ENZYME:1.3.3.3 ID 1.3.3.3 DE COPROPORPHYRINOGEN OXIDASE. AN COPROPORPHYRINOGENASE. AN COPROPORPHYRINOGEN-III OXIDASE. AN COPROGEN OXIDASE. CA COPROPORPHYRINOGEN-III + O(2) = PROTOPORPHYRINOGEN-IX + 2 CO(2). CF IRON. DI COPROPORPHYRIA; MIM:121300. PR PROSITE; PDOC00783; DR P36553, HEM6_ECOLI; P36551, HEM6_HUMAN; P36552, HEM6_MOUSE; DR P43898, HEM6_PSEAE; P33771, HEM6_SALTY; P35055, HEM6_SOYBN; DR P11353, HEM6_YEAST; PIR:A54939 >F1;A54939 coproporphyrinogen oxidase (EC 1.3.3.3) - mouse (fragments) C;Species: Mus musculus (house mouse) C;Date: 16-Feb-1996 #sequence_revision 16-Feb-1996 #text_change 16-Feb-1996 C;Accession: A54939 R;Martasek, P.; Camadro, J.M.; Delfau-Larue, M.H.; Dumas, J.B.; Montagne, J.J.; de Verneuil, H.; Labbe, P.; Grandchamp, B. Proc. Natl. Acad. Sci. U.S.A. 91, 3024-3028, 1994 A;Title: Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase. A;Reference number: A54939; MUID:94211794 A;Accession: A54939 A;Status: preliminary A;Molecule type: protein A;Residues: 1-43 C;Keywords: heme biosynthesis; mitochondrion; oxidoreductase >A54939 XPXPGRREEDGDELARRSDTFMSXTFMSTPPTFNYRYFEVEEA PIR:I37259 >F1;I37259 coproporphyrinogen oxidase (EC 1.3.3.3) precursor - human (fragment) C;Species: Homo sapiens (man) C;Date: 16-Feb-1996 #sequence_revision 16-Feb-1996 #text_change 06-Sep-1996 C;Accession: I37259; S39243 R;Martasek, P.; Camadro, J.M.; Delfau-Larue, M.H.; Dumas, J.B.; Montagne, J.J.; de Verneuil, H.; Labbe, P.; Grandchamp, B. Proc. Natl. Acad. Sci. U.S.A. 91, 3024-3028, 1994 A;Title: Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase. A;Reference number: A54939; MUID:94211794 A;Accession: I37259 A;Status: preliminary A;Molecule type: mRNA A;Residues: 1-354 A;Cross-references: EMBL:Z28409; NID:g433887; CDS_PID:g433888 C;Genetics: A;Gene: GDB:CPO A;Cross-references: GDB:119070 A;Map position: 9pter-9qter C;Keywords: heme biosynthesis; mitochondrion; oxidoreductase >I37259 MLPKTSGTRATSLGRPEEEEDELAHRCSSFMAPPVTDLGELRRRPGDMKTKMELLILETQ AQVCQALAQVDGGANFSVDRWERKEGGGGISCVLQDGCVFEKAGVSISVVHGNLSEEAAK QMRSRGKVLKTKDGKLPFCAMGVSSVTHPKNPHAPTIHFNYRYFEVEEADGHKQWWFGGG CDLTPTYLNQEDAVHFHRTLKEACDQHGPDLYPKFKKWCDDYFFIAHRGERRGIGGIFFD DLDSPSKEEVFRFVQSCARAVVPSYIPLVKKHCDDSFTPQEKLWQQLRRGRYVEFNLLYD RGTKFGLFTPGSRIESILMSLPLTARWEYMHSPSENSKEAEILEVLRHPRDWVR PIR:I52444 >P1;I52444 coproporphyrinogen oxidase (EC 1.3.3.3) - human C;Species: Homo sapiens (man) C;Date: 02-Jul-1996 #sequence_revision 02-Jul-1996 #text_change 02-Jul-1996 C;Accession: I52444 R;Taketani, S.; Kohno, H.; Furukawa, T.; Yoshinaga, T.; Tokunaga, R. Biochim. Biophys. Acta 1183, 547-549, 1994 A;Title: Molecular cloning, sequencing and expression of cDNA encoding human coproporphyrinogen oxidase. A;Reference number: I52444; MUID:94114558 A;Accession: I52444 A;Status: preliminary; translated from GB/EMBL/DDBJ A;Molecule type: mRNA A;Residues: 1-354 A;Cross-references: GB:D16611; NID:g469488; CDS_PID:g840693 C;Keywords: oxidoreductase >I52444 MLPKTSGTRATSLGRPEEEEDELAHRCSSFMAPPVTDLGELRRRPGDMKTKMELLILETQ AQVCQALAQVDGGANFSVDRWERKEGGGGISCVLQDGCVFEKAGVSISVVHGNLSEEAAK QMRSRGKVLKTKDGKLPFCAMGVSSVIHPKNPHAPTIHFNYRYFEVEEADGNKQWWFGGG CDLTPTYLNQEDAVHFHRTLKEACDQHGPDLYPKFKKWCDDYFFIAHRGERRGIGGIFFD DLDSPSKEEVFRFVQSCARAVVPSYIPLVKKHCDDSFTPQEKLWQQLRRGRYVEFNLLYD RGTKFGLFTPGSRIESILMSLPLTARWEYMHSPSENSKEAEILEVLRHPRDWVR PIR:D47045 >P1;D47045 coproporphyrinogen III oxidase, protoporphyrinogen IX oxidase - Bacillus subtilis C;Species: Bacillus subtilis C;Date: 21-Sep-1993 #sequence_revision 18-Nov-1994 #text_change 18-Nov-1994 C;Accession: D47045 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: D47045 A;Status: preliminary A;Molecule type: nucleic acid A;Residues: 1-470 A;Cross-references: NCBIN:119989; NCBIP:119993 A;Note: sequence extracted from NCBI backbone >D47045 MSDGKKHVVIIGGGITGLAAAFYMEKEIKEKNLPLELTLVEASPRVGGKIQTVKKDGYII ERGPDSFLERKKSAPQLVKDLGLEHLLVNNATGQSYVLVNRTLHPMPKGAVMGIPTKIAP FVSTGLFSLSGKARAAMDFILPASKTKDDQSLGEFFRRRVGDEVVENLIEPLLSGIYAGD IDKLSLMSTFPQFYQTEQKHRSLILGMKKTRPQGSGQQLTAKKQGQFQTLSTGLQTLVEE IEKQLKLTKVYKGTKVTKLSHSGSCYSLELDNGVTLDADSVIVTAPHKAAAGMLSELPAI SHLKNMHSTSVANVALGFPEGSVQMEHEGTGFVISRNSDFAITACTWTNKKWPHAAPEGK TLLRAYVGKAGDESIVDLSDNDIINIVLEDLKKVMNINGEPEMTCVTRWHESMPQYHVGH KQRIKELREALASAYPGVYMTGASFEGVGIPDCIDQGKAAVSDALTYLFS PIR:S28025 >P1;S28025 pucC protein - Rhodobacter sphaeroides C;Species: Rhodobacter sphaeroides C;Date: 17-Apr-1993 #sequence_revision 17-Apr-1993 #text_change 17-Apr-1993 C;Accession: S28025 R;Gibson, L.C.D.; McGlynn, P.; Chaudhri, M.; Hunter, C.N. Mol. Microbiol. 6, 3171-3186, 1992 A;Title: A putative anaerobic coproporphyrinogen III oxidase in Rhodobacter sphaeroides. II. Analysis of a region of the genome encoding hemF and the puc operon. A;Reference number: S28023 A;Accession: S28025 A;Molecule type: DNA A;Residues: 1-459 A;Cross-references: EMBL:X68796 >S28025 MSRIAEHLVRIGPRFLPFADAASDQLPLRKLLRLSLFQVAVGMAIVLLVGTLNRVMIVEL KVPASVVGIMISLPLLFAPFRALIGFKSDTHVSALGWRRVPWIYRGTLALWGGFAIMPFA LIVLGGQGYAEGQPFWLGVSSAALAFLMVGGGVHTIQTVGLALATDLAPREDQPKVVGLM YVVLLISMIFASIGFGWLLDPYYDAQLIKVISGVAVAVFFLNMIALWKMEPRNRAFTVKP EKEPEFGDHWREFISRENALHGLIVIGLGTLGFGMADVILEPYGGEVLSMTVAETTRLTA TFAGGGLVGFWLASWVLGRGFDPLRMAFLGAAAGLPGFFAIMGATEMTNVWVFLLGTLVV GFGGGLFSHGTLTATMRLAPKEQVGLALGAWGAVQATAAGVAIAGAGVLRDILQAMPDLS GYGPGAPYVAVFALEAGFLFLTMIVILPLLRSALAARRL PIR:S28440 >P1;S28440 probable coproporphyrinogen III oxidase, anaerobic - Rhodobacter sphaeroides C;Species: Rhodobacter sphaeroides C;Date: 07-May-1993 #sequence_revision 07-May-1993 #text_change 30-Sep-1993 C;Accession: S28440 R;Coomber, S.A.; Jones, R.M.; Jordan, P.M.; Hunter, C.N. Mol. Microbiol. 6, 3159-3169, 1992 A;Title: A putative anaerobic coproporphyrinogen III oxidase in Rhodobacter sphaeroides. I. Molecular cloning, transposon mutagenesis and sequence analysis of the gene. A;Reference number: S28440 A;Accession: S28440 A;Status: not compared with conceptual translation A;Molecule type: DNA A;Residues: 1-305 C;Genetics: A;Gene: hemF >S28440 MMVDEPKIRALSEEGMNRASIGIQDFTDIVQNAIGREQPFENTKACVQSVRRYGVHSLNT DLVYGLPHQNRESLAATIDKVLSLRPDRVAIFGYAHVPWMAKRQKLIDETVLPPDIERHE LANLAARLFTEGGFERIGIDHFALPDDSMAVAARSRKLRRNFQGYTDDTCPTLLGIGASS ISKFEQGYLQNTAATAAYIKSIEEGRLPGYRGHRMTEEDYLHGRAIEMIMCDFFLELPAL RARFGEPAETMVLAHRRSGREVTPFVTVDADGSMSIAKEGRALARMIARLFDAYETPEAR YSQAS PIR:B64070 >P1;B64070 oxygen-independent coproporphyrinogen III oxidase (hemN) homolog - Haemophilus influenzae (strain Rd KW20) C;Species: Haemophilus influenzae C;Date: 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 18-Aug-1995 C;Accession: B64070 R;Fleischmann, R.D.; Adams, M.D.; White, O.; Clayton, R.A.; Kirkness, E.F.; Kerlavage, A.R.; Bult, C.J.; Tomb, J.F.; Dougherty, B.A.; Merrick, J.M.; McKenney, K.; Sutton, G.; FitzHugh, W.; Fields, C.; Gocayne, J.D.; Scott, J.; Shirley, R.; Liu, L.I.; Glodek, A.; Kelley, J.M.; Weidman, J.F.; Phillips, C.A.; Spriggs, T.; Hedblom, E. Science 269, 496-512, 1995 A;Authors: Cotton, M.D.; Utterback, T.R.; Hanna, M.C.; Nguyen, D.T.; Saudek, D.M.; Brandon, R.C.; Fine, L.D.; Fritchman, J.L.; Fuhrmann, J.L.; Geoghagen, N.S.M.; Gnehm, C.L.; McDonald, L.A.; Small, K.V.; Fraser, C.M.; Smith, H.O.; Venter, J.C. A;Title: Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. A;Reference number: A64000 A;Accession: B64070 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-383 A;Cross-references: GB:L42023; TIGR:HI0463 A;Note: named as homolog to a protein from Salmonella typhimurium >B64070 MPKLPPLSLYIHIPWCVQKCPYCDFNSHAQKSDIPEQDYIYHLLQDLQADLQRFKDSIQQ RKLHSIFIGGGTPSLFSAESIAYLLKEIKKQIDFEDNIEITLEANPGTVEAERFKGYVSA GIMRISMGIQSFNDDKLQRLGRIHNAAEAKSAVNLAKVSGLKSFNLDLMHGLPNQTLEEA LDDLRQAIELSPPHISWYQLTIEPNTMFAYRPPKLPDDDALWDIFEQGHQLLTMAGYQQY ETSAYAKAGFQCKHNLNYWRFGDYLAIGCGAHGKLTFPTGEITRFSKTKHPKGYLRGEYL YEEKNVPKIDRPFEFFMNRFRLLEAVPKQEFEDYTGLSQSAVKNQIDFAIQQNYIVENAD SWQITEHGKLFLNELLELFLTEE PIR:A53302 >P1;A53302 hemF 5'-region hypothetical protein - Salmonella typhimurium C;Species: Salmonella typhimurium C;Date: 08-Sep-1995 #sequence_revision 08-Sep-1995 #text_change 08-Sep-1995 C;Accession: A53302 R;Xu, K.; Elliott, T. J. Bacteriol. 175, 4990-4999, 1993 A;Title: An oxygen-dependent coproporphyrinogen oxidase encoded by the hemF gene of Salmonella typhimurium. A;Reference number: A53302 A;Accession: A53302 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-289 A;Cross-references: GB:L19503 >A53302 MSTFKLLKTLTSRRQVLKTGLAALTLSGMSHAVAKEETLKTSNGHSKPKTKKTGSKRLVM LDPGHGGIDTGAIGRNGSQEKHVVLAIAKNVRAILRNHGIDARLTRTGDTFIPLYDRVEI AHKHGADLFMSIHADGFTNPKAAGASVFALSNRGASSAMAKYLSERENRADEVAGKKATD RDHLLQQVLFDLVQTDTIKNSLTLGSHILKKIKPIHKLHSRTTEQAAFVVLKSPSIPSVL VETSFITNPEEERLLGTTAFRQKIATAIANGIISYFHWFDNQKAHTKKR PIR:C53302 >P1;C53302 hemF 3'-region hypothetical protein - Salmonella typhimurium C;Species: Salmonella typhimurium C;Date: 08-Sep-1995 #sequence_revision 08-Sep-1995 #text_change 08-Sep-1995 C;Accession: C53302 R;Xu, K.; Elliott, T. J. Bacteriol. 175, 4990-4999, 1993 A;Title: An oxygen-dependent coproporphyrinogen oxidase encoded by the hemF gene of Salmonella typhimurium. A;Reference number: A53302 A;Accession: C53302 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-109 A;Cross-references: GB:L19503 >C53302 MQTNTRKVVTSDAKWHPHLGISFIGCLLAITLEIYFEERIFIPHSGGVSFGLIVLLVINM VTIPVVMALIALLCFIIHIPRKSVNCILLCLLSCILTIAGLFIAYPVGR PIR:A36964 >P1;A36964 N-acetylmuramoyl-L-alanine amidase homolog - Escherichia coli C;Species: Escherichia coli C;Date: 13-Sep-1995 #sequence_revision 13-Sep-1995 #text_change 13-Sep-1995 C;Accession: A36964 R;Troup, B.; Jahn, M.; Hungerer, C.; Jahn, D. J. Bacteriol. 176, 673-680, 1994 A;Title: Isolation of the hemF operon containing the gene for the Escherichia coli aerobic coproporphyrinogen III oxidase by in vivo complementation of a yeast HEM13 mutant. A;Reference number: A36964 A;Accession: A36964 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-289 A;Cross-references: GB:X75413 >A36964 MSTFKPLKTLTSRRQVLKAGLAALTLSGMSQAIAKDELLKTSNGHSKPKAKKSGGKRVVV LDPGHGGIDTGAIGRNGSKEKHVVLAIAKNVRSILRNHGIDARLTRSGDTFIPLYDRVEI AHKHGADLFMSIHADGFTNPKAAGASVFALSNRGASSAMAKYLSERENRADEVAGKKATD KDHLLQQVLFDLVQTDTIKNSLTLGSHILKKIKPVHKLHSRNTEQAAFVVLKSPSVPSVL VETSFITNPEEERLLGTAAFRQKIATAIAEGVISYFHWFDNQKAHSKKR PIR:C36964 >P1;C36964 hemF 3'-region hypothetical protein - Escherichia coli C;Species: Escherichia coli C;Date: 13-Sep-1995 #sequence_revision 13-Sep-1995 #text_change 13-Sep-1995 C;Accession: C36964 R;Troup, B.; Jahn, M.; Hungerer, C.; Jahn, D. J. Bacteriol. 176, 673-680, 1994 A;Title: Isolation of the hemF operon containing the gene for the Escherichia coli aerobic coproporphyrinogen III oxidase by in vivo complementation of a yeast HEM13 mutant. A;Reference number: A36964 A;Accession: C36964 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-350 A;Cross-references: GB:X75413 A;Note: authors translated the codon CGG for residue 285 as Pro >C36964 MKKTRTANLHHLYHEPLPENLKLTPKVEVDNVHQRQTTDVYEHALTITAWQQIYDQLHPG KFHGEFTEILLDDIQVFREYTGLALRQSCLVWPNSFWFGIPATRGEQGFIGSQCLGSAEI ATRPGGTEFELSTPDDYTILGVVLSEDVITRQANFLHNPDRVLHMLRNQSALEVKEQHKA ALWGFVQQALATFCENPENLHQPAVRKVLGDNLLMAMGAMLEEAQPMVTAESISHQSYRR LLSRAREYVLENMSEPVTVLDLCNQLHVSRRTLQNRFHAILGIGRNAWLKRIRLNAVRRE LISPWSQSMTVKDAAMQWGFWHLGQFATDYQQLFSEKPSLTLHQRMREWG PIR:A57252 >P1;A57252 coproporphyrinogen oxidase (EC 1.3.3.3) III, oxygen-independent - Escherichia coli C;Species: Escherichia coli C;Date: 19-Jan-1996 #sequence_revision 19-Jan-1996 #text_change 09-Mar-1996 C;Accession: A57252; S49373 R;Troup, B.; Hungerer, C.; Jahn, D. J. Bacteriol. 177, 3326-3331, 1995 A;Title: Cloning and characterization of the Escherichia coli hemN gene encoding the oxygen-independent coproporphyrinogen III oxidase. A;Reference number: A57252 A;Accession: A57252 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-457 A;Cross-references: EMBL:X82073 C;Genetics: A;Gene: hemN C;Keywords: oxidoreductase >A57252 MSVQQIDWDLALIQKYNYSGPRYTSYPTALEFSEDFGEQAFLQAVARYPERPLSLYVHIP FCHKLCYFCGCNKIVTRQQHKADQYLDALEQEIVHRAPLFAGRHVSQLHWGGGTPTYLNK AQISRLMKLLRENFQFNADAEISIEVDPREIELDVLDHLRAEGFNRLSMGVQDFNKEVQR LVNREQDEEFIFALLNHAREIGFTSTNIDLIYGLPKQTPESFAFTLKRVAEVNPDRLSVF NYAHLPTIFAAQRKIKDADLPSPQQKLDILQETIAFLTQSGYQFIGMDHFARPDDELAVA QREGVLHRNFQGYTTQGDTDLLGMGVSAISMIGDCYAQNQKELKQYYQQVDEQGNALWRG IALTRDDCIRRDVIKSLICNFRLDYAPIEKQWDLHFADYFAEDLKLLAPLAKDGLVDVDE KGIQVTAKGRLLIRNICMCFDTYLRQKARMQQFSRVI PIR:A27087 >P1;A27087 light-harvesting protein B-800/850 alpha chain - Rhodobacter sphaeroides C;Species: Rhodobacter sphaeroides C;Date: 19-Nov-1988 #sequence_revision 19-Nov-1988 #text_change 12-Apr-1996 C;Accession: A27087; B26645; B45795; S28024 R;Kiley, P.J.; Kaplan, S. J. Bacteriol. 169, 3268-3275, 1987 A;Title: Cloning, DNA sequence, and expression of the Rhodobacter sphaeroides light-harvesting B800-850-alpha and B800-850-beta genes. A;Reference number: A91838; MUID:87250299 A;Accession: A27087 A;Molecule type: DNA A;Residues: 1-54 R;Ashby, M.K.; Coomber, S.A.; Hunter, C.N. FEBS Lett. 213, 245-248, 1987 A;Title: Cloning, nucleotide sequence and transfer of genes for the B800-850 light harvesting complex of Rhodobacter sphaeroides. A;Reference number: A26645 A;Accession: B26645 A;Status: preliminary; not compared with conceptual translation A;Molecule type: DNA A;Residues: 1-54 R;Burgess, J.G.; Ashby, M.K.; Hunter, C.N. J. Gen. Microbiol. 135, 1809-1816, 1989 A;Title: Characterization and complementation of a mutant of Rhodobacter sphaeroides with a chromosomal deletion in the light-harvesting (LH2) genes. A;Reference number: A45795 A;Accession: B45795 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-54 A;Cross-references: GB:M28360 R;Gibson, L.C.D.; McGlynn, P.; Chaudhri, M.; Hunter, C.N. Mol. Microbiol. 6, 3171-3186, 1992 A;Title: A putative anaerobic coproporphyrinogen III oxidase in Rhodobacter sphaeroides. II. Analysis of a region of the genome encoding hemF and the puc operon. A;Reference number: S28023 A;Accession: S28024 A;Status: preliminary A;Molecule type: DNA A;Residues: 47-54 A;Cross-references: EMBL:X68796 C;Genetics: A;Gene: pucA C;Superfamily: light-harvesting protein alpha chain >A27087 MTNGKIWLVVKPTVGVPLFLSAAVIASVVIHAAVLTTTTWLPAYYQGSAAVAAE PIR:S39905 >P1;S39905 coproporphyrinogen oxidase - soybean C;Species: Glycine max (soybean) C;Date: 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 03-May-1996 C;Accession: S39905 R;Sandal, N.N. submitted to the EMBL Data Library, March 1993 A;Reference number: S39905 A;Accession: S39905 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-385 A;Cross-references: EMBL:X71083 C;Genetics: A;Introns: 174/3; 200/1; 231/3; 259/3; 289/1; 330/3; 363/3 C;Superfamily: coproporphyrinogen oxidase >S39905 MMHCASIVSAPSYAFPFRSGSASTTPTAISLTKRSWKPPPSMAKGPVRATVSIEKETPEA NRPETFLRGVDEAQSSTSVRARFEKMIREAQDTVCSALEAADGGAQFKEDVWSRPGGGGG ISRVLQDGAVWEKAGVNVSVVYGVMPPDAYRAAKGVPTDQKPGPVPFFAAGISSVLHPKN PFAPTLHFNYRYFETDAPKDAPGAPRQWWFGGGTDLTPAYIFEEDVKHFHSIQKQACDKF EPTFYPRFKKWCDDYFYIKHRGERRGLGGIFFDDLNDYDQEMLLSFATECANSVIPAYLP IIEKRKDLPFNDHQKAWQQLRRGRYVEFNLVYDRGTTFGLKTGGRIESILVSLPLTARWE YDHKPEEGSEEWKLLDACINPKEWI PIR:A48049 >P1;A48049 coproporphyrinogen oxidase (EC 1.3.3.3) - mouse C;Species: Mus musculus (house mouse) C;Date: 07-Apr-1994 #sequence_revision 18-Nov-1994 #text_change 03-May-1996 C;Accession: A48049 R;Kohno, H.; Furukawa, T.; Yoshinaga, T.; Tokunaga, R.; Taketani, S. J. Biol. Chem. 268, 21359-21363, 1993 A;Title: Coproporphyrinogen oxidase. Purification, molecular cloning, and induction of mRNA during erythroid differentiation. A;Reference number: A48049; MUID:94012692 A;Accession: A48049 A;Status: preliminary A;Molecule type: mRNA; protein A;Residues: 1-354 A;Cross-references: NCBIN:138527; NCBIP:138528 A;Experimental source: MEL, erythroleukemia cells A;Note: sequence extracted from NCBI backbone C;Superfamily: coproporphyrinogen oxidase C;Keywords: oxidoreductase >A48049 MVPKSSGARSPSPGRREEDGDELARRCSTFMSSPVTELRELRRRPEDMKTKMELMIMETQ AQVCRALAQVDGVADFTVDRWERKEGGGGITCVLQDGRVFEKAGVSISVVHGNLSEEAAN QMRGRGKTLKTKDSKLPFTAMGVSSVIHPKNPYAPTMHFNYRYFEVEEADGNTHWWFGGG CDLTPRYLNQEDAVHFHRTLKEACDQHGPDIYPKFKKWCDDYFFIVHRGERRGIGGIFFD DLDSPSKEEAFRFVKTCAEAVVPSYVPIVKKHCDDSYTPRDKLWQQLRRGRYVEFNLLYD RGTKFGLFTPGSRIESILMSLPLTARWEYMHSPPENSKEAEILEVLRHPKDWVH PIR:S52924 >P1;S52924 coproporphyrinogen oxidase (EC 1.3.3.3) oxygen-dependent - Pseudomonas aeruginosa C;Species: Pseudomonas aeruginosa C;Date: 06-Jun-1995 #sequence_revision 21-Jul-1995 #text_change 03-May-1996 C;Accession: S52924 R;Hungerer, C.; Troup, B.; Jahn, D. submitted to the EMBL Data Library, February 1995 A;Description: Cloning and regulation of the Pseudomonas aeruginosa hemF gene encoding oxygen-dependent coproporphyrinogen III oxidase. A;Reference number: S52923 A;Accession: S52924 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-305 A;Cross-references: EMBL:X85015 C;Genetics: A;Start codon: GTG C;Superfamily: coproporphyrinogen oxidase C;Keywords: oxidoreductase >S52924 MTDRIAAVKTYLLDLQDRICAALEAEDGKARFAEDAWERPAGGGGRTRVIGDGALIEKGG VNFSHVFGDSLPPSASAHRPELAGRGFQALGVSLVIHPENPHVPTSHANVRFFCAEKEGE EPVWWFGGGFDLTPYYAHEEDCVHWHRVARDACAPFGADVYPRYKEWCDRYFHLKHRNEP RGIGGLFFDDLNQWDFDTCFAFIRAIGDAYIDAYLPIVQRRKHTPFDERQREFQAYRRGR YVEFNLVFDRGTLFGLQSGGRTESILMSLPPQVRWGYDWKPEPGSEEARLTEYFLADRDW LAGQP PIR:B36964 >P1;B36964 coproporphyrinogen oxidase (EC 1.3.3.3), aerobic - Escherichia coli C;Species: Escherichia coli C;Date: 13-Sep-1995 #sequence_revision 13-Sep-1995 #text_change 03-May-1996 C;Accession: B36964 R;Troup, B.; Jahn, M.; Hungerer, C.; Jahn, D. J. Bacteriol. 176, 673-680, 1994 A;Title: Isolation of the hemF operon containing the gene for the Escherichia coli aerobic coproporphyrinogen III oxidase by in vivo complementation of a yeast HEM13 mutant. A;Reference number: A36964 A;Accession: B36964 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-299 A;Cross-references: GB:X75413 C;Genetics: A;Gene: hemF C;Superfamily: coproporphyrinogen oxidase C;Keywords: oxidoreductase >B36964 MKPDAHQVKQFLLNLQDTICQQLTAVDGAEFVEDSWQREAGGGGRSRVLRNGGVFEQAGV NFSHVHGEAMPASATAHRPELAGRSFEAMGVSLVVHPHNPYVPTSHANVRFFIAEKPGAD PVWWFGGGFDLTPFYGFEEDAIHWHRTARDLCLPFGEDVYPRYKKWCDEYFYLKHRNEQR GIGGLFFDDLNTPDFDRCFAFMQAVGKGYTDAYLPIVERRKAMAYGERERNFQLYRRGRY VEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYQPKDGSPEAALSEFIKVRDWV PIR:B53302 >P1;B53302 coproporphyrinogen oxidase (EC 1.3.3.3) - Salmonella typhimurium C;Species: Salmonella typhimurium C;Date: 08-Sep-1995 #sequence_revision 08-Sep-1995 #text_change 03-May-1996 C;Accession: B53302 R;Xu, K.; Elliott, T. J. Bacteriol. 175, 4990-4999, 1993 A;Title: An oxygen-dependent coproporphyrinogen oxidase encoded by the hemF gene of Salmonella typhimurium. A;Reference number: A53302 A;Accession: B53302 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-299 A;Cross-references: GB:L19503 C;Superfamily: coproporphyrinogen oxidase C;Keywords: oxidoreductase >B53302 MKPDAHHVKQFLLRLQDDICQTLSAVDGANFVEDSWRREAGGGGRSRVLRNGGIFEQAGV NFSHVHGDAMPASATAHRPELAGRSFEAMGVSLVVHPHNPYIPTSHANVRFFIAEKPGAD PVWWFGGGFDLTPYYGFEEDAVHWHRTARDLCQPFGDDVYPRYKKWCDDYFFLKHRNEQR GVGGLFFDDLNTPDFDHCFDFMQAVGNGYTRAYLPIVERRKAMVWGERERNFQLYRRGRY VEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDWQPEAGSPEAALSEFIQVRDWI PIR:S39523 >P1;S39523 coproporphyrinogen oxidase - soybean C;Species: Glycine max (soybean) C;Date: 13-Jan-1995 #sequence_revision 13-Jan-1995 #text_change 03-May-1996 C;Accession: S39523 R;Madsen, O.; Sandal, L.; Sandal, N.N.; Marcker, K.A. Plant Mol. Biol. 23, 35-43, 1993 A;Title: A soybean coproporphyrinogen oxidase gene is highly expressed in root nodules. A;Reference number: S39523 A;Accession: S39523 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-385 A;Cross-references: EMBL:X71083 C;Genetics: A;Introns: 174/3; 200/1; 231/3; 259/3; 289/1; 330/3; 363/3 C;Superfamily: coproporphyrinogen oxidase >S39523 MMHCASIVSAPSYAFPFRSGSASTTPTAISLTKRSWKPPPSMAKGPLRATVSIEKETPEA NRPETFLRGVDEAQSSTSVRARFEKMIREAQDTVCSALEAADGGAQFKEDVWSRPGGGGG ISRVLQDGAVWEKAGVNVSVVYGVMPPDAYRAAKGVPTDQKPGPVPFFAAGISSVLHPKN PFAPTLHFNYRYFETDAPKDAPGAPRQWWFGGGTDLTPAYIFEEDVKHFHSIQKQACDKF EPTFYPRFKKWCDDYFYIKHRGERRGLGGIFFDDLNDYDQEMLLSFATECANSVIPAYLP IIEKRKDLPFNDHQKAWQQLRRGRYVEFNLVYDRGTTFGLKTGGRIESILVSLPLTARWE YDHKPEEGSEEWKLLDACINPKEWI PIR:LBRFBS >P1;LBRFBS light-harvesting protein B-800/850 beta chain - Rhodobacter sphaeroides N;Alternate names: antenna pigment protein, beta chain; B-800/850 beta; LH-3B C;Species: Rhodobacter sphaeroides C;Date: 27-Nov-1985 #sequence_revision 12-Apr-1996 #text_change 26-Apr-1996 C;Accession: B27087; S28023; A45795; A03454 R;Kiley, P.J.; Kaplan, S. J. Bacteriol. 169, 3268-3275, 1987 A;Title: Cloning, DNA sequence, and expression of the Rhodobacter sphaeroides light-harvesting B800-850-alpha and B800-850-beta genes. A;Reference number: A91838; MUID:87250299 A;Accession: B27087 A;Molecule type: DNA A;Residues: 1-51 R;Gibson, L.C.D.; McGlynn, P.; Chaudhri, M.; Hunter, C.N. Mol. Microbiol. 6, 3171-3186, 1992 A;Title: A putative anaerobic coproporphyrinogen III oxidase in Rhodobacter sphaeroides. II. Analysis of a region of the genome encoding hemF and the puc operon. A;Reference number: S28023 A;Accession: S28023 A;Status: preliminary; nucleic acid sequence not shown; translation not shown A;Molecule type: DNA A;Residues: 1-51 A;Cross-references: EMBL:X68796 A;Note: the nucleotide sequence was submitted to the EMBL Data Library, August 1992 R;Burgess, J.G.; Ashby, M.K.; Hunter, C.N. J. Gen. Microbiol. 135, 1809-1816, 1989 A;Title: Characterization and complementation of a mutant of Rhodobacter sphaeroides with a chromosomal deletion in the light-harvesting (LH2) genes. A;Reference number: A45795 A;Accession: A45795 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-51 A;Cross-references: GB:M28360 R;Theiler, R.; Suter, F.; Wiemken, V.; Zuber, H. Hoppe-Seyler's Z. Physiol. Chem. 365, 703-719, 1984 A;Title: The light-harvesting polypeptides of Rhodopseudomonas sphaeroides R-26.1: I. Isolation, purification and sequence analyses. A;Reference number: A91736; MUID:85005243 A;Contents: mutant R-26.1 A;Accession: A03454 A;Molecule type: protein A;Residues: 2-51 C;Genetics: A;Gene: pucB A;Start codon: GTG C;Function: A;Description: this polypeptide (LH-3B) and LH-2 constitute the B-800/850 complex of R. sphaeroides 2.4.1 and the spectrally altered B-850 complex isolated from the blue-green mutant R-26.1, which absorbs at 860 nm A;Note: His-22, which is conserved only in the beta chain, is located close to an "acid cluster" at the beginning of the hydrophobic segment; its function is not yet clear C;Superfamily: light-harvesting protein beta chain C;Keywords: antenna complex; bacteriochlorophyll; light-harvesting polypeptide; magnesium; membrane protein F;2-51/Product: light-harvesting protein B-800/850 beta chain #status experimental F;2/Modified site: blocked amino end (Thr) (in mature form) #status experimental F;40/Binding site: bacteriochlorophyll magnesium (His) (axial ligand) #status predicted >LBRFBS MTDDLNKVWPSGLTVAEAEEVHKQLILGTRVFGGMALIAHFLAAAATPWLG PIR:DEBYCH >P1;DEBYCH coproporphyrinogen oxidase (EC 1.3.3.3) - yeast (Saccharomyces cerevisiae) N;Alternate names: coproporphyrinogenase; protein YD5112.02; protein YDR044w C;Species: Saccharomyces cerevisiae C;Date: 31-Mar-1989 #sequence_revision 12-Apr-1996 #text_change 13-Sep-1996 C;Accession: S55079; A28090 R;Oliver, K.; Harris, D. submitted to the EMBL Data Library, June 1995 A;Reference number: S55078 A;Accession: S55079 A;Molecule type: DNA A;Residues: 1-328 A;Cross-references: EMBL:Z49812 A;Experimental source: strain AB972 R;Zagorec, M.; Buhler, J.M.; Treich, I.; Keng, T.; Guarente, L.; Labbe-Bois, R. J. Biol. Chem. 263, 9718-9724, 1988 A;Title: Isolation, sequence, and regulation by oxygen of the yeast HEM13 gene coding for coproporphyrinogen oxidase. A;Reference number: A28090; MUID:88257098 A;Accession: A28090 A;Molecule type: DNA A;Residues: 1-225,'N',227-328 A;Cross-references: EMBL:J03873 C;Comment: This enzyme catalyzes the oxygen-requiring oxidative decarboxylation of the two carboxyethyl side chains of coproporphyrinogen III to two vinyl groups of the protoporphyrinogen IX. In S. cerevisiae, the active enzyme, found in the cytosol, is a dimer of identical chains containing two iron atoms per molecule of native protein. C;Genetics: A;Gene: LISTA:HEM13 A;Map position: 4R C;Complex: homodimer C;Superfamily: coproporphyrinogen oxidase C;Keywords: homodimer; iron; metalloprotein; oxidative decarboxylation; oxidoreductase >DEBYCH MPAPQDPRNLPIRQQMEALIRRKQAEITQGLESIDTVKFHADTWTRGNDGGGGTSMVIQD GTTFEKGGVNVSVVYGQLSPAAVSAMKADHKNLRLPEDPKTGLPVTDGVKFFACGLSMVI HPVNPHAPTTHLNYRYFETWNQDGTPQTWWFGGGADLTPSYLYEEDGQLFHQLHKDALDK HDTALYPRFKKWCDEYFYITHRKETRGIGGIFFDDYDERDPQEILKMVEDCFDAFLPSYL TIVKRRKDMPYTKEEQQWQAIRRGRYVEFNLIYDRGTQFGLRTPGSRVESILMSLPEHAS WLYNHHPAPGSREAKLLEVTTKPREWVK SWISSNEW:HEM6_YEAST ID HEM6_YEAST STANDARD; PRT; 328 AA. AC P11353; DT 01-JUL-1989 (REL. 11, CREATED) DT 01-JUN-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-JUN-1996 (REL. 34, LAST ANNOTATION UPDATE) DE COPROPORPHYRINOGEN III OXIDASE (EC 1.3.3.3) (COPROPORPHYRINOGENASE) DE (COPROGEN OXIDASE). GN HEM13 OR YD5112.02. OS SACCHAROMYCES CEREVISIAE (BAKER'S YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 88257098. RA ZAGOREC M., BUHLER J.-M., TREICH I., KENG T., GUARENTE L., RA LABBE-BOIS R.; RL J. BIOL. CHEM. 263:9718-9724(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA OLIVER K., HARRIS D., BARRELL B., RAJANDREAM M.A., WALSH S.V.; RL SUBMITTED (JUN-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [3] RP PARTIAL SEQUENCE, AND CHARACTERIZATION. RX MEDLINE; 86192489. RA CAMADRO J.M., CHAMBON H., JOLLES J., LABBE P.; RL EUR. J. BIOCHEM. 156:579-587(1986). CC -!- CATALYTIC ACTIVITY: COPROPORPHYRINOGEN-III + O(2) = CC PROTOPORPHYRINOGEN-IX + 2 CO(2). CC -!- PATHWAY: SIXTH STEP IN HEME BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SUBUNIT: HOMODIMER. CC -!- COFACTOR: CONTAINS TWO IRON ATOMS PER MOLECULE OF NATIVE PROTEIN. CC -!- SIMILARITY: TO OTHER SPECIES COPROPORPHYRINOGEN III OXIDASE. DR EMBL; J03873; G171316; -. DR EMBL; Z49812; G854428; -. DR PIR; A28090; DEBYCH. DR LISTA; SC00429; HEM13. DR SGD; L0000765; HEM13. DR PROSITE; PS01021; COPROGEN_OXIDASE. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; HEME BIOSYNTHESIS; IRON. FT CONFLICT 226 226 K -> N (IN REF. 1). SQ SEQUENCE 328 AA; 37711 MW; 959DF25B CRC32; >HEM6_YEAST MPAPQDPRNLPIRQQMEALIRRKQAEITQGLESIDTVKFHADTWTRGNDGGGGTSMVIQD GTTFEKGGVNVSVVYGQLSPAAVSAMKADHKNLRLPEDPKTGLPVTDGVKFFACGLSMVI HPVNPHAPTTHLNYRYFETWNQDGTPQTWWFGGGADLTPSYLYEEDGQLFHQLHKDALDK HDTALYPRFKKWCDEYFYITHRKETRGIGGIFFDDYDERDPQEILKMVEDCFDAFLPSYL TIVKRRKDMPYTKEEQQWQAIRRGRYVEFNLIYDRGTQFGLRTPGSRVESILMSLPEHAS WLYNHHPAPGSREAKLLEVTTKPREWVK SWISSNEW:HEM6_HUMAN ID HEM6_HUMAN STANDARD; PRT; 354 AA. AC P36551; DT 01-JUN-1994 (REL. 29, CREATED) DT 01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE) DT 01-JUN-1996 (REL. 34, LAST ANNOTATION UPDATE) DE COPROPORPHYRINOGEN III OXIDASE PRECURSOR (EC 1.3.3.3) DE (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE). GN CPO. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=FORESKIN; RX MEDLINE; 94211794. RA MARTASEK P., CAMADRO J.M., DELFAU-LARUE M.H., DUMAS J.B., RA MONTAGNE J.J., DE VERNEUIL H., LABBE P., GRANDCHAMP B.; RL PROC. NATL. ACAD. SCI. U.S.A. 91:3024-3028(1994). RN [2] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=PLACENTA; RX MEDLINE; 94114558. RA TAKETANI S., KOHNO H., FURUKAWA T., YOSHINAGA T., TOKUNAGA R.; RL BIOCHIM. BIOPHYS. ACTA 1183:547-549(1994). RN [3] RP VARIANT HCP TRP-231. RX MEDLINE; 94282043. RA MARTASEK P., NORDMANN Y., GRANDCHAMP B.; RL HUM. MOL. GENET. 3:477-480(1994). RN [4] RP VARIANT HCP SER-89 AND VARIANTS ASN-172 AND ILE-194. RX MEDLINE; 95152503. RA FUJITA H., KONDO M., TAKETANI S., NOMURA N., FURUYAMA K., AKAGI R., RA NAGAI T., TERAJIMA M., GALBRAITH R.A., SASSA S.; RL HUM. MOL. GENET. 3:1807-1810(1994). CC -!- CATALYTIC ACTIVITY: COPROPORPHYRINOGEN-III + O(2) = CC PROTOPORPHYRINOGEN-IX + 2 CO(2). CC -!- PATHWAY: SIXTH STEP IN HEME BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- COFACTOR: IRON (BY SIMILARITY). CC -!- DISEASE: DEFECTS IN CPO ARE THE CAUSE OF HEREDITARY COPROPORPHYRIA CC (HCP), AN AUTOSOMAL DOMINANT DISEASE CHARACTERIZED BY A MASSIVE CC EXCRETION OF COPROPORPHYRIN III IN THE URINE AND PREDOMINANTLY IN CC THE FECES. CC -!- SIMILARITY: TO OTHER SPECIES COPROPORPHYRINOGEN III OXIDASE. DR EMBL; Z28409; G433888; -. DR PIR; S39243; S39243. DR MIM; 121300; 11TH EDITION. DR PROSITE; PS01021; COPROGEN_OXIDASE. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; HEME BIOSYNTHESIS; IRON; KW TRANSIT PEPTIDE; MITOCHONDRION; DISEASE MUTATION; POLYMORPHISM. FT TRANSIT 1 31 MITOCHONDRION. FT CHAIN 32 354 COPROPORPHYRINOGEN III OXIDASE. FT VARIANT 89 89 G -> S (IN HCP; <5% OF ACTIVITY). FT VARIANT 172 172 H -> N. FT VARIANT 194 194 V -> I. FT VARIANT 231 231 R -> W (IN HCP). SQ SEQUENCE 354 AA; 40302 MW; FF81D21D CRC32; >HEM6_HUMAN MLPKTSGTRATSLGRPEEEEDELAHRCSSFMAPPVTDLGELRRRPGDMKTKMELLILETQ AQVCQALAQVDGGANFSVDRWERKEGGGGISCVLQDGCVFEKAGVSISVVHGNLSEEAAK QMRSRGKVLKTKDGKLPFCAMGVSSVTHPKNPHAPTIHFNYRYFEVEEADGHKQWWFGGG CDLTPTYLNQEDAVHFHRTLKEACDQHGPDLYPKFKKWCDDYFFIAHRGERRGIGGIFFD DLDSPSKEEVFRFVQSCARAVVPSYIPLVKKHCDDSFTPQEKLWQQLRRGRYVEFNLLYD RGTKFGLFTPGSRIESILMSLPLTARWEYMHSPSENSKEAEILEVLRHPRDWVR SWISSPROT:HEMZ_RHOSH ID HEMZ_RHOSH STANDARD; PRT; 450 AA. AC P51008; 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 COPROPORPHYRINOGEN III OXIDASE, ANAEROBIC 2 (EC 1.-.-.-) DE (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE). GN HEMZ. OS RHODOBACTER SPHAEROIDES (RHODOPSEUDOMONAS SPHAEROIDES). OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; PURPLE BACTERIA; OC RHODOSPIRILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=2.4.1; RX MEDLINE; 96062223. RA ZEILSTRA-RYALLS J.H., KAPLAN S.; RL J. BACTERIOL. 177:6422-6431(1995). CC -!- FUNCTION: ANAEROBIC TRANSFORMATION OF COPROPORPHYRINOGEN-III INTO CC PROTOPORPHYRINOGEN-IX. DEDICATED TO BACTERIOCHLOROPHYLL CC BIOSYNTHESIS (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL). CC -!- COFACTOR: MAGNESIUM. CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. CC -!- SIMILARITY: TO OTHER SPECIES ANAEROBIC COPROPORPHYRINOGEN III CC OXIDASES. DR EMBL; Z49746; G1070381; -. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; HEME BIOSYNTHESIS; MAGNESIUM. SQ SEQUENCE 450 AA; 49102 MW; C756DFC2 CRC32; >HEMZ_RHOSH MAAVSHLAKLGLFDARVPRYTSYPTAPNFGVGVTENLHADWISSIPAGGSISLYLHVPFC RRLCWFCACRTQGTSSDAPVRAYAAALKSELALLRARLAPGVRLARMHWGGGTPTLLPPT LIHELALAIRDAVPSDAETDFSVEIDPTEIDAARLDALFEAGMTRVSIGVQDFDPLIQQS IGREQSFELTQRLTEDLRHRGLMGLDADILYGLPHQTAPGVADSVQKLLSLSPDRVAVLG YAHVPAVSRRQLMIPTASIPGPEERLDLFETARTLILWDGYQQVGLDHFARAGDPLAHAH ACGRLCRSFQGYTDDRAEVLIGLGASAISRFPQGFTQNAPSTSDHLRAIRSGRFSTARGH VLSDEDRLRGRMIEQLLCEFRISRAQILARFAVAPERLETLFRTCAAAFPGVVEITGHGL EILEEGRPLARIVARSFDRYDASGKPQGAI SWISSPROT:HEMN_SALTY ID HEMN_SALTY STANDARD; PRT; 457 AA. AC P37129; DT 01-OCT-1994 (REL. 30, CREATED) DT 01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE OXYGEN-INDEPENDENT COPROPORPHYRINOGEN III OXIDASE (EC 1.-.-.-) DE (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE). GN HEMN. OS SALMONELLA TYPHIMURIUM. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=LT2; RX MEDLINE; 94252986. RA XU K., ELLIOTT T.; RL J. BACTERIOL. 176:3196-3203(1994). CC -!- FUNCTION: ANAEROBIC TRANSFORMATION OF COPROPORPHYRINOGEN-III INTO CC PROTOPORPHYRINOGEN-IX. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- COFACTOR: REQUIRES MAGNESIUM, ATP AND NAD (OR NADP) FOR ACTIVITY. CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. CC -!- SIMILARITY: TO OTHER SPECIES ANAEROBIC COPROPORPHYRINOGEN III CC OXIDASES. DR EMBL; U06779; G509500; -. DR STYGENE; SG10154; HEMN. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; MAGNESIUM. SQ SEQUENCE 457 AA; 52828 MW; 51F69384 CRC32; >HEMN_SALTY MSEQQIDWDLALIQKYNYSGPRYTSYPTALEFSEDFEDAAFLQAVARYPERPLSLYVHIP FCHKLCYFCGCNKIVTRQQHKADQYLDALEQEIRHRAPLFADRHVSQLHWGGGTPTYLNK AQISRLMTLLRENFHFNTDAEISIEVDPREIELDVLDHLRAEGFNRLSMGVQDFNKEVQR LVNREQDEEFIFALLNHARDIGFTSTNIDLIYGLPKQTPESFAFTLKRVTELNPDRLSVF NYAHLPTLFAAQRKIKDADLPSAQQKLDILQETIVSLTQAGYQFIGMDHFARPDDELAVA QREGVLHRNFQGYTTQGDTDLLGMGVSAISMIGDGYMQNQKELKRYYQQVDERGNALWRG ITLTRDDCIRRDVIKALICNFRLDFNAVEQQWGLHFAEYFAEDLQLLSPLAKDGLVDISE KGIQVTAKGRLLIRNICMCFDAYLRQKARMQQFSRVI SWISSPROT:HEMN_ECOLI ID HEMN_ECOLI STANDARD; PRT; 457 AA. AC P32131; DT 01-OCT-1993 (REL. 27, CREATED) DT 01-FEB-1995 (REL. 31, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE OXYGEN-INDEPENDENT COPROPORPHYRINOGEN III OXIDASE (EC 1.-.-.-) DE (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE). GN HEMN. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 95286520. RA TROUP B., HUNGERER C., JAHN D.; RL J. BACTERIOL. 177:3326-3331(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE; 93347969. RA PLUNKETT G. III, BURLAND V.D., DANIELS D.L., BLATTNER F.R.; RL NUCLEIC ACIDS RES. 21:3391-3398(1993). CC -!- FUNCTION: ANAEROBIC TRANSFORMATION OF COPROPORPHYRINOGEN-III INTO CC PROTOPORPHYRINOGEN-IX. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- COFACTOR: REQUIRES MAGNESIUM, ATP AND NAD (OR NADP) FOR ACTIVITY. CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. CC -!- SIMILARITY: TO OTHER SPECIES ANAEROBIC COPROPORPHYRINOGEN III CC OXIDASES. DR EMBL; X82073; G557233; -. DR EMBL; L19201; G304972; ALT_SEQ. DR ECOGENE; EG11836; HEMN. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; MAGNESIUM. SQ SEQUENCE 457 AA; 52715 MW; 3A1BD948 CRC32; >HEMN_ECOLI MSVQQIDWDLALIQKYNYSGPRYTSYPTALEFSEDFGEQAFLQAVARYPERPLSLYVHIP FCHKLCYFCGCNKIVTRQQHKADQYLDALEQEIVHRAPLFAGRHVSQLHWGGGTPTYLNK AQISRLMKLLRENFQFNADAEISIEVDPREIELDVLDHLRAEGFNRLSMGVQDFNKEVQR LVNREQDEEFIFALLNHAREIGFTSTNIDLIYGLPKQTPESFAFTLKRVAEVNPDRLSVF NYAHLPTIFAAQRKIKDADLPSPQQKLDILQETIAFLTQSGYQFIGMDHFARPDDELAVA QREGVLHRNFQGYTTQGDTDLLGMGVSAISMIGDCYAQNQKELKQYYQQVDEQGNALWRG IALTRDDCIRRDVIKSLICNFRLDYAPIEKQWDLHFADYFAEDLKLLAPLAKDGLVDVDE KGIQVTAKGRLLIRNICMCFDTYLRQKARMQQFSRVI SWISSPROT:HEMN_BACSU ID HEMN_BACSU STANDARD; PRT; 366 AA. AC P54304; 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 OXYGEN-INDEPENDENT COPROPORPHYRINOGEN III OXIDASE DE (EC 1.-.-.-) (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE). GN HEMN. OS BACILLUS SUBTILIS. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=168; RX MEDLINE; 96303504. RA HOMUTH G., HEINEMANN M., ZUBER U., SCHUMANN W.; RL MICROBIOLOGY 142:1641-1649(1996). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=168 / JH642; RA KOBAYASHI Y., MIZUNO M., MASUDA S., TAKEMARU K., HOSONO S., RA SATO T., TAKEUCHI M.; RL SUBMITTED (MAY-1996) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [3] RP SEQUENCE OF 328-366 FROM N.A. RC STRAIN=168 / MB11; RX MEDLINE; 92250426. RA WETZSTEIN M., VOELKER U., DEDIO J., LOEBAU S., ZUBER U., RA SCHIESSWOHL M., HERGET C., HECKER M., SCHUMANN W.; RL J. BACTERIOL. 174:3300-3310(1992). CC -!- FUNCTION: ANAEROBIC TRANSFORMATION OF COPROPORPHYRINOGEN-III INTO CC PROTOPORPHYRINOGEN-IX (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- COFACTOR: REQUIRES MAGNESIUM, ATP AND NAD (OR NADP) FOR ACTIVITY CC (BY SIMILARITY). CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. CC -!- SIMILARITY: TO OTHER SPECIES ANAEROBIC COPROPORPHYRINOGEN III CC OXIDASES. DR EMBL; X91655; -; NOT_ANNOTATED_CDS. DR EMBL; D84432; G1303805; -. DR EMBL; M84964; -; NOT_ANNOTATED_CDS. DR SUBTILIST; BG11395; HEMN. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; MAGNESIUM. FT CONFLICT 94 94 E -> D (IN REF. 2). FT CONFLICT 175 175 S -> I (IN REF. 2). SQ SEQUENCE 366 AA; 41550 MW; 20424298 CRC32; >HEMN_BACSU MKSAYIHIPFCEHICHYCDFNKYFIQSQPVDEYLNALEQEMINTIAKTGQPDLKTIFIGG GTPTSLSEEQLKKLMDMINRVLKPSSDLSEFAVEANPDDLSAEKLKILKEAGVNRLSFGV QTFEDDLLEKIGRVHKQKDVFTSFERAREIGFENISLDLMFGLPGQTLKHLEHSSNTALS LDAEHYSVYSLIVEPKTVFYNLMQKGRLHLPPQEQEAEMYEIVMSKMEAHGIHQYEISNF AKAGMESKHNLTYWSNEQYFGFGAGAHGYIGGTRTVNVGPVKHYIDLIAEKGFPYRDTHE VTTEEQIEEEMFLGLRKTAGVSKKRFAEKYGRSLDGLFPSVLKDLAEKGLIHNSESAVYL THQGNY SWISSPROT:HEMF_RHOSH ID HEMF_RHOSH STANDARD; PRT; 452 AA. AC P33770; DT 01-FEB-1994 (REL. 28, CREATED) DT 01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE COPROPORPHYRINOGEN III OXIDASE, ANAEROBIC 1 (EC 1.-.-.-) DE (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE). GN HEMF. OS RHODOBACTER SPHAEROIDES (RHODOPSEUDOMONAS SPHAEROIDES). OC PROKARYOTA; GRACILICUTES; ANOXYPHOTOBACTERIA; PURPLE BACTERIA; OC RHODOSPIRILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NCIB 8253 / N1; RX MEDLINE; 93086424. RA COOMBER S.A., JONES R.M., JORDAN P.M., HUNTER C.N.; RL MOL. MICROBIOL. 6:3159-3169(1992). CC -!- FUNCTION: ANAEROBIC TRANSFORMATION OF COPROPORPHYRINOGEN-III INTO CC PROTOPORPHYRINOGEN-IX. DEDICATED TO BACTERIOCHLOROPHYLL CC BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- COFACTOR: MAGNESIUM. CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. CC -!- SIMILARITY: TO OTHER SPECIES ANAEROBIC COPROPORPHYRINOGEN III CC OXIDASES. DR EMBL; S50573; G261152; ALT_INIT. DR PIR; S28440; S28440. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; HEME BIOSYNTHESIS; MAGNESIUM. SQ SEQUENCE 452 AA; 50088 MW; 06311371 CRC32; >HEMF_RHOSH MTNIALLQSLGLFDARVPRYTSYPAAPVFSGAVGADFQAQAIEALDPAVPISVYVHVPFC ERLCWFCACRTQGTQTLAPVEAYVGTLLQELELVKQHLPAGVKAGRLHWGGGTPTILSPE LIHKLAQAIKAVIPFAEDYEFSVEIDPMMVDEPKIRALSEEGMNRASIGIQDFTDIVQNA IGREQPFENTKACVQSVRRYGVHSLNTDLVYGLPHQNRESLAATIDKVLSLRPDRVAIFG YAHVPWMAKRQKLIDETVLPPDIERHELANLAARLFTEGGFERIGIDHFALPDDSMAVAA RSRKLRRNFQGYTDDTCPTLLGIGASSISKFEQGYLQNTAATAAYIKSIEEGRLPGYRGH RMTEEDYLHGRAIEMIMCDFFLELPALRARFGEPAETMVLAHRRSGREVTPFVTVDADGS MSIAKEGRALARMIARLFDAYETPEARYSQAS SWISSPROT:HEM6_YEAST ID HEM6_YEAST STANDARD; PRT; 328 AA. AC P11353; DT 01-JUL-1989 (REL. 11, CREATED) DT 01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE COPROPORPHYRINOGEN III OXIDASE (EC 1.3.3.3) (COPROPORPHYRINOGENASE) DE (COPROGEN OXIDASE). GN HEM13 OR YD5112.02. OS SACCHAROMYCES CEREVISIAE (BAKER'S YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 88257098. RA ZAGOREC M., BUHLER J.-M., TREICH I., KENG T., GUARENTE L., RA LABBE-BOIS R.; RL J. BIOL. CHEM. 263:9718-9724(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA OLIVER K., HARRIS D., BARRELL B., RAJANDREAM M.A., WALSH S.V.; RL SUBMITTED (JUN-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [3] RP PARTIAL SEQUENCE, AND CHARACTERIZATION. RX MEDLINE; 86192489. RA CAMADRO J.M., CHAMBON H., JOLLES J., LABBE P.; RL EUR. J. BIOCHEM. 156:579-587(1986). CC -!- CATALYTIC ACTIVITY: COPROPORPHYRINOGEN-III + O(2) = CC PROTOPORPHYRINOGEN-IX + 2 CO(2). CC -!- PATHWAY: SIXTH STEP IN HEME BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- SUBUNIT: HOMODIMER. CC -!- COFACTOR: CONTAINS TWO IRON ATOMS PER MOLECULE OF NATIVE PROTEIN. CC -!- SIMILARITY: TO OTHER SPECIES COPROPORPHYRINOGEN III OXIDASE. DR EMBL; J03873; G171316; -. DR EMBL; Z49812; G854428; -. DR PIR; A28090; DEBYCH. DR LISTA; SC00429; HEM13. DR SGD; L0000765; HEM13. DR PROSITE; PS01021; COPROGEN_OXIDASE. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; HEME BIOSYNTHESIS; IRON. FT CONFLICT 226 226 K -> N (IN REF. 1). SQ SEQUENCE 328 AA; 37711 MW; 959DF25B CRC32; >HEM6_YEAST MPAPQDPRNLPIRQQMEALIRRKQAEITQGLESIDTVKFHADTWTRGNDGGGGTSMVIQD GTTFEKGGVNVSVVYGQLSPAAVSAMKADHKNLRLPEDPKTGLPVTDGVKFFACGLSMVI HPVNPHAPTTHLNYRYFETWNQDGTPQTWWFGGGADLTPSYLYEEDGQLFHQLHKDALDK HDTALYPRFKKWCDEYFYITHRKETRGIGGIFFDDYDERDPQEILKMVEDCFDAFLPSYL TIVKRRKDMPYTKEEQQWQAIRRGRYVEFNLIYDRGTQFGLRTPGSRVESILMSLPEHAS WLYNHHPAPGSREAKLLEVTTKPREWVK SWISSPROT:HEM6_SOYBN ID HEM6_SOYBN STANDARD; PRT; 385 AA. AC P35055; DT 01-FEB-1994 (REL. 28, CREATED) DT 01-FEB-1994 (REL. 28, LAST SEQUENCE UPDATE) DT 01-JUN-1994 (REL. 29, LAST ANNOTATION UPDATE) DE COPROPORPHYRINOGEN III OXIDASE PRECURSOR (EC 1.3.3.3) DE (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE). OS GLYCINE MAX (SOYBEAN). OC EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE; FABALES; OC FABACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. EVANS; TISSUE=ROOT NODULES; RX MEDLINE; 94033295. RA MADSEN O., SANDAL L., SANDAL N.N., MARCKER K.A.; RL PLANT MOL. BIOL. 23:35-43(1993). CC -!- CATALYTIC ACTIVITY: COPROPORPHYRINOGEN-III + O(2) = CC PROTOPORPHYRINOGEN-IX + 2 CO(2). CC -!- PATHWAY: PORPHYRIN AND HEME BIOSYNTHESIS. CC -!- COFACTOR: CONTAINS TWO IRON ATOMS PER MOLECULE OF NATIVE PROTEIN. CC -!- ENZYME REGULATION: PROBABLY REGULATED BY OXYGEN TENSION. CC -!- SUBCELLULAR LOCATION: CHLOROPLAST (PROBABLE). CC -!- DEVELOPMENTAL STAGE: EXPRESION STARTS 10-12 DAYS AFTER INFECTION CC AND CONTINUES DURING THE LIFETIME OF THE NODULE. CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN NODULES AND TO A LESSER CC EXTENT IN LEAVES. NOT DETECTED IN ROOTS. CC -!- SIMILARITY: TO OTHER SPECIES COPROPORPHYRINOGEN III OXIDASE. DR EMBL; X71083; G414667; -. DR EMBL; X71083; G414666; -. DR PIR; S39905; S39905. DR PROSITE; PS01021; COPROGEN_OXIDASE. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; HEME BIOSYNTHESIS; IRON; KW CHLOROPLAST; TRANSIT PEPTIDE. FT TRANSIT 1 67 CHLOROPLAST (POTENTIAL). FT CHAIN 68 385 COPROPORPHYRINOGEN III OXIDASE. FT DOMAIN 116 120 POLY-GLY. SQ SEQUENCE 385 AA; 43265 MW; CBF57FDC CRC32; >HEM6_SOYBN MMHCASIVSAPSYAFPFRSGSASTTPTAISLTKRSWKPPPSMAKGPVRATVSIEKETPEA NRPETFLRGVDEAQSSTSVRARFEKMIREAQDTVCSALEAADGGAQFKEDVWSRPGGGGG ISRVLQDGAVWEKAGVNVSVVYGVMPPDAYRAAKGVPTDQKPGPVPFFAAGISSVLHPKN PFAPTLHFNYRYFETDAPKDAPGAPRQWWFGGGTDLTPAYIFEEDVKHFHSIQKQACDKF EPTFYPRFKKWCDDYFYIKHRGERRGLGGIFFDDLNDYDQEMLLSFATECANSVIPAYLP IIEKRKDLPFNDHQKAWQQLRRGRYVEFNLVYDRGTTFGLKTGGRIESILVSLPLTARWE YDHKPEEGSEEWKLLDACINPKEWI SWISSPROT:HEM6_SALTY ID HEM6_SALTY STANDARD; PRT; 299 AA. AC P33771; DT 01-FEB-1994 (REL. 28, CREATED) DT 01-FEB-1994 (REL. 28, LAST SEQUENCE UPDATE) DT 01-FEB-1995 (REL. 31, LAST ANNOTATION UPDATE) DE COPROPORPHYRINOGEN III OXIDASE, AEROBIC (EC 1.3.3.3) DE (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE). GN HEMF. OS SALMONELLA TYPHIMURIUM. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=LT2; RX MEDLINE; 93352403. RA XU K., ELLIOTT T.; RL J. BACTERIOL. 175:4990-4999(1993). CC -!- CATALYTIC ACTIVITY: COPROPORPHYRINOGEN-III + O(2) = CC PROTOPORPHYRINOGEN-IX + 2 CO(2). CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- COFACTOR: IRON. CC -!- SIMILARITY: TO OTHER SPECIES COPROPORPHYRINOGEN III OXIDASE. DR EMBL; L19503; G310642; -. DR STYGENE; SG10150; HEMF. DR PROSITE; PS01021; COPROGEN_OXIDASE. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; IRON. SQ SEQUENCE 299 AA; 34429 MW; F701B015 CRC32; >HEM6_SALTY MKPDAHHVKQFLLRLQDDICQTLSAVDGANFVEDSWRREAGGGGRSRVLRNGGIFEQAGV NFSHVHGDAMPASATAHRPELAGRSFEAMGVSLVVHPHNPYIPTSHANVRFFIAEKPGAD PVWWFGGGFDLTPYYGFEEDAVHWHRTARDLCQPFGDDVYPRYKKWCDDYFFLKHRNEQR GVGGLFFDDLNTPDFDHCFDFMQAVGNGYTRAYLPIVERRKAMVWGERERNFQLYRRGRY VEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDWQPEAGSPEAALSEFIQVRDWI SWISSPROT:HEM6_PSEAE ID HEM6_PSEAE STANDARD; PRT; 305 AA. AC P43898; 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 COPROPORPHYRINOGEN III OXIDASE, AEROBIC (EC 1.3.3.3) DE (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE). GN HEMF. OS PSEUDOMONAS AERUGINOSA. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; AEROBIC RODS AND COCCI; OC PSEUDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=PAO1; RA HUNGERER C., TROUP B., JAHN D.; RL SUBMITTED (FEB-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- CATALYTIC ACTIVITY: COPROPORPHYRINOGEN-III + O(2) = CC PROTOPORPHYRINOGEN-IX + 2 CO(2). CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- COFACTOR: IRON (BY SIMILARITY). CC -!- SIMILARITY: TO OTHER SPECIES COPROPORPHYRINOGEN III OXIDASE. DR EMBL; X85015; G695693; -. DR PROSITE; PS01021; COPROGEN_OXIDASE. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; IRON. SQ SEQUENCE 305 AA; 34806 MW; 8E00801B CRC32; >HEM6_PSEAE MTDRIAAVKTYLLDLQDRICAALEAEDGKARFAEDAWERPAGGGGRTRVIGDGALIEKGG VNFSHVFGDSLPPSASAHRPELAGRGFQALGVSLVIHPENPHVPTSHANVRFFCAEKEGE EPVWWFGGGFDLTPYYAHEEDCVHWHRVARDACAPFGADVYPRYKEWCDRYFHLKHRNEP RGIGGLFFDDLNQWDFDTCFAFIRAIGDAYIDAYLPIVQRRKHTPFDERQREFQAYRRGR YVEFNLVFDRGTLFGLQSGGRTESILMSLPPQVRWGYDWKPEPGSEEARLTEYFLADRDW LAGQP SWISSPROT:HEM6_MOUSE ID HEM6_MOUSE STANDARD; PRT; 354 AA. AC P36552; DT 01-JUN-1994 (REL. 29, CREATED) DT 01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE) DT 01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE) DE COPROPORPHYRINOGEN III OXIDASE PRECURSOR (EC 1.3.3.3) DE (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE). GN CPO. OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 94012692. RA KOHNO H., FURUKAWA T., YOSHINAGA T., TOKUNAGA R., TAKETANI S.; RL J. BIOL. CHEM. 268:21359-21363(1993). CC -!- CATALYTIC ACTIVITY: COPROPORPHYRINOGEN-III + O(2) = CC PROTOPORPHYRINOGEN-IX + 2 CO(2). CC -!- PATHWAY: SIXTH STEP IN HEME BIOSYNTHESIS. CC -!- COFACTOR: IRON (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- TISSUE SPECIFICITY: ERYTHROID CELLS AND NON ERYTHROID CELLS CC SUCH AS LIVER. CC -!- SIMILARITY: TO OTHER SPECIES COPROPORPHYRINOGEN III OXIDASE. DR EMBL; D16333; G436577; -. DR PIR; A48049; A48049. DR PROSITE; PS01021; COPROGEN_OXIDASE. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; HEME BIOSYNTHESIS; IRON; KW TRANSIT PEPTIDE; MITOCHONDRION. FT TRANSIT 1 31 MITOCHONDRION (BY SIMILARITY). FT CHAIN 32 354 COPROPORPHYRINOGEN III OXIDASE. SQ SEQUENCE 354 AA; 40648 MW; 99F1D5C0 CRC32; >HEM6_MOUSE MVPKSSGARSPSPGRREEDGDELARRCSTFMSSPVTELRELRRRPEDMKTKMELMIMETQ AQVCRALAQVDGVADFTVDRWERKEGGGGITCVLQDGRVFEKAGVSISVVHGNLSEEAAN QMRGRGKTLKTKDSKLPFTAMGVSSVIHPKNPYAPTMHFNYRYFEVEEADGNTHWWFGGG CDLTPRYLNQEDAVHFHRTLKEACDQHGPDIYPKFKKWCDDYFFIVHRGERRGIGGIFFD DLDSPSKEEAFRFVKTCAEAVVPSYVPIVKKHCDDSYTPRDKLWQQLRRGRYVEFNLLYD RGTKFGLFTPGSRIESILMSLPLTARWEYMHSPPENSKEAEILEVLRHPKDWVH SWISSPROT:HEM6_HUMAN ID HEM6_HUMAN STANDARD; PRT; 354 AA. AC P36551; DT 01-JUN-1994 (REL. 29, CREATED) DT 01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE COPROPORPHYRINOGEN III OXIDASE PRECURSOR (EC 1.3.3.3) DE (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE). GN CPO. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=FORESKIN; RX MEDLINE; 94211794. RA MARTASEK P., CAMADRO J.M., DELFAU-LARUE M.H., DUMAS J.B., RA MONTAGNE J.J., DE VERNEUIL H., LABBE P., GRANDCHAMP B.; RL PROC. NATL. ACAD. SCI. U.S.A. 91:3024-3028(1994). RN [2] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=PLACENTA; RX MEDLINE; 94114558. RA TAKETANI S., KOHNO H., FURUKAWA T., YOSHINAGA T., TOKUNAGA R.; RL BIOCHIM. BIOPHYS. ACTA 1183:547-549(1994). RN [3] RP VARIANT HCP TRP-231. RX MEDLINE; 94282043. RA MARTASEK P., NORDMANN Y., GRANDCHAMP B.; RL HUM. MOL. GENET. 3:477-480(1994). RN [4] RP VARIANT HCP SER-89 AND VARIANTS ASN-172 AND ILE-194. RX MEDLINE; 95152503. RA FUJITA H., KONDO M., TAKETANI S., NOMURA N., FURUYAMA K., AKAGI R., RA NAGAI T., TERAJIMA M., GALBRAITH R.A., SASSA S.; RL HUM. MOL. GENET. 3:1807-1810(1994). CC -!- CATALYTIC ACTIVITY: COPROPORPHYRINOGEN-III + O(2) = CC PROTOPORPHYRINOGEN-IX + 2 CO(2). CC -!- PATHWAY: SIXTH STEP IN HEME BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: MITOCHONDRIAL. CC -!- COFACTOR: IRON (BY SIMILARITY). CC -!- DISEASE: DEFECTS IN CPO ARE THE CAUSE OF HEREDITARY COPROPORPHYRIA CC (HCP), AN AUTOSOMAL DOMINANT DISEASE CHARACTERIZED BY A MASSIVE CC EXCRETION OF COPROPORPHYRIN III IN THE URINE AND PREDOMINANTLY IN CC THE FECES. CC -!- SIMILARITY: TO OTHER SPECIES COPROPORPHYRINOGEN III OXIDASE. DR EMBL; Z28409; G433888; -. DR PIR; S39243; S39243. DR MIM; 121300; -. DR PROSITE; PS01021; COPROGEN_OXIDASE. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; HEME BIOSYNTHESIS; IRON; KW TRANSIT PEPTIDE; MITOCHONDRION; DISEASE MUTATION; POLYMORPHISM. FT TRANSIT 1 31 MITOCHONDRION. FT CHAIN 32 354 COPROPORPHYRINOGEN III OXIDASE. FT VARIANT 89 89 G -> S (IN HCP; <5% OF ACTIVITY). FT VARIANT 172 172 H -> N. FT VARIANT 194 194 V -> I. FT VARIANT 231 231 R -> W (IN HCP). SQ SEQUENCE 354 AA; 40302 MW; FF81D21D CRC32; >HEM6_HUMAN MLPKTSGTRATSLGRPEEEEDELAHRCSSFMAPPVTDLGELRRRPGDMKTKMELLILETQ AQVCQALAQVDGGANFSVDRWERKEGGGGISCVLQDGCVFEKAGVSISVVHGNLSEEAAK QMRSRGKVLKTKDGKLPFCAMGVSSVTHPKNPHAPTIHFNYRYFEVEEADGHKQWWFGGG CDLTPTYLNQEDAVHFHRTLKEACDQHGPDLYPKFKKWCDDYFFIAHRGERRGIGGIFFD DLDSPSKEEVFRFVQSCARAVVPSYIPLVKKHCDDSFTPQEKLWQQLRRGRYVEFNLLYD RGTKFGLFTPGSRIESILMSLPLTARWEYMHSPSENSKEAEILEVLRHPRDWVR SWISSPROT:HEM6_ECOLI ID HEM6_ECOLI STANDARD; PRT; 299 AA. AC P36553; DT 01-JUN-1994 (REL. 29, CREATED) DT 01-JUN-1994 (REL. 29, LAST SEQUENCE UPDATE) DT 01-OCT-1994 (REL. 30, LAST ANNOTATION UPDATE) DE COPROPORPHYRINOGEN III OXIDASE, AEROBIC (EC 1.3.3.3) DE (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE). GN HEMF. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 94131946. RA TROUP B., JAHN M., HUNGERER C., JAHN D.; RL J. BACTERIOL. 176:673-680(1994). CC -!- CATALYTIC ACTIVITY: COPROPORPHYRINOGEN-III + O(2) = CC PROTOPORPHYRINOGEN-IX + 2 CO(2). CC -!- PATHWAY: PORPHYRIN BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- COFACTOR: IRON. CC -!- SIMILARITY: TO OTHER SPECIES COPROPORPHYRINOGEN III OXIDASE. DR EMBL; X75413; G453969; -. DR ECOGENE; EG12189; HEMF. DR PROSITE; PS01021; COPROGEN_OXIDASE. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; IRON. SQ SEQUENCE 299 AA; 34322 MW; 21F2593F CRC32; >HEM6_ECOLI MKPDAHQVKQFLLNLQDTICQQLTAVDGAEFVEDSWQREAGGGGRSRVLRNGGVFEQAGV NFSHVHGEAMPASATAHRPELAGRSFEAMGVSLVVHPHNPYVPTSHANVRFFIAEKPGAD PVWWFGGGFDLTPFYGFEEDAIHWHRTARDLCLPFGEDVYPRYKKWCDEYFYLKHRNEQR GIGGLFFDDLNTPDFDRCFAFMQAVGKGYTDAYLPIVERRKAMAYGERERNFQLYRRGRY VEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYQPKDGSPEAALSEFIKVRDWV TREMBL:Q53013 ID Q53013 PRELIMINARY; PRT; 251 AA. AC Q53013; 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 COPROPORPHYRINOGEN III OXIDASE. OS RHIZOBIUM ETLI. OC PROKARYOTA; BACTERIA; GRACILICUTES; SCOTOBACTERIA; OC AEROBIC RODS AND COCCI; RHIZOBIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CE-3; RA VALDERRAMA B., DAVALOS A., MORA J.; RL SUBMITTED (APR-1993) TO EMBL/GENBANK/DDBJ DATA BANKS. DR EMBL; L13618; G294687; -. SQ SEQUENCE 251 AA; 27037 MW; BB030DC1 CRC32; >Q53013 MPQALSVGDVHFGGGSPTIMPSADFLSLMELLRGRFALERGATIAVEVDPRTFTTDMAEA LERTGVNRASVGVQSFDPVVQKAINRIQSEAQVMTAVENLRLYGVRRINFDLMFGLPNQT VQSCLESAMLAIAMRPDRLAVFGYSHVPSFRKNQRLIDTAALPDIAARAEQASAMADTLV AAGYLQIGLDHFALPDDELAIAQRAGRLRRNSLGYSAETCSTVIGLGRPPLVVAATVTFK TISRKAVITGT TREMBL:Q42946 ID Q42946 PRELIMINARY; PRT; 397 AA. AC Q42946; 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 COPROPORPHYRINOGEN OXIDASE (EC 1.3.3.3) (COPROPORPHYRINOGENASE) DE (COPROPORPHYRINOGEN-III OXIDASE) (COPROGEN OXIDASE). GN CPX. 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; 96073433. RA KRUSE E., MOCK H.P., GRIMM B.; RL PLANTA 196:796-803(1995). CC -!- CATALYTIC ACTIVITY: COPROPORPHYRINOGEN-III + O(2) = CC PROTOPORPHYRINOGEN-IX + 2 CO(2). CC -!- COFACTOR: IRON. DR EMBL; X82831; E125695; -. KW OXIDOREDUCTASE. SQ SEQUENCE 397 AA; 44935 MW; 9C7A27BA CRC32; >Q42946 MLTPILSSASCSWTPTSQFPHSWHSSPSFLTKPLNLPFTESYKTAKRPTPNYSFKVQAMI EKEVAVSHKPDAFLRESDMGSNVTSNSSSVRGRFEKMRREAQDSVCLAIEKADGGAKFKE DVWSRPGGGGGHSSVLQDGAVFEKAGVNVSVVYGVMPPEAYRAARPTDNGNVKPGPIPFF AAGVSSVLHPKNPFAPTLHFNYRYFETDAPKDAPGAPRQWWFGGGTDFTPAYIFEEDVKH FHSVQKAACDKFDASFYPRFKKWCVDYFYIKHRDERRGLGGIFFDDFNDYDQEMLLSFST ECANSVIPAYIPIVEKRKDTPFTDKHKAWQQLRRGRYVEFNLVYDRGTTFGLKTGGRIES ILVSLPLTARWEYDHKPEEGTEEWKLLDACINPKEWI TREMBL:Q42840 ID Q42840 PRELIMINARY; PRT; 391 AA. AC Q42840; 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 COPROPORPHYRINOGEN OXIDASE (EC 1.3.3.3) (COPROPORPHYRINOGENASE) DE (COPROPORPHYRINOGEN-III OXIDASE) (COPROGEN OXIDASE). GN CPX. 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; 96073433. RA KRUSE E., MOCK H.P., GRIMM B.; RL PLANTA 196:796-803(1995). CC -!- CATALYTIC ACTIVITY: COPROPORPHYRINOGEN-III + O(2) = CC PROTOPORPHYRINOGEN-IX + 2 CO(2). CC -!- COFACTOR: IRON. DR EMBL; X82830; E125694; -. KW OXIDOREDUCTASE. SQ SEQUENCE 391 AA; 43556 MW; 8BC8B5F5 CRC32; >Q42840 MASSLLTTPSQTLAPNPAAARARRSSPAAAQVSFSSPLLPGRRALRCARPVAIEKEVPEK EAPTTFLREDGSGAGSGSVRERFEGMIRRVQGEICAALEEADGSGKRFVEDVWSRPGGVC VHSRVLQDGNVFEKAGVNVSAVIGVCPRSAYRAAKGAAKNGAADGHKAGPVPFFSAGISS VLHPKNPFAPTLHFNYRYFETDAPKDVPGAPRSWWFGGGTDLTPSYLIEEDVKHFHSVQK QTCDKFDPSFYPRFKKWCDDYFYIKHRNERRGLGGIFFDDLNDYDQDMLLNFATECAGSV IPAYIPIIERRKDTPFNEEQKAWQQVRRGRYVEFNLVYDRGTTFGLKTGGRIESILVSLP LTARWEYDHKPEEGSEEWKLLDACINPKEWL TREMBL:Q39581 ID Q39581 PRELIMINARY; PRT; 142 AA. AC Q39581; 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 COPROPORPHYRINOGEN OXIDASE (FRAGMENT). GN CPX. OS CHLAMYDOMONAS REINHARDTII. OC EUKARYOTA; PLANTA; PHYCOPHYTA; CHLOROPHYTA (GREEN ALGAE); OC CHLOROPHYCEAE; VOLVOCALES; CHLAMYDOMONADACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 95196749. RA HILL K.L., MERCHANT S.; RL EMBO J. 14:857-865(1995). RN [2] RP SEQUENCE FROM N.A. RA HILL K.L.; RL THESIS (1994), CHEMISTRY & BIOCHEMISTRY, UNIVERSITY OF CALIFORNIA, RL LOS ANGELES DR EMBL; U26344; G837300; -. FT NON_TER 1 1 FT NON_TER 142 142 SQ SEQUENCE 142 AA; 17124 MW; B95D4DD3 CRC32; >Q39581 HFNYRYFETEEWNAIPGQWWLGGGTDITPSYVVPEDMKHFHGTYKAVCDRHDPAYYYEKF RTWCDEYFLIKHRAEPRALGGIFFDDLNDRNPEDILKFSTDAVNNVVEAYCPIIKKHMND PYTPEEKEWQQIRRGRYVEFNL TREMBLNEW:ECD874_2 ID ECD874_2 standard; PRT; 299 AA. AC D90874; DR EMBL; D90874; ECD874. SuspectSTRv DE gene: "hemF"; product: "COPROPORPHYRINOGEN III OXIDASE, AEROBIC (EC DE 1.3.3.3) (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE)."; DE E.coli genomic DNA, Kohara clone #421(55.1-55.5 min.). OS Escherichia coli OC Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OG Plasmid pColK-K235 FT CDS 59..958 FT /gene="hemF" FT /note="similar to [SwissProt Accession Number P36553]" FT /codon_start=1 FT /product="COPROPORPHYRINOGEN III OXIDASE, AEROBIC (EC FT 1.3.3.3) (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE)." FT /transl_table=11 FT /db_xref="PID:g1799873" FT /translation="MKPDAHQVKQFLLNLQDTICQQLTAVDGAEFVEDSWQREAGGGGR FT SRVLRNGGVFEQAGVNFSHVHGEAMPASATAHRPELAGRSFEAMGVSLVVHPHNPYVPT FT SHANVRFFIAEKPGADPVWWFGGGFDLTPFYGFEEDAIHWHRTARDLCLPFGEDVYPRY FT KKWCDEYFYLKHRNEQRGIGGLFFDDLNTPDFDRCFAFMQAVGKGYTDAYLPIVERRKA FT MAYGERERNFQLYRRGRYVEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYQPK FT DGSPEAALSEFIKVRDWV" SQ Sequence 299 BP; >ECD874_2 MKPDAHQVKQFLLNLQDTICQQLTAVDGAEFVEDSWQREAGGGGRSRVLRNGGVFEQAGV NFSHVHGEAMPASATAHRPELAGRSFEAMGVSLVVHPHNPYVPTSHANVRFFIAEKPGAD PVWWFGGGFDLTPFYGFEEDAIHWHRTARDLCLPFGEDVYPRYKKWCDEYFYLKHRNEQR GIGGLFFDDLNTPDFDRCFAFMQAVGKGYTDAYLPIVERRKAMAYGERERNFQLYRRGRY VEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYQPKDGSPEAALSEFIKVRDWV TREMBLNEW:ECD873_5 ID ECD873_5 standard; PRT; 299 AA. AC D90873; DR EMBL; D90873; ECD873. SuspectSTRv DE gene: "hemF"; product: "COPROPORPHYRINOGEN III OXIDASE, AEROBIC (EC DE 1.3.3.3) (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE)."; DE E.coli genomic DNA, Kohara clone #420(54.9-55.2 min.). OS Escherichia coli OC Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OG Plasmid pColK-K235 FT CDS 7163..8062 FT /gene="hemF" FT /note="similar to [SwissProt Accession Number P36553]" FT /codon_start=1 FT /product="COPROPORPHYRINOGEN III OXIDASE, AEROBIC (EC FT 1.3.3.3) (COPROPORPHYRINOGENASE) (COPROGEN OXIDASE)." FT /transl_table=11 FT /db_xref="PID:g1799866" FT /translation="MKPDAHQVKQFLLNLQDTICQQLTAVDGAEFVEDSWQREAGGGGR FT SRVLRNGGVFEQAGVNFSHVHGEAMPASATAHRPELAGRSFEAMGVSLVVHPHNPYVPT FT SHANVRFFIAEKPGADPVWWFGGGFDLTPFYGFEEDAIHWHRTARDLCLPFGEDVYPRY FT KKWCDEYFYLKHRNEQRGIGGLFFDDLNTPDFDRCFAFMQAVGKGYTDAYLPIVERRKA FT MAYGERERNFQLYRRGRYVEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYQPK FT DGSPEAALSEFIKVRDWV" SQ Sequence 299 BP; >ECD873_5 MKPDAHQVKQFLLNLQDTICQQLTAVDGAEFVEDSWQREAGGGGRSRVLRNGGVFEQAGV NFSHVHGEAMPASATAHRPELAGRSFEAMGVSLVVHPHNPYVPTSHANVRFFIAEKPGAD PVWWFGGGFDLTPFYGFEEDAIHWHRTARDLCLPFGEDVYPRYKKWCDEYFYLKHRNEQR GIGGLFFDDLNTPDFDRCFAFMQAVGKGYTDAYLPIVERRKAMAYGERERNFQLYRRGRY VEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYQPKDGSPEAALSEFIKVRDWV TREMBLNEW:ECAE462_3 ID ECAE462_3 standard; PRT; 459 AA. AC AE000462; DR EMBL; AE000462; ECAE462. SuspectSTRv DE gene: "hemN"; product: "oxygen-independent coproporphyrinogen III oxidase"; DE DE Escherichia coli from bases 4047390 to 4057720 (section 352 of 400) DE of the complete genome. OS Escherichia coli OC Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OG Chloroplast FT CDS 1972..3351 FT /gene="hemN" FT /EC_number="1.-.-.-" FT /note="o459; 99 pct identical to 457 amino acids of FT HEMN_ECOLI SW: P32131 but has 2 additional N-ter residues" FT /codon_start=1 FT /product="oxygen-independent coproporphyrinogen III FT oxidase" FT /transl_table=11 FT /db_xref="PID:g1790298" FT /translation="MSMSVQQIDWDLALIQKYNYSGPRYTSYPTALEFSEDFGEQAFLQ FT AVARYPERPLSLYVHIPFCHKLCYFCGCNKIVTRQQHKADQYLDALEQEIVHRAPLFAG FT RHVSQLHWGGGTPTYLNKAQISRLMKLLRENFQFNADAEISIEVDPREIELDVLDHLRA FT EGFNRLSMGVQDFNKEVQRLVNREQDEEFIFALLNHAREIGFTSTNIDLIYGLPKQTPE FT SFAFTLKRVAELNPDRLSVFNYAHLPTIFAAQRKIKDADLPSPQQKLDILQETIAFLTQ FT SGYQFIGMDHFARPDDELAVAQREGVLHRNFQGYTTQGDTDLLGMGVSAISMIGDCYAQ FT NQKELKQYYQQVDEQGNALWRGIALTRDDCIRRDVIKSLICNFRLDYAPIEKQWDLHFA FT DYFAEDLKLLAPLAKDGLVDVDEKGIQVTAKGRLLIRNICMCFDTYLRQKARMQQFSRV FT I" SQ Sequence 459 BP; >ECAE462_3 MSMSVQQIDWDLALIQKYNYSGPRYTSYPTALEFSEDFGEQAFLQAVARYPERPLSLYVH IPFCHKLCYFCGCNKIVTRQQHKADQYLDALEQEIVHRAPLFAGRHVSQLHWGGGTPTYL NKAQISRLMKLLRENFQFNADAEISIEVDPREIELDVLDHLRAEGFNRLSMGVQDFNKEV QRLVNREQDEEFIFALLNHAREIGFTSTNIDLIYGLPKQTPESFAFTLKRVAELNPDRLS VFNYAHLPTIFAAQRKIKDADLPSPQQKLDILQETIAFLTQSGYQFIGMDHFARPDDELA VAQREGVLHRNFQGYTTQGDTDLLGMGVSAISMIGDCYAQNQKELKQYYQQVDEQGNALW RGIALTRDDCIRRDVIKSLICNFRLDYAPIEKQWDLHFADYFAEDLKLLAPLAKDGLVDV DEKGIQVTAKGRLLIRNICMCFDTYLRQKARMQQFSRVI TREMBLNEW:ECAE331_2 ID ECAE331_2 standard; PRT; 299 AA. AC AE000331; DR EMBL; AE000331; ECAE331. DE gene: "hemF"; product: "coproporphyrinogen III oxidase"; DE Escherichia coli from bases 2550064 to 2561168 (section 221 of 400) DE of the complete genome. OS Escherichia coli OC Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OG Chloroplast FT CDS 955..1854 FT /gene="hemF" FT /EC_number="1.3.3.3" FT /note="o299; 100 pct identical to HEM6_ECOLI SW: P36553" FT /codon_start=1 FT /product="coproporphyrinogen III oxidase" FT /transl_table=11 FT /db_xref="PID:g1788777" FT /translation="MKPDAHQVKQFLLNLQDTICQQLTAVDGAEFVEDSWQREAGGGGR FT SRVLRNGGVFEQAGVNFSHVHGEAMPASATAHRPELAGRSFEAMGVSLVVHPHNPYVPT FT SHANVRFFIAEKPGADPVWWFGGGFDLTPFYGFEEDAIHWHRTARDLCLPFGEDVYPRY FT KKWCDEYFYLKHRNEQRGIGGLFFDDLNTPDFDRCFAFMQAVGKGYTDAYLPIVERRKA FT MAYGERERNFQLYRRGRYVEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYQPK FT DGSPEAALSEFIKVRDWV" SQ Sequence 299 BP; >ECAE331_2 MKPDAHQVKQFLLNLQDTICQQLTAVDGAEFVEDSWQREAGGGGRSRVLRNGGVFEQAGV NFSHVHGEAMPASATAHRPELAGRSFEAMGVSLVVHPHNPYVPTSHANVRFFIAEKPGAD PVWWFGGGFDLTPFYGFEEDAIHWHRTARDLCLPFGEDVYPRYKKWCDEYFYLKHRNEQR GIGGLFFDDLNTPDFDRCFAFMQAVGKGYTDAYLPIVERRKAMAYGERERNFQLYRRGRY VEFNLVWDRGTLFGLQTGGRTESILMSMPPLVRWEYDYQPKDGSPEAALSEFIKVRDWV TREMBLNEW:SSD901_40 ID SSD901_40 standard; PRT; 340 AA. AC D90901; DR EMBL; D90901; SSD901. DE gene: "hemF"; product: "coproporphyrinogen III oxidase"; DE Synechocystis sp. PCC6803 complete genome, 3/27, 271600-402289. OS Synechocystis sp. OC Eubacteria; Cyanobacteria; Chroococcales; Synechocystis. OG Mitochondrion FT CDS complement(44283..45305) FT /gene="hemF" FT /note="ORF_ID:sll1185" FT /codon_start=1 FT /product="coproporphyrinogen III oxidase" FT /transl_table=11 FT /db_xref="PID:g1651937" FT /translation="MTVSPTTQPQTNHSLPPADAKQRVSQFMQTLQDEICQGLEALDGK FT GKFQEDSWQREEGGGGRSRVLADGDFLEQGGVNFSEVWGKSLPPSILKQRPEAEGHEFY FT ATGTSMVLHPKNPYIPTVHLNYRYFEAGPVWWFGGGADLTPYYPFAEDAAHFHHTLKNA FT CDQTHGEFYPVFKRWCDEYFYLKHRQEMRGIGGIFFDYQDGNAPLYRGPDPNGPAAQYS FT NQLAPIEPLGWEDLFSFAQRCGRAFLPAYSPIVEKRRNTEYGDRQRQFQLYRRGRYVEF FT NLVYDRGTIFGLQTNGRTESILMSLPPLVRWQYCYSPEAGSPEAELTEKFLVPQDWVNS FT " SQ Sequence 340 BP; >SSD901_40 MTVSPTTQPQTNHSLPPADAKQRVSQFMQTLQDEICQGLEALDGKGKFQEDSWQREEGGG GRSRVLADGDFLEQGGVNFSEVWGKSLPPSILKQRPEAEGHEFYATGTSMVLHPKNPYIP TVHLNYRYFEAGPVWWFGGGADLTPYYPFAEDAAHFHHTLKNACDQTHGEFYPVFKRWCD EYFYLKHRQEMRGIGGIFFDYQDGNAPLYRGPDPNGPAAQYSNQLAPIEPLGWEDLFSFA QRCGRAFLPAYSPIVEKRRNTEYGDRQRQFQLYRRGRYVEFNLVYDRGTIFGLQTNGRTE SILMSLPPLVRWQYCYSPEAGSPEAELTEKFLVPQDWVNS TREMBLNEW:RSU80081_2 ID RSU80081_2 standard; PRT; 212 AA. AC U80081; DR EMBL; U80081; RSU80081. DE gene: "regX"; product: "putative response regulator"; DE Rhodobacter sphaeroides oxygen-independent coproporphyrinogen DE oxidase (hemN) and putative response regulator (regX) genes, DE complete cds. OS Rhodobacter sphaeroides OC Eubacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. OG Mitochondrion FT CDS complement(1479..2117) FT /gene="regX" FT /note="inactivation of regX does not prevent anaerobic FT growth on nitrate; similar to NarL and NarP" FT /codon_start=1 FT /product="putative response regulator" FT /transl_table=11 FT /db_xref="PID:g1724131" FT /translation="MIDPRTLERECLVRCVELAHPEIKVMGFGSIDEWQNRRDRHGHEV FT ILYSTGNRPVTEVSREIATLVAEAGVGPVVVIGAANDLCEMIAAFDCGARSYLPSSVGI FT DDIVERAALRPSTGSSCRRRRDGPARRPSDREESHMAVNEHLTERQRAVCDAVRRGKSN FT KIIAGELNLCESTVKVHIRNIMKKLGAKNRTEAAFKLNSSMFAGEGRLS" SQ Sequence 212 BP; >RSU80081_2 MIDPRTLERECLVRCVELAHPEIKVMGFGSIDEWQNRRDRHGHEVILYSTGNRPVTEVSR EIATLVAEAGVGPVVVIGAANDLCEMIAAFDCGARSYLPSSVGIDDIVERAALRPSTGSS CRRRRDGPARRPSDREESHMAVNEHLTERQRAVCDAVRRGKSNKIIAGELNLCESTVKVH IRNIMKKLGAKNRTEAAFKLNSSMFAGEGRLS TREMBLNEW:RSU80081_1 ID RSU80081_1 standard; PRT; 452 AA. AC U80081; DR EMBL; U80081; RSU80081. DE gene: "hemN"; product: "oxygen-independent coproporphyrinogen oxidase"; DE Rhodobacter sphaeroides oxygen-independent coproporphyrinogen DE oxidase (hemN) and putative response regulator (regX) genes, DE complete cds. OS Rhodobacter sphaeroides OC Eubacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. OG Mitochondrion FT CDS 71..1429 FT /gene="hemN" FT /note="inactivation of hemN prevents anaerobic growth both FT photosynthetically and with nitrate" FT /codon_start=1 FT /product="oxygen-independent coproporphyrinogen oxidase" FT /transl_table=11 FT /db_xref="PID:g1724130" FT /translation="MTNIALLQSLGLFDARVPRYTCYPAAPVFSGAVGADFQAQAIEAL FT DPAVPISVYIHVPFCERLCWFCACPTQGTQTLAPVEAYVGTLLQELELVKKHLPAGVKA FT GRLHWGGGTPTILSPELIHKLAQAIKAVIPFAEDYEFSVEIDPMMVDEPKIRALSEEGM FT NRASIGIQDFTDIVQSAIGREQPFENTRACVETCARYGVHSLNTDLVYGLPHQNRESLA FT ATIDKVLQLGPDRVAIFGYAHVPWMAKRQKLIDENVLPNDMERHELANLAAKMFTEGGF FT ERIGIDHFARPDDSMAVAARTGKLGRNFQGYTDDTCPTLLGIGASSISKFEQGYLQNTA FT ATAAYIKAIEEGRLPAYRGHRMTDEDYLHGRAIEMIMCEFRLDLPALRARFGEAAETMV FT PRLTEAAAKFAPFITVDEAGSMSIEAEGRALTRMIARVFDAYESPEARYSQAS" SQ Sequence 452 BP; >RSU80081_1 MTNIALLQSLGLFDARVPRYTCYPAAPVFSGAVGADFQAQAIEALDPAVPISVYIHVPFC ERLCWFCACPTQGTQTLAPVEAYVGTLLQELELVKKHLPAGVKAGRLHWGGGTPTILSPE LIHKLAQAIKAVIPFAEDYEFSVEIDPMMVDEPKIRALSEEGMNRASIGIQDFTDIVQSA IGREQPFENTRACVETCARYGVHSLNTDLVYGLPHQNRESLAATIDKVLQLGPDRVAIFG YAHVPWMAKRQKLIDENVLPNDMERHELANLAAKMFTEGGFERIGIDHFARPDDSMAVAA RTGKLGRNFQGYTDDTCPTLLGIGASSISKFEQGYLQNTAATAAYIKAIEEGRLPAYRGH RMTDEDYLHGRAIEMIMCEFRLDLPALRARFGEAAETMVPRLTEAAAKFAPFITVDEAGS MSIEAEGRALTRMIARVFDAYESPEARYSQAS TREMBLNEW:PHU46781_7 ID PHU46781_7 standard; PRT; 1055 AA. AC U46781; DR EMBL; U46781; PHU46781. DE gene: "hsdR"; product: "HSDR"; DE Pasteurella haemolytica putative coproporphyrinogen III oxidase DE (hemN') gene, partial cds, leukotoxin transcriptional activator and DE restriction modification methylase subunit (alxA-hsdM), (hsdS) and DE (hsdR) genes, complete cds. OS Pasteurella haemolytica OC Eubacteria; Proteobacteria; gamma subdivision; Pasteurellaceae; OC Pasteurella. OG Mitochondrion FT CDS 5317..8484 FT /gene="hsdR" FT /note="restriction modification restriction subunit" FT /codon_start=1 FT /product="HSDR" FT /transl_table=11 FT /db_xref="PID:g1685100" FT /translation="MITINENTIEQSAIATLQSLGWDYTYGKKILAGLEHEWRDGTAEV FT ILKPLLAQAIAKFNPNLPACEVENVVAQVCRADSGDLADGNRQAYDWLRNGVKITYQLY FT GEQVSDVVQLIDFQRPENNDFRIVNQLDISGKKGKRIPDLIGFVNGLPLVVFELKNPLK FT ENADIGKAFAQLQTYKDEISDLFVFNQALVISDGIVARIGSLTADFDRFTPWRVVDEKN FT QSKRIVFEDELTALLQGVMTPKNLLDYVQNFVVFERDGKNRLIKKIGAYHQFYGVNEAV FT DCTLLAATGNRKIGVFWHTQGSGKSLSMLFYAGKVLSQSSLKNPTLVLVTDRNDLDGQL FT YATFCGGEALLKQTPIQADGRDELRSALASRSAGGVIFTTIQKFGLMEGELAHPVLNER FT ENIIVITDEAHRSQYGFSQKINHKGEYREGYAKHLRSALPNASFIGFTGTPIELDDKDT FT QEVFGKYVSIYDFEDAVEDGATVPIIYEPRQISLGESGEFSKVMEEAQQLIDDDENSYN FT FRLREKLHSVDSRLQKMAEDIIAHYDERTKQQDGKAMVVVMSRAICVKLYEKITALRPE FT WHSNDVLQGSIKIVMTSNASDPAEWQKHNQDKKTLEKRFKDPDDPLNIVIVRDMWLTGF FT DAPCCNTMYIDKPMSGHNLMQAIARVNRVFRNKSRENGGLIVDYVGLTDELEKAMKQYT FT NAGGKEKPVRDISAVLEKMVEHITVIRGQFAHRLTDKRLILPKMLQISEPPKLLNAILT FT SANHILALDRIQPPDNTAKDKTPRKNAFLQSVRLAEKGYALCGALKAVEPYKQELAFYD FT AVRATIIKNSTAPRNSSSENDRLLQLTALMNRAVQSDGVVDLFDLLKKDRPNINLLSDE FT FLETVKNSPTKDLWLSAMERYLASQLRDESGANLATKKAFEQKLKEAMNQYHNHNLSVL FT EILEELIALAKEFEARQKRGEALGLSPAEMAFYDALARNESAVREMGDEVLMKLAKDIT FT DKLRKSVTVDWQYKDSVRAKMRTLIALLCVPINTRPIYRRKRLSLCCNKRKRSPESSLS FT PKRRNLY" SQ Sequence 1055 BP; >PHU46781_7 MITINENTIEQSAIATLQSLGWDYTYGKKILAGLEHEWRDGTAEVILKPLLAQAIAKFNP NLPACEVENVVAQVCRADSGDLADGNRQAYDWLRNGVKITYQLYGEQVSDVVQLIDFQRP ENNDFRIVNQLDISGKKGKRIPDLIGFVNGLPLVVFELKNPLKENADIGKAFAQLQTYKD EISDLFVFNQALVISDGIVARIGSLTADFDRFTPWRVVDEKNQSKRIVFEDELTALLQGV MTPKNLLDYVQNFVVFERDGKNRLIKKIGAYHQFYGVNEAVDCTLLAATGNRKIGVFWHT QGSGKSLSMLFYAGKVLSQSSLKNPTLVLVTDRNDLDGQLYATFCGGEALLKQTPIQADG RDELRSALASRSAGGVIFTTIQKFGLMEGELAHPVLNERENIIVITDEAHRSQYGFSQKI NHKGEYREGYAKHLRSALPNASFIGFTGTPIELDDKDTQEVFGKYVSIYDFEDAVEDGAT VPIIYEPRQISLGESGEFSKVMEEAQQLIDDDENSYNFRLREKLHSVDSRLQKMAEDIIA HYDERTKQQDGKAMVVVMSRAICVKLYEKITALRPEWHSNDVLQGSIKIVMTSNASDPAE WQKHNQDKKTLEKRFKDPDDPLNIVIVRDMWLTGFDAPCCNTMYIDKPMSGHNLMQAIAR VNRVFRNKSRENGGLIVDYVGLTDELEKAMKQYTNAGGKEKPVRDISAVLEKMVEHITVI RGQFAHRLTDKRLILPKMLQISEPPKLLNAILTSANHILALDRIQPPDNTAKDKTPRKNA FLQSVRLAEKGYALCGALKAVEPYKQELAFYDAVRATIIKNSTAPRNSSSENDRLLQLTA LMNRAVQSDGVVDLFDLLKKDRPNINLLSDEFLETVKNSPTKDLWLSAMERYLASQLRDE SGANLATKKAFEQKLKEAMNQYHNHNLSVLEILEELIALAKEFEARQKRGEALGLSPAEM AFYDALARNESAVREMGDEVLMKLAKDITDKLRKSVTVDWQYKDSVRAKMRTLIALLCVP INTRPIYRRKRLSLCCNKRKRSPESSLSPKRRNLY TREMBLNEW:PHU46781_6 ID PHU46781_6 standard; PRT; 442 AA. AC U46781; DR EMBL; U46781; PHU46781. DE gene: "hsdS"; product: "HSDS"; DE Pasteurella haemolytica putative coproporphyrinogen III oxidase DE (hemN') gene, partial cds, leukotoxin transcriptional activator and DE restriction modification methylase subunit (alxA-hsdM), (hsdS) and DE (hsdR) genes, complete cds. OS Pasteurella haemolytica OC Eubacteria; Proteobacteria; gamma subdivision; Pasteurellaceae; OC Pasteurella. OG Mitochondrion FT CDS 3989..5317 FT /gene="hsdS" FT /note="restriction modification specificity subunit" FT /codon_start=1 FT /product="HSDS" FT /transl_table=11 FT /db_xref="PID:g1685099" FT /translation="MAFNQYVFSDIVELISEKIKIKDLKKENYISTDNMLPNFGGITLA FT ENLPNSASCNRFAKKDILFSNIRTYFKKVWLAEFSGGCSPDVLVMRSKNTDILLNEYLF FT LLIRSDDFINFTVISANGAKMPRGDKNAMKGFIFNIPSIEYQKKCIANYFAFDQKIQLN FT TQTNQTLEAIAQAIFKSWFVDFDPVRAKAAALSEGKSEHEANLAAMSVICGKDTSELND FT TEYKALWQIAEAFPSEFGDEGLPIGWKFNQADNLFDVGIGKTPPRKESEWFSDNANDTE FT WISIKDMGNQGLFITESSEYLKAEAVDTFNIKRIPENTVILSFKLTVGRVSITTKETTT FT NEAIAHFKIPSSSNLSSEFLYCYLKNFDFNNLGSTSSIATAVNSKMIKEMEILEPSVLV FT INHFNEYIEGIFNKIKENIIQNNNLSKIRDKLLPKLLSGEMEL" SQ Sequence 442 BP; >PHU46781_6 MAFNQYVFSDIVELISEKIKIKDLKKENYISTDNMLPNFGGITLAENLPNSASCNRFAKK DILFSNIRTYFKKVWLAEFSGGCSPDVLVMRSKNTDILLNEYLFLLIRSDDFINFTVISA NGAKMPRGDKNAMKGFIFNIPSIEYQKKCIANYFAFDQKIQLNTQTNQTLEAIAQAIFKS WFVDFDPVRAKAAALSEGKSEHEANLAAMSVICGKDTSELNDTEYKALWQIAEAFPSEFG DEGLPIGWKFNQADNLFDVGIGKTPPRKESEWFSDNANDTEWISIKDMGNQGLFITESSE YLKAEAVDTFNIKRIPENTVILSFKLTVGRVSITTKETTTNEAIAHFKIPSSSNLSSEFL YCYLKNFDFNNLGSTSSIATAVNSKMIKEMEILEPSVLVINHFNEYIEGIFNKIKENIIQ NNNLSKIRDKLLPKLLSGEMEL TREMBLNEW:PHU46781_5 ID PHU46781_5 standard; PRT; 616 AA. AC U46781; DR EMBL; U46781; PHU46781. DE gene: "alxA-hsdM"; product: "ALXA and HSDM"; DE Pasteurella haemolytica putative coproporphyrinogen III oxidase DE (hemN') gene, partial cds, leukotoxin transcriptional activator and DE restriction modification methylase subunit (alxA-hsdM), (hsdS) and DE (hsdR) genes, complete cds. OS Pasteurella haemolytica OC Eubacteria; Proteobacteria; gamma subdivision; Pasteurellaceae; OC Pasteurella. OG Mitochondrion FT CDS 2149..3999 FT /gene="alxA-hsdM" FT /note="13 STAQH repeats within amino terminus of predicted FT peptide; activator of leukotoxin transcription and FT restriction modification methylase subunit; two peptides FT produced from precursor" FT /codon_start=1 FT /product="ALXA and HSDM" FT /transl_table=11 FT /db_xref="PID:g1747491" FT /translation="MPNSTAQHSTAQHSTAQHSTAQHSTAQHSTAQHSTAQHSTAQHST FT AQHSTAQHSTAQHSTAQHSTAQHSVISTSDTSQAFLNELDQTLWTAADKLRKNLDAANY FT KHIVLGFIFLKYISDSFTDFQAKLKTQLTTPESELYLDPALFDEQEFSQILAEELEQRD FT YYAAENIFWVPEQARWDNIKSLSKLNLGDELPWGDKFKGVSRLIDDAFEAIERENPKLK FT GVLQRIAGFGVPDEMLTGLIDLFSRTNFTQPMHNGEPVHLQAKDILGHVYEYFLGQFAL FT AEGKKGGQYFTPKSIVTLIVEMLEPYSGRIYDPAMGSGGFFVQADRFIQAHAGNRNAIS FT VYGQESNSTTRKLAVMNMAIRGIPFDFGDKPEDTLLNPLHIDKKMDVVMANPPFNQKEW FT WNESLANDPRWAYGTPPQGNANFAWLQHMIYHLSPKGKMALLPRNGSMSSQTSGEGDIR FT KNIVQADLVEAMIALPNQLFTNTQIPACIWIINKAKARKGEVLFINATQIGYLKDRVLR FT DFTADDIAKISDTYHNWQKQNGYENIPAFCYCATLDEIAKNDFVLTAGRYVGAVQEEND FT GVRFAEKMQELTALLNEQFKQGRELEQQIAENLKGLGYGI" SQ Sequence 616 BP; >PHU46781_5 MPNSTAQHSTAQHSTAQHSTAQHSTAQHSTAQHSTAQHSTAQHSTAQHSTAQHSTAQHST AQHSTAQHSVISTSDTSQAFLNELDQTLWTAADKLRKNLDAANYKHIVLGFIFLKYISDS FTDFQAKLKTQLTTPESELYLDPALFDEQEFSQILAEELEQRDYYAAENIFWVPEQARWD NIKSLSKLNLGDELPWGDKFKGVSRLIDDAFEAIERENPKLKGVLQRIAGFGVPDEMLTG LIDLFSRTNFTQPMHNGEPVHLQAKDILGHVYEYFLGQFALAEGKKGGQYFTPKSIVTLI VEMLEPYSGRIYDPAMGSGGFFVQADRFIQAHAGNRNAISVYGQESNSTTRKLAVMNMAI RGIPFDFGDKPEDTLLNPLHIDKKMDVVMANPPFNQKEWWNESLANDPRWAYGTPPQGNA NFAWLQHMIYHLSPKGKMALLPRNGSMSSQTSGEGDIRKNIVQADLVEAMIALPNQLFTN TQIPACIWIINKAKARKGEVLFINATQIGYLKDRVLRDFTADDIAKISDTYHNWQKQNGY ENIPAFCYCATLDEIAKNDFVLTAGRYVGAVQEENDGVRFAEKMQELTALLNEQFKQGRE LEQQIAENLKGLGYGI TREMBLNEW:PHU46781_4 ID PHU46781_4 standard; PRT; 125 AA. AC U46781; DR EMBL; U46781; PHU46781. DE Pasteurella haemolytica putative coproporphyrinogen III oxidase DE (hemN') gene, partial cds, leukotoxin transcriptional activator and DE restriction modification methylase subunit (alxA-hsdM), (hsdS) and DE (hsdR) genes, complete cds. OS Pasteurella haemolytica OC Eubacteria; Proteobacteria; gamma subdivision; Pasteurellaceae; OC Pasteurella. OG Mitochondrion FT CDS complement(1594..1971) FT /note="orf1" FT /codon_start=1 FT /transl_table=11 FT /db_xref="PID:g1685096" FT /translation="MEYQFTHSIHGVVAKCSMDHEAFARWLNAEITENPSQLAPIFAEI FT EKCRAAFPNHYECVFEGREYSLYFDYDEVMAKANNLDAAFDDEEMEEGFQFYNEESIAF FT CGLDDFEKFLKAYQHFVQTYH" SQ Sequence 125 BP; >PHU46781_4 MEYQFTHSIHGVVAKCSMDHEAFARWLNAEITENPSQLAPIFAEIEKCRAAFPNHYECVF EGREYSLYFDYDEVMAKANNLDAAFDDEEMEEGFQFYNEESIAFCGLDDFEKFLKAYQHF VQTYH TREMBLNEW:PHU46781_3 ID PHU46781_3 standard; PRT; 195 AA. AC U46781; DR EMBL; U46781; PHU46781. DE Pasteurella haemolytica putative coproporphyrinogen III oxidase DE (hemN') gene, partial cds, leukotoxin transcriptional activator and DE restriction modification methylase subunit (alxA-hsdM), (hsdS) and DE (hsdR) genes, complete cds. OS Pasteurella haemolytica OC Eubacteria; Proteobacteria; gamma subdivision; Pasteurellaceae; OC Pasteurella. OG Mitochondrion FT CDS complement(918..1505) FT /note="orf2" FT /codon_start=1 FT /transl_table=11 FT /db_xref="PID:g1685095" FT /translation="MSRTKKTRRITDIMPARKTDKPKQPMPKLGGGKNRKLTRYELDAQ FT AREEKRKRKHKGLPTGSRNADPAEQKKAVVKEVKDPRIGSRKKVPLMVEFVNQPEKGRT FT IKAVPVEPIKPTLSPEQELEQLENNECLNQLLDDLEAGKTLSAEDQKFMNECLDRIDEL FT MTELGIEYEDEEGDNGDALLRQFETMDINKFR" SQ Sequence 195 BP; >PHU46781_3 MSRTKKTRRITDIMPARKTDKPKQPMPKLGGGKNRKLTRYELDAQAREEKRKRKHKGLPT GSRNADPAEQKKAVVKEVKDPRIGSRKKVPLMVEFVNQPEKGRTIKAVPVEPIKPTLSPE QELEQLENNECLNQLLDDLEAGKTLSAEDQKFMNECLDRIDELMTELGIEYEDEEGDNGD ALLRQFETMDINKFR TREMBLNEW:PHU46781_2 ID PHU46781_2 standard; PRT; 156 AA. AC U46781; DR EMBL; U46781; PHU46781. DE Pasteurella haemolytica putative coproporphyrinogen III oxidase DE (hemN') gene, partial cds, leukotoxin transcriptional activator and DE restriction modification methylase subunit (alxA-hsdM), (hsdS) and DE (hsdR) genes, complete cds. OS Pasteurella haemolytica OC Eubacteria; Proteobacteria; gamma subdivision; Pasteurellaceae; OC Pasteurella. OG Mitochondrion FT CDS complement(437..907) FT /note="orf3" FT /codon_start=1 FT /transl_table=11 FT /db_xref="PID:g1685094" FT /translation="MMLRIFLMVLAALILISLGGYALHLMLKVRAQKKHEQALIEQAKQ FT AQKDRYIRILDSIEVIARAMISEQCDFSEGVLRLKPLLDVLGRKLSDYTAMWALYGVVE FT NMPILDERKNLKRNERMKLDLEREAKEAELESDIKNECYQLLKDIEEMRKAI" SQ Sequence 156 BP; >PHU46781_2 MMLRIFLMVLAALILISLGGYALHLMLKVRAQKKHEQALIEQAKQAQKDRYIRILDSIEV IARAMISEQCDFSEGVLRLKPLLDVLGRKLSDYTAMWALYGVVENMPILDERKNLKRNER MKLDLEREAKEAELESDIKNECYQLLKDIEEMRKAI TREMBLNEW:PHU46781_1 ID PHU46781_1 standard; PRT; 146 AA. AC U46781; DR EMBL; U46781; PHU46781. DE gene: "hemN'"; product: "HEMN"; DE Pasteurella haemolytica putative coproporphyrinogen III oxidase DE (hemN') gene, partial cds, leukotoxin transcriptional activator and DE restriction modification methylase subunit (alxA-hsdM), (hsdS) and DE (hsdR) genes, complete cds. OS Pasteurella haemolytica OC Eubacteria; Proteobacteria; gamma subdivision; Pasteurellaceae; OC Pasteurella. OG Mitochondrion FT CDS complement(<1..439) FT /gene="hemN'" FT /note="putative coproporphyrinogen III oxidase" FT /codon_start=3 FT /product="HEMN" FT /transl_table=11 FT /db_xref="PID:g1685093" FT /translation="MSEIIWDLALIQKYNHSGPRYTSYPTALEFNENYTNEDFIRAAAR FT YPERPLSLYVHIPFCHKLCYFCGCNKVITRHRHKVEIYLDYLEREIKTRAPLFQNRLVT FT QIHWGRGTPTYLDEDQSARLMQMLRANFDVSDDAEISIEMDP" SQ Sequence 146 BP; >PHU46781_1 MSEIIWDLALIQKYNHSGPRYTSYPTALEFNENYTNEDFIRAAARYPERPLSLYVHIPFC HKLCYFCGCNKVITRHRHKVEIYLDYLEREIKTRAPLFQNRLVTQIHWGRGTPTYLDEDQ SARLMQMLRANFDVSDDAEISIEMDP