTHASE) (HMBS) (PRE-UROPORPHYRINOGEN SYNTHASE) (FRAGMENT). GN HEMC. OS YERSINIA PESTIS. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=EV 40; RA TROTOT P., SISMEIRO O., VIVAR S.C., GLASER P., DANCHIN A.; RL SUBMITTED (MAR-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: TETRAPOLYMERISATION OF THE MONOPYRROLE PBG INTO THE CC HYDROXYMETHYLBILANE PREUROPORPHYRINOGEN IN SEVERAL DISCRETE STEPS. CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- SUBUNIT: MONOMER. CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- COFACTOR: COVALENTLY BINDS A DIPYRROMETHANE COFACTOR TO WHICH CC THE PORPHOBILINOGEN SUBUNITS ARE ADDED. CC -!- SIMILARITY: STRONG, TO OTHER EUKARYOTIC AND PROKARYOTIC HMBS. DR EMBL; U22968; G726352; -. DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM. KW PORPHYRIN BIOSYNTHESIS; LYASE. FT NON_TER 183 183 SQ SEQUENCE 183 AA; 20088 MW; 05594B07 CRC32; >HEM3_YERPE MLDKIIRIATRQSPLALWQAHYVQHLLQANHPGLQIELVPMVTRGDIILDTPLAKVGGKG LFVKELELALLDGRADIAVHSMKDVPIAFPEGLGLVTICEREDPRDAFVSSHYAHLDDLP AGSVVGTSSLRRQCQLRERRPDLIIRDLRGNVGTRLAKLDNGDYQAIILAVAGLKRLGLG KPN SWISSPROT:HEM3_YERIN ID HEM3_YERIN STANDARD; PRT; 183 AA. AC P30527; DT 01-APR-1993 (REL. 25, CREATED) DT 01-APR-1993 (REL. 25, LAST SEQUENCE UPDATE) DT 01-FEB-1995 (REL. 31, LAST ANNOTATION UPDATE) DE PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (PBG) (HYDROXYMETHYLBILANE DE SYNTHASE) (HMBS) (PRE-UROPORPHYRINOGEN SYNTHASE) (FRAGMENT). GN HEMC. OS YERSINIA INTERMEDIA. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RA GLASER P., SISMEIRO O., DANCHIN A.; RL SUBMITTED (JUN-1992) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: TETRAPOLYMERISATION OF THE MONOPYRROLE PBG INTO THE CC HYDROXYMETHYLBILANE PREUROPORPHYRINOGEN IN SEVERAL DISCRETE STEPS. CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- SUBUNIT: MONOMER. CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- COFACTOR: COVALENTLY BINDS A DIPYRROMETHANE COFACTOR TO WHICH CC THE PORPHOBILINOGEN SUBUNITS ARE ADDED. CC -!- SIMILARITY: STRONG, TO OTHER EUKARYOTIC AND PROKARYOTIC HMBS. DR EMBL; X66781; G48614; -. DR PIR; S24980; S24980. DR HSSP; P06983; 1PDA. DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM. KW PORPHYRIN BIOSYNTHESIS; LYASE. FT NON_TER 183 183 SQ SEQUENCE 183 AA; 20034 MW; E979D327 CRC32; >HEM3_YERIN MLDKIIRIATRQSPLALWQAHYVQHLLQANHPGLQVELVPMVTRGDIILDTPLAKVGGKG LFVKELELALLDGRADIAVHSMKDVPVAFPEGLGLVTICEPDDPRDAFVSPHFAHIDDLP AGSIVGNSSLRRQCQLRERRPDLIIRDLRGNVGTRLAKLDNGDYHAIILAVAGLNRLGLA SRI SWISSPROT:HEM3_YEAST ID HEM3_YEAST STANDARD; PRT; 327 AA. AC P28789; DT 01-DEC-1992 (REL. 24, CREATED) DT 01-DEC-1992 (REL. 24, LAST SEQUENCE UPDATE) DT 01-FEB-1995 (REL. 31, LAST ANNOTATION UPDATE) DE PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (PBG) (HYDROXYMETHYLBILANE DE SYNTHASE) (HMBS) (PRE-UROPORPHYRINOGEN SYNTHASE). GN HEM3. OS SACCHAROMYCES CEREVISIAE (BAKER'S YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 92374992. RA KENG T., RICHARD C., LAROCQUE R.; RL MOL. GEN. GENET. 234:233-243(1992). CC -!- FUNCTION: TETRAPOLYMERISATION OF THE MONOPYRROLE PBG INTO THE CC HYDROXYMETHYLBILANE PREUROPORPHYRINOGEN IN SEVERAL DISCRETE STEPS. CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- PATHWAY: THIRD STEP IN PORPHYRIN BIOSYNTHESIS BY THE SHEMIN CC PATHWAY. INVOLVED IN HEME BIOSYNTHESIS. CC -!- COFACTOR: COVALENTLY BINDS A DIPYRROMETHANE COFACTOR TO WHICH CC THE PORPHOBILINOGEN SUBUNITS ARE ADDED. CC -!- SIMILARITY: STRONG, TO OTHER EUKARYOTIC AND PROKARYOTIC HMBS. DR EMBL; Z11745; G3771; -. DR PIR; S20129; S20129. DR PIR; S25071; S25071. DR HSSP; P06983; 1PDA. DR LISTA; SC00432; HEM3. DR SGD; L0000762; HEM3. DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; LYASE. FT BINDING 251 251 PYRROMETHANE COFACTOR (BY SIMILARITY). SQ SEQUENCE 327 AA; 36674 MW; 3CB2A9D9 CRC32; >HEM3_YEAST MGPETLHIGGRKSKLAVIQSNHVLKLIEEKYPDYDCKVFTLQTLGDQIQFKPLYSFGGKA LWTKELEDHLYHDDPSKKLDLIVHSLKDMPTLLPEGFELGGITKRVDPTDCLVMPFYSAY KSLDDLPDGGIVGTSSVRRSAQLKRKYPHLKFESVRGNIQTRLQKLDDPKSPYQCIILAS AGLMRMGLENRITQRFHSDTMYHAVGQGALGIEIRKGDTKMMKILDEICDLNATICCLSE RALMRTLEGGCSVPIGVESKYNEETKKLLLKAIVVDVEGTEAVEDEIEMLIENVKEDSMA CGKILAERMIADGAKKILDEINLDRIK SWISSPROT:HEM3_SCHPO ID HEM3_SCHPO STANDARD; PRT; 125 AA. AC Q09899; DT 01-FEB-1996 (REL. 33, CREATED) DT 01-FEB-1996 (REL. 33, LAST SEQUENCE UPDATE) DT 01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE) DE PUTATIVE PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (PBG) DE (HYDROXYMETHYLBILANE SYNTHASE) (HMBS) (PRE-UROPORPHYRINOGEN SYNTHASE) DE (FRAGMENT). GN SPAC24B11.13. OS SCHIZOSACCHAROMYCES POMBE (FISSION YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=972; RA ODELL C., CHURCHER C.M., BARRELL B.G., RAJANDREAM M.A., WALSH S.V.; RL SUBMITTED (NOV-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: TETRAPOLYMERISATION OF THE MONOPYRROLE PBG INTO THE CC HYDROXYMETHYLBILANE PREUROPORPHYRINOGEN IN SEVERAL DISCRETE STEPS CC (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- PATHWAY: THIRD STEP IN PORPHYRIN BIOSYNTHESIS BY THE SHEMIN CC PATHWAY. INVOLVED IN HEME BIOSYNTHESIS. CC -!- COFACTOR: COVALENTLY BINDS A DIPYRROMETHANE COFACTOR TO WHICH CC THE PORPHOBILINOGEN SUBUNITS ARE ADDED (BY SIMILARITY). CC -!- SIMILARITY: STRONG, TO OTHER EUKARYOTIC AND PROKARYOTIC HMBS. DR EMBL; Z67757; E208900; -. KW HYPOTHETICAL PROTEIN; PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; KW LYASE. FT NON_TER 125 125 SQ SEQUENCE 125 AA; 14151 MW; 5AFDFF36 CRC32; >HEM3_SCHPO MPSCTSFPIGTRKSKLAVIQSEIIREELEKHYPHLEFPIISRDTIGDEILSKALFEFKRQ LAKSLWTRELEALLVTNQCRILVHSLKDLPSEMPDGMVIACIPKRSCPLDAIVFKAGSHY KTVAD SWISSPROT:HEM3_RAT ID HEM3_RAT STANDARD; PRT; 344 AA. AC P19356; DT 01-NOV-1990 (REL. 16, CREATED) DT 01-NOV-1990 (REL. 16, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8), ERYTHROCYTE DE (HYDROXYMETHYLBILANE SYNTHASE) (HMBS) (PRE-UROPORPHYRINOGEN SYNTHASE). GN HMBS. OS RATTUS NORVEGICUS (RAT). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 88217524. RA STUBNICER A.C., PICAT C., GRANDCHAMP B.; RL NUCLEIC ACIDS RES. 16:3102-3102(1988). CC -!- FUNCTION: TETRAPOLYMERISATION OF THE MONOPYRROLE PBG INTO THE CC HYDROXYMETHYLBILANE PREUROPORPHYRINOGEN IN SEVERAL DISCRETE STEPS. CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- PATHWAY: THIRD STEP IN PORPHYRIN BIOSYNTHESIS BY THE SHEMIN CC PATHWAY. INVOLVED IN HEME BIOSYNTHESIS. CC -!- COFACTOR: COVALENTLY BINDS A DIPYRROMETHANE COFACTOR TO WHICH CC THE PORPHOBILINOGEN SUBUNITS ARE ADDED. CC -!- ALTERNATIVE PRODUCTS: THERE ARE TWO ISOZYMES OF THIS ENZYME IN CC MAMMALS; THEY ARE PRODUCED BY THE SAME GENE FROM ALTERNATIVE CC SPLICING. CC -!- SIMILARITY: STRONG, TO OTHER EUKARYOTIC AND PROKARYOTIC HMBS. DR EMBL; X06827; G56856; -. DR PIR; S00746; IBRTE. DR HSSP; P06983; 1PDA. DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; LYASE; KW ALTERNATIVE SPLICING. FT BINDING 244 244 PYRROMETHANE COFACTOR (BY SIMILARITY). SQ SEQUENCE 344 AA; 37790 MW; 70590B70 CRC32; >HEM3_RAT MRVIRVGTRKSQLARIQTDTVVAMLKTLYPGIQFEIIAMSTTGDKILDTALSKIGEKSLF TKELENALEKNEVDLVVHSLKDVPTILPPGFTIGAICKRENPCDAVVFEGKFIGKTLETL PEKSAVGTSSLRRVAQLQRKFPHLEFKSIRGNLNTRLRKLDEQLEFSAIILAVAGLQRMG WQNRVGQILHPEECMYAVGQGALAVEVRAKDQDILDLVGVLHDPETLLRCIAERDFLRHL EGGCSVPVAVHTVMKDGQLYLTGGVWSLDGSDSMQETMQATIQVPVQQEDGPEDDPQLVG ITARNIPRGAQLAAENLGISLASLLLNKGAKNILDVARQLNDVR SWISSPROT:HEM3_MYCTU ID HEM3_MYCTU STANDARD; PRT; 155 AA. AC Q11173; 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 PROBABLE PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (PBG) DE (HYDROXYMETHYLBILANE SYNTHASE) (HMBS) (PRE-UROPORPHYRINOGEN SYNTHASE) DE (FRAGMENT). GN HEMC OR MTCY20G9.37. OS MYCOBACTERIUM TUBERCULOSIS. OC PROKARYOTA; FIRMICUTES; ACTINOMYCETALES; MYCOBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=H37RV; RA MURPHY L., HARRIS D., BARRELL B.G., RAJANDREAM M.A., WALSH S.V.; RL SUBMITTED (JUL-1996) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: TETRAPOLYMERISATION OF THE MONOPYRROLE PBG INTO THE CC HYDROXYMETHYLBILANE PREUROPORPHYRINOGEN IN SEVERAL DISCRETE STEPS CC (BY SIMILARITY). CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- COFACTOR: COVALENTLY BINDS A DIPYRROMETHANE COFACTOR TO WHICH CC THE PORPHOBILINOGEN SUBUNITS ARE ADDED (BY SIMILARITY). CC -!- SIMILARITY: STRONG, TO OTHER EUKARYOTIC AND PROKARYOTIC HMBS. DR EMBL; Z77162; E255045; -. KW PORPHYRIN BIOSYNTHESIS; LYASE. FT NON_TER 155 155 SQ SEQUENCE 155 AA; 16021 MW; D64B8B7C CRC32; >HEM3_MYCTU MIRIGTRGSLLATTQAATVRDALIAGGHSAELVTISTEGDRSMAPIASLGVGVFTTALRE AMEAGLVDAAVHSYKDLPTAADPRFTVAAIPPRNDPRDAVVARDGLTLGELPVGSLVGTS SPRRAAQLRALGLGLEIRPLRGNLDTRLNKVSSGD SWISSPROT:HEM3_MOUSE ID HEM3_MOUSE STANDARD; PRT; 361 AA. AC P22907; DT 01-AUG-1991 (REL. 19, CREATED) DT 01-AUG-1991 (REL. 19, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (HYDROXYMETHYLBILANE SYNTHASE) DE (HMBS) (PRE-UROPORPHYRINOGEN SYNTHASE). GN HMBS OR UROS1. OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 89359283. RA BEAUMONT C., PORCHER C., PICAT C., NORDMANN Y., GRANDCHAMP B.; RL J. BIOL. CHEM. 264:14829-14834(1989). CC -!- FUNCTION: TETRAPOLYMERISATION OF THE MONOPYRROLE PBG INTO THE CC HYDROXYMETHYLBILANE PREUROPORPHYRINOGEN IN SEVERAL DISCRETE STEPS. CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- PATHWAY: THIRD STEP IN PORPHYRIN BIOSYNTHESIS BY THE SHEMIN CC PATHWAY. INVOLVED IN HEME BIOSYNTHESIS. CC -!- COFACTOR: COVALENTLY BINDS A DIPYRROMETHANE COFACTOR TO WHICH CC THE PORPHOBILINOGEN SUBUNITS ARE ADDED. CC -!- ALTERNATIVE PRODUCTS: THERE ARE TWO ISOZYMES OF THIS ENZYME IN CC MAMMALS; THEY ARE PRODUCED BY THE SAME GENE FROM ALTERNATIVE CC SPLICING. THE NONERYTHROPOIETIC FORM DIFFERS FROM THE ERYTHROCYTE CC FORM BY AN EXTRA N-TERMINAL 18 RESIDUES. CC -!- SIMILARITY: STRONG, TO OTHER EUKARYOTIC AND PROKARYOTIC HMBS. DR EMBL; M28666; G387506; ALT_SEQ. DR EMBL; M28663; G387506; JOINED. DR EMBL; M28664; G387506; JOINED. DR EMBL; M28665; G387506; JOINED. DR EMBL; M28666; G387507; -. DR EMBL; M28663; G387507; JOINED. DR EMBL; M28664; G387507; JOINED. DR EMBL; M28665; G387507; JOINED. DR PIR; A36513; IBMSN. DR HSSP; P06983; 1PDA. DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; LYASE; KW ALTERNATIVE SPLICING. FT BINDING 261 261 PYRROMETHANE COFACTOR (BY SIMILARITY). FT VARSPLIC 1 17 MISSING (IN ERYTHROCYTE FORM). SQ SEQUENCE 361 AA; 39302 MW; 734DCB5A CRC32; >HEM3_MOUSE MSGNGGAATTAEENGSKMRVIRVGTRKSQLARIQTETVVAMLKALYPGIQFEIIAMSTTG DKIVDTALSKIGEKSLFTKELENALEKNEVDLVVHSLKDVPTILPPGFTIGAICKRQNPC DAVVFHPKFIGKTLETLPEKSAVGTSSLRRVAQLQRKFPNLEFKSIRGNLNTRLRKLDEL QEFSAIVLAVAGLQRMGWQNRVGQILHPEECMYAVGQGALAVEVRAKDQDILDLVSVLHD PETLLRCIAERAFLRHLEGGCSVPVAVHTVIKDGQLYLTGGVWSLDGSDSMQETMQATIQ VPVQQEDGPEDDPQLVGITARNIPRGAQLAAENLGISLASLLLNKGAKNILDVARQLNDV R SWISSPROT:HEM3_HUMAN ID HEM3_HUMAN STANDARD; PRT; 361 AA. AC P08397; P08396; DT 01-AUG-1988 (REL. 08, CREATED) DT 01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (HYDROXYMETHYLBILANE SYNTHASE) DE (HMBS) (PRE-UROPORPHYRINOGEN SYNTHASE). GN HMBS OR PBGD. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 87133520. RA GRANDCHAMP B., DE VERNEUIL H., BEAUMONT C., CHRETIEN S., WALTER O., RA NORDMANN Y.; RL EUR. J. BIOCHEM. 162:105-110(1987). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 93162658. RA YOO H.-W., WARNER C.A., CHEN C.-H., DESNICK R.J.; RL GENOMICS 15:21-29(1993). RN [3] RP SEQUENCE OF 18-361 FROM N.A. RX MEDLINE; 86312872. RA RAICH N., ROMEO P.H., DUBART A., BEAUPAIN D., COHEN-SOLAL M., RA GOOSSENS M.; RL NUCLEIC ACIDS RES. 14:5955-5968(1986). RN [4] RP REVIEW ON AIP VARIANTS. RX MEDLINE; 95170732. RA ASTRIN K.N., DESNICK R.J.; RL HUM. MUTAT. 4:243-252(1994). RN [5] RP VARIANTS AIP GLN-167 AND GLN-173. RX MEDLINE; 91056151. RA DELFAU M.H., PICAT C., DE ROOIJ F.W.M., HAMER K., BOGARD M., RA WILSON J.H.P., DEYBACH J.C., NORDMANN Y., GRANDCHAMP B.; RL J. CLIN. INVEST. 86:1511-1516(1990). RN [6] RP VARIANTS AIP GLN-149 AND ARG-245. RX MEDLINE; 91328149. RA DELFAU M.H., PICAT C., DE ROOIJ F., VOORTMAN G., DEYBACH J.C., RA NORDMANN Y., GRANDCHAMP B.; RL AM. J. HUM. GENET. 49:421-428(1991). RN [7] RP VARIANT AIP TRP-167. RX MEDLINE; 92359114. RA GU X.-F., DE ROOIJ F., VOORTMAN G., TE VELDE K., NORDMANN Y., RA GRANDCHAMP B.; RL AM. J. HUM. GENET. 51:660-665(1992). RN [8] RP VARIANTS AIP LYS-34; GLN-167; ARG-177 AND ASN-256. RX MEDLINE; 93052213. RA MGONE C.S., LANYON W.G., MOORE M.R., CONNOR J.M.; RL HUM. GENET. 90:12-16(1992). RN [9] RP VARIANTS AIP TRP-167 AND GLN-173. RX MEDLINE; 93250838. RA KAUPPINEN R., PELTONEN L., PIHLAJA H., MUSTAJOKI P.; RL HUM. MUTAT. 1:392-396(1992). RN [10] RP VARIANTS AIP ARG-247; THR-252 AND VAL-252. RX MEDLINE; 94085963. RA MGONE C.S., LANYON W.G., MOORE M.R., LOUIE G.V., CONNOR J.M.; RL HUM. GENET. 92:619-622(1993). RN [11] RP VARIANT AIP HIS-26. RX MEDLINE; 94004882. RA LLEWELLYN D.H., WHATLEY S., ELDER G.H.; RL HUM. MOL. GENET. 2:1315-1316(1993). RN [12] RP VARIANT AIP ARG-111. RX MEDLINE; 94093570. RA GU X.-F., DE ROOIJ F., DE BAAR E., BRUYLAND M., LISSENS W., RA NORDMANN Y., GRANDCHAMP B.; RL HUM. MOL. GENET. 2:1735-1736(1993). RN [13] RP VARIANTS AIP THR-31; SER-55; LEU-149; LYS-223 AND LYS-250. RX MEDLINE; 94095201. RA GU X.-F., DE ROOIJ F., VOORTMAN G., TE VELDE K., DEYBACH J.-C., RA NORDMANN Y., GRANDCHAMP B.; RL HUM. GENET. 93:47-52(1994). RN [14] RP VARIANT AIP TRP-201. RX MEDLINE; 94095203. RA LUNDIN G., WEDELL A., THUNELL S., ANVRET M.; RL HUM. GENET. 93:59-62(1994). RN [15] RP VARIANTS AIP GLN-116; TRP-173; ARG-177; ILE-269 AND ARG-274. RX MEDLINE; 94362681. RA MGONE C.S., LANYON W.G., MOORE M.R., LOUIE G.V., CONNOR J.M.; RL HUM. MOL. GENET. 3:809-811(1994). RN [16] RP VARIANTS AIP PHE-93; TRP-116; TRP-201 AND PHE-247. RX MEDLINE; 95051536. RA CHEN C.-H., ASTRIN K.H., LEE G., ANDERSON K.E., DESNICK R.J.; RL J. CLIN. INVEST. 94:1927-1937(1994). RN [17] RP VARIANTS AIP. RX MEDLINE; 95276733. RA KAUPPINEN R., MUSTAJOKI S., PIHLAJA H., PELTONEN L., MUSTAJOKI P.; RL HUM. MOL. GENET. 4:215-222(1995). RN [18] RP VARIANTS AIP LEU-119 AND ALA-250. RX MEDLINE; 96423328. RA LUNDIN G., HASHEMI J., FLODERUS Y., THUNELL S., SAGEN E., LAEGREID A., RA WASSIF W., PETERS T., ANVRET M.; RL J. MED. GENET. 32:979-981(1995). CC -!- FUNCTION: TETRAPOLYMERISATION OF THE MONOPYRROLE PBG INTO THE CC HYDROXYMETHYLBILANE PREUROPORPHYRINOGEN IN SEVERAL DISCRETE STEPS. CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- PATHWAY: THIRD STEP IN PORPHYRIN BIOSYNTHESIS BY THE SHEMIN CC PATHWAY. INVOLVED IN HEME BIOSYNTHESIS. CC -!- COFACTOR: COVALENTLY BINDS A DIPYRROMETHANE COFACTOR TO WHICH CC THE PORPHOBILINOGEN SUBUNITS ARE ADDED. CC -!- DISEASE: DEFECTS IN HMBS ARE THE CAUSE OF ACUTE INTERMITTENT CC PORPHYRIA (AIP); AN AUTOSOMAL DOMINANT DISEASE CHARACTERIZED BY CC ACUTE ATTACKS OF NEUROLOGICAL DYSFUNCTIONS WITH ABDOMINAL PAIN, CC HYPERTENSION, TACHYCARDIA, AND PERIPHERAL NEUROPATHY. MOST ATTACKS CC ARE PRECIPITATED BY DRUGS, ALCOHOL, CALORIC DEPRIVATION, CC INFECTIONS, OR ENDOCRINE FACTORS. CC -!- ALTERNATIVE PRODUCTS: THERE ARE TWO ISOZYMES OF THIS ENZYME IN CC MAMMALS; THEY ARE PRODUCED BY THE SAME GENE FROM ALTERNATIVE CC SPLICING. THE NONERYTHROPOIETIC FORM DIFFERS FROM THE ERYTHROCYTE CC FORM BY AN EXTRA N-TERMINAL 18 RESIDUES. CC -!- SIMILARITY: STRONG, TO OTHER EUKARYOTIC AND PROKARYOTIC HMBS. DR EMBL; X04808; G35309; -. DR EMBL; M95623; G292386; -. DR EMBL; M95623; G292385; -. DR EMBL; X04217; G35307; -. DR EMBL; X68018; G35305; -. DR PIR; A26416; IBHUN. DR HSSP; P06983; 1PDA. DR MIM; 176000; -. DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; LYASE; KW ALTERNATIVE SPLICING; DISEASE MUTATION. FT BINDING 261 261 PYRROMETHANE COFACTOR (BY SIMILARITY). FT VARSPLIC 1 17 MISSING (IN ERYTHROCYTE FORM). FT VARIANT 26 26 R -> H (IN AIP). FT VARIANT 31 31 A -> T (IN AIP). FT VARIANT 34 34 Q -> K (IN AIP). FT VARIANT 55 55 A -> S (IN AIP). FT VARIANT 93 93 V -> F (IN AIP; LOSS OF ACTIVITY). FT VARIANT 98 98 K -> R (IN AIP). FT VARIANT 111 111 G -> R (IN AIP). FT VARIANT 116 116 R -> Q (IN AIP). FT VARIANT 116 116 R -> W (IN AIP; LOSS OF ACTIVITY). FT VARIANT 119 119 P -> L (IN AIP). FT VARIANT 149 149 R -> L (IN AIP). FT VARIANT 149 149 R -> Q (IN AIP). FT VARIANT 167 167 R -> Q (IN AIP). FT VARIANT 167 167 R -> W (IN AIP). FT VARIANT 173 173 R -> Q (IN AIP; 0.6% OF WILD-TYPE FT ACTIVITY). FT VARIANT 173 173 R -> W (IN AIP). FT VARIANT 177 177 L -> R (IN AIP). FT VARIANT 195 195 R -> C (IN AIP). FT VARIANT 201 201 R -> W (IN AIP; RESIDUAL ACTIVITY). FT VARIANT 223 223 E -> K (IN AIP). FT VARIANT 225 225 R -> G (IN AIP). FT VARIANT 238 238 L -> R (IN AIP). FT VARIANT 245 245 L -> R (IN AIP). FT VARIANT 247 247 C -> F (IN AIP; RESIDUAL ACTIVITY). FT VARIANT 247 247 C -> R (IN AIP). FT VARIANT 250 250 E -> A (IN AIP). FT VARIANT 250 250 E -> K (IN AIP). FT VARIANT 252 252 A -> T (IN AIP). FT VARIANT 252 252 A -> V (IN AIP). FT VARIANT 256 256 H -> N (IN AIP). FT VARIANT 269 269 T -> I (IN AIP). FT VARIANT 274 274 G -> R (IN AIP). FT VARIANT 280 280 G -> R (IN AIP). FT CONFLICT 177 177 L -> M (IN REF. 2). FT CONFLICT 210 210 E -> K (IN REF. 1). FT CONFLICT 349 349 N -> T (IN REF. 3). SQ SEQUENCE 361 AA; 39330 MW; 45F0D074 CRC32; >HEM3_HUMAN MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTG DKILDTALSKIGEKSLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPH DAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQ QEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHD PETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIH VPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNLGISLANLLLSKGAKNILDVARQLNDA H SWISSPROT:HEM3_EUGGR ID HEM3_EUGGR STANDARD; PRT; 480 AA. AC P13446; DT 01-JAN-1990 (REL. 13, CREATED) DT 01-JAN-1990 (REL. 13, LAST SEQUENCE UPDATE) DT 01-FEB-1995 (REL. 31, LAST ANNOTATION UPDATE) DE PORPHOBILINOGEN DEAMINASE PRECURSOR (EC 4.3.1.8) (PBG) DE (HYDROXYMETHYLBILANE SYNTHASE) (HMBS) (PRE-UROPORPHYRINOGEN SYNTHASE). OS EUGLENA GRACILIS. OC EUKARYOTA; PLANTA; PHYCOPHYTA; EUGLENOPHYTA. RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=Z; RX MEDLINE; 90005485. RA SHARIF A.L., SMITH A.G., ABELL C.; RL EUR. J. BIOCHEM. 184:353-359(1989). CC -!- FUNCTION: TETRAPOLYMERISATION OF THE MONOPYRROLE PBG INTO THE CC HYDROXYMETHYLBILANE PREUROPORPHYRINOGEN IN SEVERAL DISCRETE STEPS. CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC INVOLVED IN CHLOROPHYLL BIOSYNTHESIS. CC -!- COFACTOR: COVALENTLY BINDS A DIPYRROMETHANE COFACTOR TO WHICH CC THE PORPHOBILINOGEN SUBUNITS ARE ADDED. CC -!- SIMILARITY: STRONG, TO OTHER EUKARYOTIC AND PROKARYOTIC HMBS. DR EMBL; X15743; G18412; -. DR PIR; S06109; IBEG. DR HSSP; P06983; 1PDA. DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; LYASE; CHLOROPLAST; KW TRANSIT PEPTIDE. FT TRANSIT 1 139 CHLOROPLAST. FT CHAIN 140 480 PORPHOBILINOGEN DEAMINASE. FT BINDING 395 395 PYRROMETHANE COFACTOR (BY SIMILARITY). SQ SEQUENCE 480 AA; 51743 MW; 2FE1A917 CRC32; >HEM3_EUGGR MYCGRYETIGETRGNSLNVFIGAAAGFVAAVALINSGLATSFYSTPVRAVPQVIVPSSLA ASSQLPVVPKETNIQVNSAQILYPDSTVKGQERTITILGVCSFLSASLFYIWKQFGMKAR TTKPADLQEVSGGRIWSLASTTGSNIGAGKTVRVATRKSPLAMWQAEFIQSELERLWPGI TVELQPMSTRGDKILDSPLAKVGGKGLFVKELETALLENRSDIAVHSTKDVPMELPEGLV LGVICKRHDPCDAIVFPKGSNLKSLEDLPHGARVGTSSLRRQCQLLLKRPDLKFLELRGN VNTRLAKLDSGDYDAIILAAAGLKRLGFSDRVLPGETNIIDPNVMCPAAGQGALSIELRT NDPEIAALLEPLHHIPDAVTVACERAMNRRLNGGCQVPISGFAQLKDGQLRMEARVGSVT GKGPLIIQSKTFRLPWSGRTWPQLQKESEALGVEVADMLLADGAQAYLDEAYASRTLGWA SWISSPROT:HEM3_ERWCH ID HEM3_ERWCH STANDARD; PRT; 89 AA. AC P40129; DT 01-FEB-1995 (REL. 31, CREATED) DT 01-FEB-1995 (REL. 31, LAST SEQUENCE UPDATE) DT 01-FEB-1995 (REL. 31, LAST ANNOTATION UPDATE) DE PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (PBG) (HYDROXYMETHYLBILANE DE SYNTHASE) (HMBS) (PRE-UROPORPHYRINOGEN SYNTHASE) (FRAGMENT). GN HEMC. OS ERWINIA CHRYSANTHEMI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=B374; RX MEDLINE; 89055613. RA DANCHIN A., LENZEN G.; RL ADV. SECOND MESSENGER PHOSPHOPROTEIN RES. 12:7-28(1988). CC -!- FUNCTION: TETRAPOLYMERISATION OF THE MONOPYRROLE PBG INTO THE CC HYDROXYMETHYLBILANE PREUROPORPHYRINOGEN IN SEVERAL DISCRETE STEPS. CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- SUBUNIT: MONOMER (BY SIMILARITY). CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC INVOLVED IN CHLOROPHYLL BIOSYNTHESIS. CC -!- COFACTOR: COVALENTLY BINDS A DIPYRROMETHANE COFACTOR TO WHICH CC THE PORPHOBILINOGEN SUBUNITS ARE ADDED. CC -!- SIMILARITY: STRONG, TO OTHER EUKARYOTIC AND PROKARYOTIC HMBS. DR EMBL; X63207; G41671; -. DR PIR; S23698; S23698. DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; LYASE. FT NON_TER 89 89 SQ SEQUENCE 89 AA; 9922 MW; E93BEC00 CRC32; >HEM3_ERWCH MVDTILRIATRQSPLALWQAHFVQQRLEACHPGLRVELVPMVTRGXLLLDTPLAKVGGKG LFVKELELALLENRADIAVHSMKDVPVEF SWISSPROT:HEM3_ECOLI ID HEM3_ECOLI STANDARD; PRT; 313 AA. AC P06983; DT 01-APR-1988 (REL. 07, CREATED) DT 01-APR-1988 (REL. 07, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (PBG) (HYDROXYMETHYLBILANE DE SYNTHASE) (HMBS) (PRE-UROPORPHYRINOGEN SYNTHASE). GN HEMC OR POPE. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 86312890. RA THOMAS S.D., JORDAN P.M.; RL NUCLEIC ACIDS RES. 14:6215-6226(1986). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12 / CS520; RX MEDLINE; 89041586. RA ALEFOUNDER P.R.; RL NUCLEIC ACIDS RES. 16:9871-9871(1988). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE; 92358234. RA DANIELS D.L., PLUNKETT G. III, BURLAND V.D., BLATTNER F.R.; RL SCIENCE 257:771-778(1992). RN [4] RP SEQUENCE OF 1-89 FROM N.A. RC STRAIN=K12; RA GLASER P., SISMEIRO O., DANCHIN A.; RL SUBMITTED (JUN-1992) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [5] RP SEQUENCE OF 1-10. RX MEDLINE; 89025710. RA JORDAN P.M., THOMAS S.D., WARREN M.J.; RL BIOCHEM. J. 254:427-435(1988). RN [6] RP COFACTOR ATTACHMENT SITE. RX MEDLINE; 89061636. RA MILLER A.D., HART G.J., PACKMAN L.C., BATTERSBY A.R.; RL BIOCHEM. J. 254:915-918(1988). RN [7] RP INACTIVATION BY PYRIDOXAL 5'-PHOSPHATE. RX MEDLINE; 90056403. RA MILLER A.D., PACKMAN L.C., HART G.J., ALEFOUNDER P.R., ABELL C., RA BATTERSBY A.R.; RL BIOCHEM. J. 262:119-124(1989). RN [8] RP MUTAGENESIS OF LYS-55 AND LYS-59. RX MEDLINE; 91054416. RA HADENER A., ALEFOUNDER P.R., HART G.J., ABELL C., BATTERSBY A.R.; RL BIOCHEM. J. 271:487-491(1990). RN [9] RP MUTAGENESIS OF ARGININES. RX MEDLINE; 91222140. RA LANDER M., PITT A.R., ALEFOUNDER P.R., BARDY D., ABELL C., RA BATTERSBY A.R.; RL BIOCHEM. J. 275:447-452(1991). RN [10] RP MUTAGENESIS OF ARGININES. RX MEDLINE; 92082485. RA JORDAN P.M., WOODCOCK S.C.; RL BIOCHEM. J. 280:445-449(1991). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). RX MEDLINE; 92396207. RA LOUIE G.V., BROWNLIE P.D., LABERT R., COOPER J.B., BLUNDELL T.L., RA WOOD S.P., WARREN M.J., WOODCOCK S.C., JORDAN P.M.; RL NATURE 359:33-39(1992). CC -!- FUNCTION: TETRAPOLYMERISATION OF THE MONOPYRROLE PBG INTO THE CC HYDROXYMETHYLBILANE PREUROPORPHYRINOGEN IN SEVERAL DISCRETE STEPS. CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- SUBUNIT: MONOMER. CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC INVOLVED IN CHLOROPHYLL BIOSYNTHESIS. CC -!- ARGININE RESIDUES THAT ARE CLOSELY ASSOCIATED WITH ONE ANOTHER CC MIGHT BE INVOLVED IN SUBSTRATE BINDING. CC -!- COFACTOR: COVALENTLY BINDS A DIPYRROMETHANE COFACTOR TO WHICH CC THE PORPHOBILINOGEN SUBUNITS ARE ADDED. CC -!- SIMILARITY: STRONG, TO OTHER EUKARYOTIC AND PROKARYOTIC HMBS. DR EMBL; X04242; G41664; -. DR EMBL; X12614; G41666; -. DR EMBL; M87049; G148204; ALT_SEQ. DR EMBL; X66782; G41186; -. DR PIR; A25512; IBEC. DR PIR; S19283; S19283. DR PIR; S30695; S30695. DR PIR; S24974; S24974. DR PDB; 1PDA; 31-OCT-93. DR ECOGENE; EG10429; HEMC. DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM. KW PORPHYRIN BIOSYNTHESIS; LYASE; 3D-STRUCTURE. FT BINDING 242 242 PYRROMETHANE COFACTOR. FT MUTAGEN 7 7 R->L: NO LOSS OF ACTIVITY. FT MUTAGEN 11 11 R->L: LOSS OF ACTIVITY. FT MUTAGEN 55 55 K->Q: NO LOSS OF ACTIVITY. FT MUTAGEN 59 59 K->Q: 25 FOLD DECREASE IN ACTIVITY. FT MUTAGEN 101 101 R->L: NO LOSS OF ACTIVITY. FT MUTAGEN 131 131 R->L: COMPLETE LOSS OF ACTIVITY. FT MUTAGEN 132 132 R->L: COMPLETE LOSS OF ACTIVITY. FT MUTAGEN 155 155 R->L: LOSS OF ACTIVITY. FT MUTAGEN 176 176 R->L: LOSS OF ACTIVITY. FT CONFLICT 137 137 A -> G (IN REF. 3). FT CONFLICT 186 186 A -> G (IN REF. 3). FT CONFLICT 241 241 A -> G (IN REF. 2 AND 3). FT CONFLICT 261 261 G -> A (IN REF. 2 AND 3). FT CONFLICT 265 265 A -> R (IN REF. 3). FT STRAND 5 10 FT HELIX 14 30 FT TURN 32 33 FT STRAND 35 40 FT HELIX 44 47 FT TURN 61 63 FT HELIX 64 71 FT TURN 72 73 FT STRAND 77 81 FT HELIX 82 84 FT TURN 91 92 FT STRAND 93 98 FT STRAND 106 109 FT TURN 116 118 FT TURN 121 122 FT STRAND 124 126 FT HELIX 130 139 FT TURN 141 142 FT STRAND 144 146 FT HELIX 152 160 FT TURN 161 162 FT STRAND 166 170 FT HELIX 171 176 FT TURN 177 178 FT HELIX 180 182 FT STRAND 185 186 FT TURN 189 191 FT TURN 196 199 FT STRAND 201 206 FT TURN 207 208 FT HELIX 210 219 FT HELIX 222 237 FT TURN 238 239 FT TURN 242 243 FT STRAND 246 253 FT TURN 254 255 FT STRAND 256 264 FT TURN 266 267 FT STRAND 271 278 FT HELIX 280 296 FT TURN 297 298 FT HELIX 299 304 FT TURN 305 306 SQ SEQUENCE 313 AA; 33851 MW; F8DE1B52 CRC32; >HEM3_ECOLI MLDNVLRIATRQSPLALWQAHYVKDKLMASHPGLVVELVPMVTRGDVILDTPLAKVGGKG LFVKELEVALLENRADIAVHSMKDVPVEFPQGLGLVTICEREDPRDAFVSNNYDSLDALP AGSIVGTSSLRRQCQLAERRPDLIIRSLRGNVGTRLSKLDNGEYDAIILAVAGLKRLGLE SRIRAALPPEISLPAVGQGAVGIECRLDDSRTRELLAALNHHETALRVTAERAMNTRLEG ACQVPIGSYAELIDGEIWLRGLVGAPDGSQIIRGERRGAPQDAEQMGISLAEELLNNGAR EILAEVYNGDAPA SWISSPROT:HEM3_CHLVI ID HEM3_CHLVI STANDARD; PRT; 43 AA. AC P28464; DT 01-DEC-1992 (REL. 24, CREATED) DT 01-DEC-1992 (REL. 24, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (PBG) (HYDROXYMETHYLBILANE DE SYNTHASE) (HMBS) (PRE-UROPORPHYRINOGEN SYNTHASE) (FRAGMENT). GN HEMC. OS CHLOROBIUM VIBRIOFORME. OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; GREEN BACTERIA; OC CHLOROBIACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 92171712. RA MAJUMDAR D., AVISSAR Y.J., WYCHE J.H., BEALE S.I.; RL ARCH. MICROBIOL. 156:281-289(1991). CC -!- FUNCTION: TETRAPOLYMERISATION OF THE MONOPYRROLE PBG INTO THE CC HYDROXYMETHYLBILANE PREUROPORPHYRINOGEN IN SEVERAL DISCRETE STEPS. CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- SUBUNIT: MONOMER. CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC INVOLVED IN CHLOROPHYLL BIOSYNTHESIS. CC -!- COFACTOR: COVALENTLY BINDS A DIPYRROMETHANE COFACTOR TO WHICH CC THE PORPHOBILINOGEN SUBUNITS ARE ADDED. CC -!- SIMILARITY: STRONG, TO OTHER EUKARYOTIC AND PROKARYOTIC HMBS. DR EMBL; M59194; G144476; -. DR PIR; S27547; S27547. DR PIR; B48359; B48359. DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM. KW PORPHYRIN BIOSYNTHESIS; CHLOROPHYLL BIOSYNTHESIS; LYASE. FT NON_TER 43 43 SQ SEQUENCE 43 AA; 4670 MW; 2F9059CC CRC32; >HEM3_CHLVI MNISLKLVKTTGDVLLDSPLSKIGDMGLFTKDIEKHLLAGEID SWISSPROT:HEM3_BACSU ID HEM3_BACSU STANDARD; PRT; 314 AA. AC P16616; DT 01-AUG-1990 (REL. 15, CREATED) DT 01-AUG-1990 (REL. 15, LAST SEQUENCE UPDATE) DT 01-FEB-1995 (REL. 31, LAST ANNOTATION UPDATE) DE PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (PBG) (HYDROXYMETHYLBILANE DE SYNTHASE) (HMBS) (PRE-UROPORPHYRINOGEN SYNTHASE). GN HEMC. OS BACILLUS SUBTILIS. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 90236876. RA PETRICEK M., RUTBERG L., SCHROEDER I., HEDERSTEDT L.; RL J. BACTERIOL. 172:2250-2258(1990). CC -!- FUNCTION: TETRAPOLYMERISATION OF THE MONOPYRROLE PBG INTO THE CC HYDROXYMETHYLBILANE PREUROPORPHYRINOGEN IN SEVERAL DISCRETE STEPS. CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- SUBUNIT: MONOMER. CC -!- PATHWAY: FOURTH STEP IN PORPHYRIN BIOSYNTHESIS BY THE C5 PATHWAY. CC -!- COFACTOR: COVALENTLY BINDS A DIPYRROMETHANE COFACTOR TO WHICH CC THE PORPHOBILINOGEN SUBUNITS ARE ADDED. CC -!- SIMILARITY: STRONG, TO OTHER EUKARYOTIC AND PROKARYOTIC HMBS. DR EMBL; M32130; -; NOT_ANNOTATED_CDS. DR EMBL; M57676; G143037; -. DR PIR; C35252; IBBS. DR PIR; A42728; A42728. DR HSSP; P06983; 1PDA. DR SUBTILIST; BG10342; HEMC. DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM. KW PORPHYRIN BIOSYNTHESIS; LYASE. FT BINDING 242 242 PYRROMETHANE COFACTOR (BY SIMILARITY). SQ SEQUENCE 314 AA; 34838 MW; D0F269D0 CRC32; >HEM3_BACSU MMRTIKVGSRRSKLAMTQTKWVIQKLKEINPSFAFEIKEIVTKGDRIVDVTLSKVGGKGL FVKEIEQALLNEEIDMAVHSMKDMPAVLPEGLVIGCIPEREDPRDALISKNRVKLSEMKK GAVIGTSSLRRSAQLLIERPDLTIKWIRGNIDTRLQKLETEDYDAIILAAAGLSRMGWKQ DVVTEFLEPERCLPAVGQGALAIECRESDEELLALFSQFTDEYTKRTVLAERAFLNAMEG GCQVPIAGYSVLNGQDEIEMTGLVASPDGKIIFKETVTGNDPEEVGKRCAALMADKGAKD LIDRVKRELDEDGK TREMBL:E150950 ID E150950 PRELIMINARY; PRT; 2 AA. AC D28419_1; DT 24-SEP-1996 (EMBLREL. 48, CREATED) DT 24-SEP-1996 (EMBLREL. 48, LAST SEQUENCE UPDATE) DT 24-SEP-1996 (EMBLREL. 48, LAST ANNOTATION UPDATE) DE PORPHOBILINOGEN DEAMINASE (FRAGMENT). OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LYMPHOMA; RA KATO S.; RL SUBMITTED (MAR-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [2] RP SEQUENCE FROM N.A. RC TISSUE=LYMPHOMA; RX MEDLINE; 95121910. RA KATO S., SEKINE S., OH S., KIM N., UMEZAWA Y., ABE N., RA YOKOYAMA-KOBAYASHI M., AOKI T.; RL GENE 150:243-250(1994). DR EMBL; D28419; E150950; -. FT NON_TER 2 2 SQ SEQUENCE 2 AA; 236 MW; 0993DC06 CRC32; >E150950 MS TREMBL:G189644 ID G189644 PRELIMINARY; PRT; 11 AA. AC M18799_1; DT 24-SEP-1996 (EMBLREL. 48, CREATED) DT 24-SEP-1996 (EMBLREL. 48, LAST SEQUENCE UPDATE) DT 24-SEP-1996 (EMBLREL. 48, LAST ANNOTATION UPDATE) DE PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (HYDROXYMETHYLBILANE SYNTHASE) DE (PRE-UROPORPHYRINOGEN SYNTHASE) (FRAGMENT). GN PBGD. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RA ROMEO P.H.; RL SUBMITTED (OCT-1988) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [2] RP SEQUENCE FROM N.A. RX MEDLINE; 88124819. RA CHRETIEN S., DUBART A., BEAUPAIN D., RAICH N., GRANDCHAMP B., ROSA J., RA GOOSSENS M., ROMEO P.H.; RL PROC. NATL. ACAD. SCI. U.S.A. 85:6-10(1988). CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- COFACTOR: DIPYRROMETHANE. DR EMBL; M18799; G189644; -. KW LYASE. FT NON_TER 11 11 SQ SEQUENCE 11 AA; 964 MW; 01F2F94A CRC32; >G189644 MSGNGNAAATA TREMBL:Q60169 ID Q60169 PRELIMINARY; PRT; 314 AA. AC Q60169; 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 POROPHORBILINOGEN DEAMINASE (EC 4.3.1.8) DE (HYDROXYMETHYLBILANE SYNTHASE) (PORPHOBILINOGEN DEAMINASE) DE (PRE-UROPORPHYRINOGEN SYNTHASE). GN HEMC. OS PSEUDOMONAS AERUGINOSA. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC PSEUDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RA MOHR C.D., SONSTEBY S.K., DERETIC V.; RL MOL. GEN. GENET. 242:177-184(1991). CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- COFACTOR: DIPYRROMETHANE. DR EMBL; M74844; G496214; -. DR EMBL; M68873; G151255; -. KW LYASE. SQ SEQUENCE 314 AA; 33587 MW; BD8A2DFC CRC32; >Q60169 MSSREIRIATRQSALALWQAEYVNSTGLEQAHPGLTVTLLPMTSRGDKLLDAPLAKIGGK GLFVKELETALLEGAADIAVHSMKDVPMDFPEGLGLYTICEREDPRDAFVSNTYASLEQL PAGSVVGTSRLGRQAQLLARRPDLQIRFLRGNVNTRLAKLDAGEYDAIILAAAGVIRLGF ESRIRSSISVDDSLPAGGQGAVGIECRTADSDLHALLEPLHHTDTALRVTAERALNKRLN GGCQVPIACYAIREGDQLWLRGLVGQPDGTQLLRAEGRAPLADAEALGVRVAEDLLEQGA EAILEAVYGEAGHP TREMBL:Q59684 ID Q59684 PRELIMINARY; PRT; 313 AA. AC Q59684; 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 PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (HYDROXYMETHYLBILANE SYNTHASE) DE (PRE-UROPORPHYRINOGEN SYNTHASE). GN HEMC. OS PROTEUS MIRABILIS. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RA TROTOT P., SISMEIRO O., VIVAR S.C., GLASER P., DANCHIN A.; RL SUBMITTED (APR-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- COFACTOR: DIPYRROMETHANE. DR EMBL; U22969; G726359; -. KW LYASE. SQ SEQUENCE 313 AA; 33912 MW; 51223F50 CRC32; >Q59684 MPKSTIRIATRQSPLAMWQALYVKEQLQIAHPSLVVELVPMVTKGDIILDTPLAKVGGKG LFVKELELALLSSRADIAVHSMKDVPIDFPEGLGLVTICEREDPRDAFVSNHYDSLEQLP AGSVVGTSSLRRQCQLKALRPDLIIRDLRGNVGTRLSKLDNGDYDAIILAVAGLKRLKLT ERIRSSLSAEQSLPAVGQGAVGIECRLDDHDTQALLAALNHADTATCVKAERAMNTRLEG GCQVPIGSYAIWQNDKIWLRALVGAPDGKTILRGERLVSPEDAEQAGISLAEELLDKGAR EILTAVYQGNTAI TREMBL:Q59293 ID Q59293 PRELIMINARY; PRT; 295 AA. AC Q59293; 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 PORPHOBILINOGEN DEAMINASE (EC 4.3.1.8) (HYDROXYMETHYLBILANE SYNTHASE) DE (PRE-UROPORPHYRINOGEN SYNTHASE). GN HEMC. 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: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- COFACTOR: DIPYRROMETHANE. DR EMBL; D28503; G460692; -. KW LYASE. SQ SEQUENCE 295 AA; 32744 MW; E12FE822 CRC32; >Q59293 MVFDMKKIRIGSRDSKLAIIQSELIMSAIRKYDPDIELELITMKTTGDKILDKTLDKIEG KGLFVKELDNALYNNEVDITVHSYKDMPLEENPELPVVALSKREDPRDAFILPQNGENGE PIGSSSLRRQLQLKELFPGCKTAPIRGNVQTRLKKLDSGEFSAIVLAAAGIKRLGLESRI GRYFSVDEILPAASQGIIAVQGRVGENFDFLKLFHSEESLCISLAERTFVREMNGGCSTP IAAYATIQGSEIILKGLYCNETTGELRKECVSGNRNNPVELGYELVKKMKSSKSI TREMBL:Q57989 ID Q57989 PRELIMINARY; PRT; 292 AA. AC Q57989; 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 PORPHOBILINOGEN DEAMINASE. GN MJ0569. OS METHANOCOCCUS JANNASCHII. OC ARCHAEBACTERIA; EURYARCHAEOTA; METHANOCOCCALES; METHANOCOCCACEAE. RN [1] RP SEQUENCE FROM N.A. RA BULT C.J., WHITE O., OLSEN G.J., ZHOU L., FLEISCHMANN R.D., RA SUTTON G.G., BLAKE J.A., FITZGERALD L.M., CLAYTON R.A., RA GOCAYNE J.D., KERLAVAGE A.R., DOUGHERTY B.A., TOMB J.F., RA ADAMS M.D., REICH C.I., OVERBEEK R., KIRKNESS E.F., RA WEINSTOCK K.G., MERRICK J.M., GLODEK A., SCOTT J.L., RA GEOGHAGEN N.S.M., WEIDMAN J.F., FUHRMANN J.L., PRESLEY E.A., RA NGUYEN D., UTTERBACK T.R., KELLEY J.M., PETERSON J.D., SADOW P.W., RA HANNA M.C., COTTON M.D., HURST M.A., ROBERTS K.M., KAINE B.P., RA BORODOVSKY M., KLENK H.P., FRASER C.M., SMITH H.O., WOESE C.R., RA VENTER J.C.; RL SCIENCE 273:1058-1073(1996). DR EMBL; U67506; G1591276; -. SQ SEQUENCE 292 AA; 32783 MW; 9A12E9B4 CRC32; >Q57989 MIRIGTRGSKLALYQANKVAELLKNLGYKVEIKIIKTTGDRVLDKKLSDIGIGVFTKELD LAMLNNEIDIAVHSLKDIPTIWNENLMVGAVLERDSYHDLLIWNKDIDFNEDSKIVIGTS SMRRRAFLKFIYPNAKFELLRGNVDTRLRKLKEGLYDAIVLSEAGIIRLGVSLEDFNYKR LDILPAPAQGIIAVACKRDDEEMKSILKEINHERTYLESLCERTALNEFGGGCSVPFGAL AVYDEKNELLKLKAAVVTNDELKNASGEVKCKIDEIDKAVELGKKIGLKLKN TREMBL:Q43316 ID Q43316 PRELIMINARY; PRT; 382 AA. AC Q43316; 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 HYDROXYMETHYLBILANE SYNTHASE (EC 4.3.1.8) (PORPHOBILINOGEN DEAMINASE) DE (PRE-UROPORPHYRINOGEN SYNTHASE). GN HEMC. OS ARABIDOPSIS THALIANA (MOUSE-EAR CRESS). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; OC CAPPARALES; CRUCIFERAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ECOTYPE LANDSBERG ERECTA; RX MEDLINE; 95093027. RA LIM S.H., WITTY M., WALLACE-COOK A., ILAG L.I., SMITH A.G.; RL PLANT MOL. BIOL. 26:863-872(1994). CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- COFACTOR: DIPYRROMETHANE. DR EMBL; X73839; G313838; -. DR EMBL; X73535; G313150; -. KW LYASE; CHLOROPLAST. SQ SEQUENCE 382 AA; 41043 MW; D224E9CD CRC32; >Q43316 MDIASSSLSQAHKVVLTRQPSSRVNTCSLGSVSAIGFSLPQISSPALGKCRRKQSSSGFV KACVAVEQKTRTAIIRIGTRGSPLALAQAYETREKLKKKHPELVEDGAIHIEIIKTTGDK ILSQPLADIGGKGLFTKEIDEALINGHIDIAVHSMKDVPTYLPEKTILPCNLPREDVRDA FICLTAATLAELPAGSVVGTASLRRKSQILHKYPALHVEENFRGNVQTRLSKLQGGKVQA TLLALAGLKRLSMTENVASILSLDEMLPAVAQGAIGIACRTDDDKMATYLASLNHEETRL AISCERAFLETLDGSCRTPIAGYASKDEEGNCIFRGLVASPDGTKVLETSRKGPYVYEDM VKMGKDAGQELLSRAGPGFFGN TREMBL:Q43082 ID Q43082 PRELIMINARY; PRT; 369 AA. AC Q43082; 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 HYDROXYMETHYLBILANE SYNTHASE PRECURSOR (EC 4.3.1.8) DE (PORPHOBILINOGEN DEAMINASE) (PRE-UROPORPHYRINOGEN SYNTHASE). GN HEMC. OS PISUM SATIVUM (GARDEN PEA). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; FABALES; OC FABACEAE. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=LEAF; RX MEDLINE; 94269188. RA WITTY M., WALLACE-COOK A.D.M., ALBRECHT H., SPANO A.J., MICHEL H., RA SHABANOWITZ J., HUNT D.F., TIMKO M.P., SMITH A.G.; RL PLANT PHYSIOL. 103:139-147(1993). CC -!- CATALYTIC ACTIVITY: 4 PORPHOBILINOGEN + H(2)O = CC HYDROXYMETHYLBILANE + 4 NH(3). CC -!- COFACTOR: DIPYRROMETHANE. DR EMBL; X73418; G313724; -. KW TRANSIT PEPTIDE; LYASE. FT TRANSIT 1 46 POTENTIAL. FT CHAIN 47 369 HYDROXYMETHYLBILANE SYNTHASE. SQ SEQUENCE 369 AA; 39930 MW; C641D99E CRC32; >Q43082 MEMTLYSSSSFSLPSAPSNPSLSLFTSSFRFSSFKTSPFSKCRIRASLAVEQQTQQNKTA LIRIGTRGSPLALAQAHETRDKLMASHTELAEEGAIQIVIIKTTGDKILSQPLADIGGKG LFTKEIDEALINGDIDIAVHSMKDVPTYLPEETILPCNLPREDVRDAFISLSAASLADLP AGSVIGTASLRRKSQILHRYPSLTVQDNFRGNVQTRLRKLSEGVVKATLLALAGLKRLNM TENVTSTLSIDDMLPAVAQGAIGIACRSNDDKMAEYLASLNHEETRLAISCERAFLTTLD GSCRTPIAGYASRDKDGNCLFRGLVASPDGTRVLETSRIGSYTYEDMMKIGKDAGEELLS RAGPGFFNS TREMBLNEW:ECAE456_6 ID ECAE456_6 standard; PRT; 320 AA. AC AE000456; DR EMBL; AE000456; ECAE456. DE gene: "hemC"; product: "porphobilinogen deaminase"; DE Escherichia coli from bases 3980238 to 3991803 (section 346 of 400) DE of the complete genome. OS Escherichia coli OC Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OG Chloroplast FT CDS complement(6965..7927) FT /gene="hemC" FT /EC_number="4.3.1.8" FT /note="f320; 98 pct identical to 313 amino acids of FT HEM3_ECOLI SW: P06983 but has 7 additional N-ter residues" FT /codon_start=1 FT /product="porphobilinogen deaminase" FT /transl_table=11 FT /db_xref="PID:g1790237" FT /translation="MIMTVTSMLDNVLRIATRQSPLALWQAHYVKDKLMASHPGLVVEL FT VPMVTRGDVILDTPLAKVGGKGLFVKELEVALLENRADIAVHSMKDVPVEFPQGLGLVT FT ICEREDPRDAFVSNNYDSLDALPAGSIVGTSSLRRQCQLGERRPDLIIRSLRGNVGTRL FT SKLDNGEYDAIILAVAGLKRLGLESRIRAGLPPEISLPAVGQGAVGIECRLDDSRTREL FT LAALNHHETALRVTAERAMNTRLEGGCQVPIGSYAELIDGEIWLRALVGRPDGSQIIRG FT ERRGAPQDAEQMGISLAEELLNNGAREILAEVYNGDAPA" SQ Sequence 320 BP; >ECAE456_6 MIMTVTSMLDNVLRIATRQSPLALWQAHYVKDKLMASHPGLVVELVPMVTRGDVILDTPL AKVGGKGLFVKELEVALLENRADIAVHSMKDVPVEFPQGLGLVTICEREDPRDAFVSNNY DSLDALPAGSIVGTSSLRRQCQLGERRPDLIIRSLRGNVGTRLSKLDNGEYDAIILAVAG LKRLGLESRIRAGLPPEISLPAVGQGAVGIECRLDDSRTRELLAALNHHETALRVTAERA MNTRLEGGCQVPIGSYAELIDGEIWLRALVGRPDGSQIIRGERRGAPQDAEQMGISLAEE LLNNGAREILAEVYNGDAPA TREMBLNEW:SSD908_61 ID SSD908_61 standard; PRT; 320 AA. AC D90908; DR EMBL; D90908; SSD908. DE gene: "hemC"; product: "porphobilinogen deaminase"; DE Synechocystis sp. PCC6803 complete genome, 10/27, 1188886-1311234. OS Synechocystis sp. OC Eubacteria; Cyanobacteria; Chroococcales; Synechocystis. OG Mitochondrion FT CDS 58307..59269 FT /gene="hemC" FT /note="ORF_ID:slr1887" FT /codon_start=1 FT /product="porphobilinogen deaminase" FT /transl_table=11 FT /db_xref="PID:g1652786" FT /translation="MTVSTSAPTVRIGSRKSQLALVQTYWVQEELQKHFPDRQFDVETM FT ETQGDKILDVALAKIGDKGLFTQELEDGMLGKRTDLAVHSLKDLPTNLPAGLMLGCVTK FT RVNPADALVLNAKHQGKDLASLPEGAVIGTSSLRRLAQLRYHFPHLTFKDVRGNVNTRL FT AKLDSNEYDAIILAAAGLERLDMANRIDQLIPPEISLHAVGQGALGIECREGDQEILSL FT LKVLEDENSRDRCLAERAFLRQLEGGCQVPIGVNTHLDGDNLTLTGMVASLDGQRLIKD FT TLSAPRKEAEKLGQDLALKLREQGAGEILAEILAEAGRG" SQ Sequence 320 BP; >SSD908_61 MTVSTSAPTVRIGSRKSQLALVQTYWVQEELQKHFPDRQFDVETMETQGDKILDVALAKI GDKGLFTQELEDGMLGKRTDLAVHSLKDLPTNLPAGLMLGCVTKRVNPADALVLNAKHQG KDLASLPEGAVIGTSSLRRLAQLRYHFPHLTFKDVRGNVNTRLAKLDSNEYDAIILAAAG LERLDMANRIDQLIPPEISLHAVGQGALGIECREGDQEILSLLKVLEDENSRDRCLAERA FLRQLEGGCQVPIGVNTHLDGDNLTLTGMVASLDGQRLIKDTLSAPRKEAEKLGQDLALK LREQGAGEILAEILAEAGRG