ENZYME:1.3.3.4 ID 1.3.3.4 DE PROTOPORPHYRINOGEN OXIDASE. CA PROTOPORPHYRINOGEN-IX + O(2) = PROTOPORPHYRIN-IX + H(2)O. CF FMN. CC -!- ALSO SLOWLY OXIDIZES MESOPHORPHYRINOGEN-IX. DI PORPHYRIA VARIEGATA; MIM:176200. DR P32397, HEMG_BACSU; P27863, HEMG_ECOLI; P50336, PPOX_HUMAN; DR P51175, PPOX_MOUSE; P40012, PPOX_YEAST; PIR:JC4971 >P1;JC4971 protoporphyrinogen oxidase (EC 1.3.3.4) - human C;Species: Homo sapiens (man) C;Date: 31-Dec-1996 #sequence_revision 31-Dec-1996 #text_change 31-Dec-1996 C;Accession: JC4971 R;Puy, H.; Robreau, A.M.; Rosipal, R.; Nordmann, Y.; Deybach, J.C. Biochem. Biophys. Res. Commun. 226, 226-230, 1996 A;Title: Protoporphyrinogen oxidase: Complete genomic sequence and polymorphisms in the human gene. A;Reference number: JC4971 A;Accession: JC4971 A;Status: nucleic acid sequence not shown A;Molecule type: mRNA A;Residues: 1-477 A;Cross-references: EMBL:X99450 C;Comment: This enzyme acts as the penultimate step in the heme biosynthetic pathway, and catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX within the inner mitochondrial membrane. C;Genetics: A;Gene: prox A;Map position: 1q23 A;Introns: 29/3; 74/3; 113/2; 157/3; 206/1; 269/3; 290/1; 329/3; 366/3;4 16/3; 431/1 C;Keywords: oxidoreductase >JC4971 MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRG IRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSP PFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSI RSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQAL ETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAA PLARALSAITAVSVAVVNLQYQGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSP PGLRVTVMLGGSWLQTLEASGCVLSQELFQQRAQEAAATQLGLKEMPSHCLVHLHKNCIP QYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLGTEPNS PIR:A56449 >P1;A56449 protoporphyrinogen oxidase (EC 1.3.3.4) - human C;Species: Homo sapiens (man) C;Date: 27-Oct-1995 #sequence_revision 27-Oct-1995 #text_change 02-Jul-1996 C;Accession: A56449; I38995 R;Nishimura, K.; Taketani, S.; Inokuchi, H. J. Biol. Chem. 270, 8076-8080, 1995 A;Title: Cloning of a human cDNA for protoporphyrinogen oxidase by complementation in Vivo of a hemG mutant of Escherichia coli. A;Reference number: A56449 A;Accession: A56449 A;Status: preliminary A;Molecule type: mRNA A;Residues: 1-477 A;Cross-references: GB:D38537 R;Dailey, T.A.; Meissner, P.; Dailey, H.A. J. Biol. Chem. 269, 813-815, 1994 A;Title: Expression of a cloned protoporphyrinogen oxidase. A;Reference number: A49858; MUID:94117488 A;Accession: I38995 A;Status: preliminary; translated from GB/EMBL/DDBJ A;Molecule type: mRNA A;Residues: 1-477 A;Cross-references: EMBL:U26446; NID:g837327; CDS_PID:g837328 C;Keywords: oxidoreductase >A56449 MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRG IRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSP PFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSI RSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQAL ETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAA PLARALSAITAVSVAVVNLQYQGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSP PGLRVTVMLGGSWLQTLEASGCVLSQELFQQRAQEAAATQLGLKEMPSHCLVHLHKNCIP QYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLGTEPNS PIR:PC2364 >F1;PC2364 protoporphyrinogen oxidase (EC 1.3.3.4) - common tobacco (fragment) C;Species: Nicotiana tabacum (common tobacco) C;Date: 22-Apr-1995 #sequence_revision 26-May-1995 #text_change 26-May-1995 C;Accession: PC2364 R;Yamato, S.; Ida, T.; Katagiri, M.; Ohkawa, H. Biosci. Biotechnol. Biochem. 59, 558-559, 1995 A;Title: A tobacco soluble protoporphyrinogen-oxidizing enzyme similar to plant peroxidases in their amino acid sequences and immunochemical reactivity. A;Reference number: PC2364 A;Accession: PC2364 A;Molecule type: protein A;Residues: 1-29 C;Comment: This enzyme catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX in the biosynthetic pathway of heme and chlorophyll in plant cells. C;Keywords: oxidoreductase >PC2364 GASLIRLHFHDCFVDGVALAGAHTVGFTR PIR:F64228 >P1;F64228 protoporphyrinogen oxidase (EC 1.3.3.4) - Mycoplasma genitalium (SGC3) C;Species: Mycoplasma genitalium C;Date: 17-Nov-1995 #sequence_revision 17-Nov-1995 #text_change 17-Nov-1995 C;Accession: F64228 R;Fraser, C.M.; Gocayne, J.D.; White, O.; Adams, M.D.; Clayton, R.A.; Fleischmann, R.D.; Bult, C.J.; Kerlavage, A.R.; Sutton, G.; Kelley, J.M.; Fritchman, J.L.; Weidman, J.F.; Small, K.V.; Sandusky, M.; Fuhrmann, J.; Nguyen, D.; Utterback, T.R.; Saudek, D.M.; Phillips, C.A.; Merrick, J.M.; Tomb, J.F.; Dougherty, B.A.; Bott, K.F.; Hu, P.C.; Lucier, T.S.; Peterson, S.N.; Smith, H.O.; Hutchison III, C.A.; Venter, J.C. Science 270, 397-403, 1995 A;Title: The minimal gene complement of Mycoplasma genitalium. A;Reference number: A64200 A;Accession: F64228 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-456 A;Cross-references: GB:L43967; TIGR:MG259 A;Experimental source: strain G-37 A;Note: neither nucleotide sequence nor conceptual translation is shown C;Genetics: A;Genetic code: SGC3 C;Keywords: oxidoreductase >F64228 MTLYEFFLNQKLVYQSSPHFNGVFLTILEHYGFQFKTIDKLWKSKLLITSELTDKIKQQL KCYFIEKIPLPYLLGTIQLRKLTFKTKKGVFIPRIDSLALIASVNLKKIKTALDLCCGSG TLAIALKKKCDTLDVYGSDIDIQALKLAQQNALINNVSINWIEADWFDCFNKIKTPIDLI VTNPPYLKKTQLNKTLNYEPKHSLVFQNKNSYFAYKQLFNLLLTKRSIKQLIFECSLFQK ERLLNLFSIFKSRPIFNFQKQFIGMKVDNQKLPVVDIKNTKTIKQLLKMGLAGIVNTDTQ MGLISYSESTLDKIKQRALNKHYVSMFGLEELKKLPKKLQQIASYFWPGSYTFIKNNKSY RVPKNLGLLNLFNAIGRVFCTSANISNQKPYTKLSDYQNDSYWIKQPCFIIRSTSKVQSN NTPSLVYNLDTKQLVRTTAKQTKQFHKLITKHQLAI 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:H64129 >P1;H64129 protoporphyrinogen oxidase (hemK) homolog - Haemophilus influenzae (strain Rd KW20) C;Species: Haemophilus influenzae C;Date: 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 10-May-1996 C;Accession: H64129 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: H64129 A;Status: preliminary; nucleic acid sequence not shown; translation not shown A;Molecule type: DNA A;Residues: 1-292 A;Cross-references: GB:L42023; TIGR:HI1559 A;Note: named as homolog to a protein from Escherichia coli >H64129 MNYKEWLAQAIADLAKKNPTENSKIDALVLLQHATGKSRTQILAFDDTEIDEKVRLKLTA LLDRRLKGEPIAYILGEKEFWSLPLNVSKGTLIPRPDTEILVEKALQIALEKLEENPPHF RILDLGTGTGAIALALASELAPICQKRHIPLEIIGVDLMSDVVALAQSNAERNQLNVEFL QSRWFDNITGKFDLIVSNPPYIDAQDEHLHQGDVRFEPLSALVANDEGYADLRHIIELAS SYLNSNGVLLLEHGWQQGEKVRSIFQENHWEMVETVRDYSDNERVTLGFWKK PIR:F64189 >P1;F64189 protoporphyrinogen oxidase (hemK) homolog - Haemophilus influenzae (strain Rd KW20) C;Species: Haemophilus influenzae C;Date: 18-Aug-1995 #sequence_revision 18-Aug-1995 #text_change 10-May-1996 C;Accession: F64189 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: F64189 A;Status: preliminary; nucleic acid sequence not shown; translation not shown A;Molecule type: DNA A;Residues: 1-314 A;Cross-references: GB:L42023; TIGR:HI1201 A;Note: named as homolog to a protein from Escherichia coli >F64189 METSHNQELVATILEDNVANELQTIQDFLRWTYSILNRSDIYFGQGHDNPWDESLQLVLS SLHLPIDLPTELFNSRLTPSEKETLVQLVLTRIEQRVPVAYLTNSAWFCGHEFYVDERTI IPRSPISALIQDRFEDLISQEPNHILDLCTGSGCIAIACAYAFPNAEVDAVDLSVDALNV AEINISRHQLEHRVFPIQSNLFENILGQKYDLIVTNPPYVDEEDLADMPEEFHFEPELAL GSGSDGLNITKQILKQAPDYLTENGVLVCEVGNSMISLIEQYPDVPFEWVELKNGGLGVF AIQRKDLVKYHDLF PIR:C64080 >P1;C64080 protoporphyrinogen oxidase (hemG) homolog (hemY) 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: C64080 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: C64080 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-428 A;Cross-references: GB:L42023; TIGR:HI0602 A;Note: named as homolog to a protein from Escherichia coli >C64080 MFRVLFLMLTLLVGLVAGPYISGQQGYVRIETANRIIEMSITTLVIFFIISLAIIYAFEW GVTRFFRLSRSSYQWFSNRKRVKAQKQTLEGLVKMDEGDYAKAEKLIGKNAKHSAEPVLN LIKAAEAAQQRGDEFSANRYLIEATELAGSDNLLVEIARTRILLQQNKLPAARSSVDSLL EMARRNKEVLKLAVEIYLRSKAYQALDKILDNVANSGLFNDEEFKDLRSKTENGLLDEKM NEEGIDGLLTWWNQQPRHRRNNIELKISLIQRLIDCNDHESATELTFEILKKLGDNTAIS LPLCTQITRLQPEDNSKLLKLIEKRAKRVDEKQKCCINRALGYLYVRNNEFIKAADVFKN VIACPEQLEQNDLMMASYVFEQAGDKALAEQVRQESLKSVMAIQDVIPESAEEKTEENST ALLESKSE PIR:S30740 >P1;S30740 trkH protein - Escherichia coli C;Species: Escherichia coli C;Date: 02-Dec-1993 #sequence_revision 01-Sep-1995 #text_change 01-Mar-1996 C;Accession: S30740; PC2366 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: S30740 A;Status: preliminary; nucleic acid sequence not shown; translation not shown A;Molecule type: DNA A;Residues: 1-431 A;Cross-references: EMBL:M87049 A;Note: the nucleotide sequence was submitted to the EMBL Data Library, November 1992 R;Nishimura, K.; Nakayashiki, T.; Inokuchi, H. DNA Res. 2, 1-8, 1995 A;Title: Cloning and identification of the hemG gene encoding protoporphyrinogen oxidase (PPO) of Escherichia coli K-12. A;Reference number: JC2513 A;Accession: PC2366 A;Molecule type: DNA A;Residues: 361-431 A;Experimental source: strain VSR751 C;Genetics: A;Gene: trkH A;Map position: 86 min >S30740 MHFRAITRIVGLLVILFSGTMIIPGLVALIYRDGAGRAFTQTFFVALAIGSMLWWPNRKE KGELKSREFLIVVLFWTVLGSVGALPFIFSESPNLTITDAFFESFSGLTTTGATTLVGLD SLPHAILFYRQMLQWFGGMGIIVLAVAILPILGVGGMQLYRAEMPGPLKDNKMRPRIAET AKTLWLIYVLLTVACALALWFAGMDAFDAIGHSFATIAIGGFSTHDASIGYFDSPTINTI IAIFLLISGCNYGLHFSLLSGRSLKVYWRDPEFRMFIGVQFTLVVICTLVLWFHNVYSSA LMTINQAFFQVVSMATTAGFTTDSIARWPLFLPVLLLCSAFIGGCAGSTGGGLKVIRILL LFKQGNRELKRLVHPNAVYSIKLGNRALPERILEAVWGFFSAYALVFIVSMLAIIARAWM TFLPLRRLLRH PIR:I83570 >P1;I83570 protoporphyrinogen oxidase (EC 1.3.3.4) hemK - Escherichia coli C;Species: Escherichia coli C;Date: 07-Jun-1996 #sequence_revision 07-Jun-1996 #text_change 31-Dec-1996 C;Accession: I83570 R;Strohmaier, H.; Remler, P.; Renner, W.; Hogenauer, G. J. Bacteriol. 177, 4488-4500, 1995 A;Title: Expression of genes kdsA and kdsB involved in 3-deoxy-D-manno-octulosonic acid metabolism and biosynthesis of enterobacterial lipopolysaccharide is growth phase regulated primarily at the transcriptional level in Escherichia coli K-12. A;Reference number: I60364; MUID:95362678 A;Accession: I83570 A;Status: preliminary; translated from GB/EMBL/DDBJ A;Molecule type: DNA A;Residues: 1-277 A;Cross-references: EMBL:U18555; NID:g968925; CDS_PID:g968931 C;Keywords: oxidoreductase >I83570 MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLT RRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQALARLPEQPCRILDLGTGT GAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALAGQQFAMI VSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEHGW QQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ PIR:I65968 >P1;I65968 protoporphyrinogen oxidase (EC 1.3.3.4) hemK - Escherichia coli C;Species: Escherichia coli C;Date: 07-Jun-1996 #sequence_revision 07-Jun-1996 #text_change 31-Dec-1996 C;Accession: I65968 R;Nakayashiki, T.; Nishimura, K.; Inokuchi, H. DNA 153, 67-70, 1995 A;Title: Cloning and sequencing of a previously unidentified gene that is involved in the biosynthesis of heme in Escherichia coli. A;Reference number: I52973 A;Accession: I65968 A;Status: preliminary; translated from GB/EMBL/DDBJ A;Molecule type: DNA A;Residues: 1-225 A;Cross-references: GB:D28567; NID:g466531; CDS_PID:g466533 C;Keywords: oxidoreductase >I65968 MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLT RRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQALARLPEQPCRILDLGTGT GAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALAGQQFAMI VSNPPYIDEQDPHLQQGDVRFEPRHCAGCGRQWNGRHRAYHRTVA PIR:JC2513 >P1;JC2513 protoporphyrinogen oxidase (EC 1.3.3.4) - Escherichia coli C;Species: Escherichia coli C;Date: 13-Jun-1995 #sequence_revision 14-Jul-1995 #text_change 19-Oct-1995 C;Accession: JC2513; S41629 R;Nishimura, K.; Nakayashiki, T.; Inokuchi, H. DNA Res. 2, 1-8, 1995 A;Title: Cloning and identification of the hemG gene encoding protoporphyrinogen oxidase (PPO) of Escherichia coli K-12. A;Reference number: JC2513 A;Accession: JC2513 A;Molecule type: DNA A;Residues: 1-181 A;Experimental source: strain VSR751 R;Sasarman, A.; Letowski, J.; Czaika, G.; Ramirez, V.; Nead, M.A.; Jacobs, J.M.; Morais, R. Can. J. Microbiol. 39, 1155-1161, 1993 A;Title: Nucleotide sequence of the hemG gene involved in the protoporphyrinogen oxidase activity of Escherichia coli K12. A;Reference number: S41629 A;Accession: S41629 A;Status: preliminary A;Molecule type: DNA A;Residues: 1-181 A;Cross-references: EMBL:X68660 C;Comment: This enzyme catalyzes the oxidation of protoporphyrinogen IX into protoporphyrin IX. C;Genetics: A;Gene: hemG A;Map position: 86 min A;Start codon: GTG C;Keywords: FMN; oxidoreductase F;5-21/Region: flavodoxin motif >JC2513 MKTLILFSTRDGQTREIASYLASELKELGIQADVANVHRIEEPQWENYDRVVIGASIRYG HYHSAFQEFVKKHATRLNSMPSAFYSVNLVARKPEKRTPQTNSYARKFLMNSQWRPDRCA VIAGALRYPRYRWYDRFMIKLIMKMSGGETDTRKEVVYTDWEQVANFAREIAHLTDKPTL K SWISSNEW:HEMG_BACSU ID HEMG_BACSU STANDARD; PRT; 470 AA. AC P32397; DT 01-OCT-1993 (REL. 27, CREATED) DT 01-OCT-1993 (REL. 27, LAST SEQUENCE UPDATE) DT 01-JUN-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.4) (PPO). GN HEMG OR HEMY. OS BACILLUS SUBTILIS. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 93094140. RA HANSSON M., HEDERSTEDT L.; RL J. BACTERIOL. 174:8081-8093(1992). RN [2] RP CHARACTERIZATION. RX MEDLINE; 94117488. RA DAILEY T.A., MEISSNER P., DAILEY H.A.; RL J. BIOL. CHEM. 269:813-815(1994). CC -!- FUNCTION: CATALYZES THE 6-ELECTRON OXIDATION OF PROTOPORPHYRINOGEN CC IX TO FORM PROTOPORPHYRIN IX. CC -!- CATALYTIC ACTIVITY: PROTOPORPHYRINOGEN-IX + O(2) = PROTOPORPHYRIN- CC IX + H(2)O. CC -!- PATHWAY: PENULTIMATE STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- COFACTOR: FMN FLAVOPROTEIN (POTENTIAL). CC -!- SIMILARITY: TO HUMAN PPO AND TO S.POMBE SPAC1F5.07C AND YEAST CC YER014W. DR EMBL; M97208; G143045; -. DR PIR; D47045; D47045. DR SUBTILIST; BG10431; HEMG. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; FLAVOPROTEIN; FMN. SQ SEQUENCE 470 AA; 51203 MW; E87BF0C9 CRC32; >HEMG_BACSU MSDGKKHVVIIGGGITGLAAAFYMEKEIKEKNLPLELTLVEASPRVGGKIQTVKKDGYII ERGPDSFLERKKSAPQLVKDLGLEHLLVNNATGQSYVLVNRTLHPMPKGAVMGIPTKIAP FVSTGLFSLSGKARAAMDFILPASKTKDDQSLGEFFRRRVGDEVVENLIEPLLSGIYAGD IDKLSLMSTFPQFYQTEQKHRSLILGMKKTRPQGSGQQLTAKKQGQFQTLSTGLQTLVEE IEKQLKLTKVYKGTKVTKLSHSGSCYSLELDNGVTLDADSVIVTAPHKAAAGMLSELPAI SHLKNMHSTSVANVALGFPEGSVQMEHEGTGFVISRNSDFAITACTWTNKKWPHAAPEGK TLLRAYVGKAGDESIVDLSDNDIINIVLEDLKKVMNINGEPEMTCVTRWHESMPQYHVGH KQRIKELREALASAYPGVYMTGASFEGVGIPDCIDQGKAAVSDALTYLFS SWISSNEW:HEMG_ECOLI ID HEMG_ECOLI STANDARD; PRT; 181 AA. AC P27863; DT 01-AUG-1992 (REL. 23, CREATED) DT 01-AUG-1992 (REL. 23, LAST SEQUENCE UPDATE) DT 01-JUN-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.4) (PPO). GN HEMG. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] 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 [2] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 91057145. RA NAKAHIGASHI K., INOKUCHI H.; RL NUCLEIC ACIDS RES. 18:6439-6439(1990). RN [3] RP SEQUENCE FROM N.A., SEQUENCE OF 1-18, AND CHARACTERIZATION. RC STRAIN=K12; RX MEDLINE; 94177529. RA SASARMAN A., LETOWSKI J., CZAIKA G., RAMIREZ V., NEAD M.A., RA JACOBS J.M., MORAIS R.; RL CAN. J. MICROBIOL. 39:1155-1161(1993). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 95308321. RA NISHIMURA K., NAKAHIGASHI K., INOKUCHI H.; RL DNA RES. 2:1-8(1995). CC -!- FUNCTION: CATALYZES THE 6-ELECTRON OXIDATION OF PROTOPORPHYRINOGEN CC IX TO FORM PROTOPORPHYRIN IX. CC -!- CATALYTIC ACTIVITY: PROTOPORPHYRINOGEN-IX + O(2) = PROTOPORPHYRIN- CC IX + H(2)O. CC -!- PATHWAY: PENULTIMATE STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- COFACTOR: FMN FLAVOPROTEIN (POTENTIAL). CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC FRAMESHIFTS. DR EMBL; M87049; G148250; ALT_SEQ. DR EMBL; X54687; -; NOT_ANNOTATED_CDS. DR EMBL; X68660; G581103; -. DR PIR; S30741; S30741. DR PIR; S41629; S41629. DR ECOGENE; EG11485; HEMG. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; FLAVOPROTEIN; FMN. SQ SEQUENCE 181 AA; 21226 MW; FF3382BD CRC32; >HEMG_ECOLI MKTLILFSTRDGQTREIASYLASELKELGIQADVANVHRIEEPQWENYDRVVIGASIRYG HYHSAFQEFVKKHATRLNSMPSAFYSVNLVARKPEKRTPQTNSYARKFLMNSQWRPDRCA VIAGALRYPRYRWYDRFMIKLIMKMSGGETDTRKEVVYTDWEQVANFAREIAHLTDKPTL K SWISSNEW:PPOX_HUMAN ID PPOX_HUMAN STANDARD; PRT; 477 AA. AC P50336; DT 01-JUN-1996 (REL. 34, CREATED) DT 01-JUN-1996 (REL. 34, LAST SEQUENCE UPDATE) DT 01-JUN-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.4) (PPO). GN PPOX. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RX MEDLINE; 95229621. RA NISHIMURA K., TAKETANI S., INOKUCHI H.; RL J. BIOL. CHEM. 270:8076-8080(1995). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA DAILEY T.A., DAILEY H.A.; RL SUBMITTED (MAY-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: CATALYZES THE 6-ELECTRON OXIDATION OF PROTOPORPHYRINOGEN CC IX TO FORM PROTOPORPHYRIN IX. CC -!- CATALYTIC ACTIVITY: PROTOPORPHYRINOGEN-IX + O(2) = PROTOPORPHYRIN- CC IX + H(2)O. CC -!- PATHWAY: PENULTIMATE STEP IN HEME AND PORPHYRIN BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: MITOCHONDRION INNER MEMBRANE. CC -!- COFACTOR: FMN FLAVOPROTEIN (POTENTIAL). CC -!- DISEASE: DEFECTS IN PPOX ARE THE CAUSE OF PORPHYRIA VARIEGATA CC (VP), A DISEASE CHARACTERIZED BY SKIN HYPERPIGMENTATION AND HAIR CC HYPERTRICHOSIS, ASSOCIATED WITH ACUTE ATTACKS, LIKE THOSE OF ACUTE CC INTERMITTENT PORPHYRIA. CC -!- SIMILARITY: TO B.SUBTILIS PPO AND TO S.POMBE SPAC1F5.07C AND YEAST CC YER014W. DR EMBL; D38537; G854664; -. DR EMBL; U26446; G837328; -. DR MIM; 600923; 11TH EDITION. DR MIM; 176200; 11TH EDITION. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; OXIDOREDUCTASE; KW FLAVOPROTEIN; FMN; MITOCHONDRION. SQ SEQUENCE 477 AA; 50765 MW; DC0FFEA8 CRC32; >PPOX_HUMAN MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRG IRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSP PFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSI RSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQAL ETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAA PLARALSAITAVSVAVVNLQYQGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSP PGLRVTVMLGGSWLQTLEASGCVLSQELFQQRAQEAAATQLGLKEMPSHCLVHLHKNCIP QYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLGTEPNS SWISSPROT:PPOX_YEAST ID PPOX_YEAST STANDARD; PRT; 539 AA. AC P40012; DT 01-FEB-1995 (REL. 31, CREATED) DT 01-FEB-1995 (REL. 31, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.4) (PPO). GN HEM14 OR YER014W. OS SACCHAROMYCES CEREVISIAE (BAKER'S YEAST). OC EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RA DIETRICH F.S., MULLIGAN J.T., HENNESSEY K.M., ALLEN E., ARAUJO R., RA AVILES E., BERNO A., BRENNAN T., CARPENTER J., CHEN E., CHERRY J.M., RA CHUNG E., DUNCAN M., GUZMAN E., HARTZELL G., HUNICKE-SMITH S., RA HYMAN R., KAYSER A., KOMP C., LASHKARI D., LEW H., LIN D., RA MOSEDALE D., NAKAHARA K., NAMATH A., NORGREN R., OEFNER P., OH C., RA PETEL F.X., ROBERTS D., SEHL P., SCHRAMM S., SHOGREN T., SMITH V., RA TAYLOR P., WEI Y., YELTON M., BOTSTEIN D., DAVIS R.W.; RL SUBMITTED (DEC-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [2] RP IDENTIFICATION. RA CAMADRO J.M., LABBE P.; RL UNPUBLISHED RESULTS, CITED BY: RL DEYBACH J.-C., PUY H., ROBREAU A.-M., LAMORIL J., DA SILVA V., RL GRANDCHAMP B., NORDMANN Y.; RL HUM. MOL. GENET. 5:407-410(1996). CC -!- FUNCTION: CATALYZES THE 6-ELECTRON OXIDATION OF PROTOPORPHYRINOGEN CC IX TO FORM PROTOPORPHYRIN IX. CC -!- CATALYTIC ACTIVITY: PROTOPORPHYRINOGEN-IX + O(2) = PROTOPORPHYRIN- CC IX + H(2)O. CC -!- PATHWAY: PENULTIMATE STEP IN HEME AND PORPHYRIN BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: MITOCHONDRION INNER MEMBRANE (POTENTIAL). CC -!- COFACTOR: FMN FLAVOPROTEIN (POTENTIAL). CC -!- SIMILARITY: OTHER SPECIES PROTOPORPHYRINOGEN OXIDASE. DR EMBL; U18778; G603606; -. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; OXIDOREDUCTASE; KW FLAVOPROTEIN; FMN; MITOCHONDRION. SQ SEQUENCE 539 AA; 59703 MW; CC6D1B01 CRC32; >PPOX_YEAST MLLPLTKLKPRAKVAVVGGGVSGLCFTYFLSKLRPDVEITLFESQNRTGGWIYSCNTRDM SGNPIMLEKGPRTLRGVSDGTVLIMDTLKDLGKEAVIQSIDKGCIADKKFLLDPSDKLVQ VPNSISTTVKFLLNPLGKGLITGMMGEWFRKKSPHPGQDESVESICDRRFGNNYISNNMI SALLRGIYGDDVSLLSAKRTFKKIYYNELKHGSNTQAMIDNMRGKSRSKKTENLHQSLTG CLNDYSNAFGKDRSKLLDLSNTLKKYPMLGLAGGLETFPKIVRNALNEFKNVKIVTGNPV TQIMKRPANETTIGLKAKSGDQYETFDHLRLTITPPKIAKLLPKDQNSLSKLLDEIQSNT IILVNYYLPNKDVIDADLQGFGYLVPKSNKNPGKLLGVIFDSVIERNFKPLFDKLSTNPN ALNKYTKVTAMIGGCMLNEHGVPVVPSREVTINAVKDALNNHLGISNKDLEAGQWEFTIA DRCLPRFHVGYDAWQERAERKLQESYGQTVSVGGMGFSRSPGVPDVIVDGFNDALQLSK SWISSPROT:PPOX_MOUSE ID PPOX_MOUSE STANDARD; PRT; 477 AA. AC P51175; 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 PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.4) (PPO). GN PPOX. OS MUS MUSCULUS (MOUSE). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; RODENTIA. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 96132666. RA DAILEY T.A., DAILEY H.A., MEISSNER P., PRASAD A.R.; RL ARCH. BIOCHEM. BIOPHYS. 324:379-384(1995). CC -!- FUNCTION: CATALYZES THE 6-ELECTRON OXIDATION OF PROTOPORPHYRINOGEN CC IX TO FORM PROTOPORPHYRIN IX. CC -!- CATALYTIC ACTIVITY: PROTOPORPHYRINOGEN-IX + O(2) = PROTOPORPHYRIN- CC IX + H(2)O. CC -!- PATHWAY: PENULTIMATE STEP IN HEME AND PORPHYRIN BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: MITOCHONDRION INNER MEMBRANE. CC -!- COFACTOR: FMN FLAVOPROTEIN (POTENTIAL). CC -!- SIMILARITY: OTHER SPECIES PROTOPORPHYRINOGEN OXIDASE. DR EMBL; U25114; G793940; -. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; OXIDOREDUCTASE; KW FLAVOPROTEIN; FMN; MITOCHONDRION. SQ SEQUENCE 477 AA; 50870 MW; 120769A6 CRC32; >PPOX_MOUSE MGRTVIVLGGGISGLAASYHLIRGPSPPKVILVEGSKRLGGWIRSIRGSDGAIFELGPRG IRPAGALGARTLLLVSELGLESEVLPVRGDHPAAQNRFLYVGGTLHPLPSGLRGLLRPSP PFSKPLFWAGLRELLKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSI RSCFPSLFQAEQTHRSILLGLLLGAGQSPQPDSSLIRQARAERWSQWSLRGGLEVLPQAL HNHLASKGVTVLSGQPVCGLSLQPEGRWKVSLGDSSLEADHIISAIPASELSKLLPAEAA PLARILSTIKAVSVAVVNLQYRGACLPVQGFGHLVPSSEDPTVLGIVYDSVAFPEQDGNP PSLRVTVMLGGYWLQKLKAAGHQLSPELFQQQAQEAAATQLGLKEPPSHCLVHLHKNCIP QYTIGHWQKLDSAMQFLTAQRLPLTLAGASYEGVAVNDCIESGRQAAVAVLGTESNS SWISSPROT:PPOX_HUMAN ID PPOX_HUMAN STANDARD; PRT; 477 AA. AC P50336; 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 PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.4) (PPO). GN PPOX. OS HOMO SAPIENS (HUMAN). OC EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA; OC EUTHERIA; PRIMATES. RN [1] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RX MEDLINE; 95229621. RA NISHIMURA K., TAKETANI S., INOKUCHI H.; RL J. BIOL. CHEM. 270:8076-8080(1995). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=PLACENTA; RA DAILEY T.A., DAILEY H.A.; RL SUBMITTED (MAY-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [3] RP VARIANT VP ARG-232, AND VARIANT HIS-304. RA DEYBACH J.-C., PUY H., ROBREAU A.-M., LAMORIL J., DA SILVA V., RA GRANDCHAMP B., NORDMANN Y.; RL HUM. MOL. GENET. 5:407-410(1996). RN [4] RP VARIANT VP TRP-59. RX MEDLINE; 96241580. RA MEISSNER P.N., DAILEY T.A., HIFT R.J., ZIMAN M., CORRIGALL A.V., RA ROBERTS A.G., MEISSNER D.M., KIRSCH R.E., DAILEY H.A.; RL NAT. GENET. 13:95-97(1996). CC -!- FUNCTION: CATALYZES THE 6-ELECTRON OXIDATION OF PROTOPORPHYRINOGEN CC IX TO FORM PROTOPORPHYRIN IX. CC -!- CATALYTIC ACTIVITY: PROTOPORPHYRINOGEN-IX + O(2) = PROTOPORPHYRIN- CC IX + H(2)O. CC -!- PATHWAY: PENULTIMATE STEP IN HEME AND PORPHYRIN BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: MITOCHONDRION INNER MEMBRANE. CC -!- COFACTOR: FMN FLAVOPROTEIN (POTENTIAL). CC -!- DISEASE: DEFECTS IN PPOX ARE THE CAUSE OF PORPHYRIA VARIEGATA CC (VP), A DISEASE CHARACTERIZED BY SKIN HYPERPIGMENTATION AND HAIR CC HYPERTRICHOSIS, ASSOCIATED WITH ACUTE ATTACKS, LIKE THOSE OF ACUTE CC INTERMITTENT PORPHYRIA. CC -!- SIMILARITY: OTHER SPECIES PROTOPORPHYRINOGEN OXIDASE. DR EMBL; D38537; G854664; -. DR EMBL; U26446; G837328; -. DR MIM; 600923; -. DR MIM; 176200; -. KW PORPHYRIN BIOSYNTHESIS; HEME BIOSYNTHESIS; OXIDOREDUCTASE; KW FLAVOPROTEIN; FMN; MITOCHONDRION; DISEASE MUTATION; POLYMORPHISM. FT VARIANT 59 59 R -> W (IN VP). FT VARIANT 232 232 G -> R (IN VP). FT VARIANT 304 304 R -> H. SQ SEQUENCE 477 AA; 50765 MW; DC0FFEA8 CRC32; >PPOX_HUMAN MGRTVVVLGGGISGLAASYHLSRAPCPPKVVLVESSERLGGWIRSVRGPNGAIFELGPRG IRPAGALGARTLLLVSELGLDSEVLPVRGDHPAAQNRFLYVGGALHALPTGLRGLLRPSP PFSKPLFWAGLRELTKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSI RSCFPSLFQAEQTHRSILLGLLLGAGRTPQPDSALIRQALAERWSQWSLRGGLEMLPQAL ETHLTSRGVSVLRGQPVCGLSLQAEGRWKVSLRDSSLEADHVISAIPASVLSELLPAEAA PLARALSAITAVSVAVVNLQYQGAHLPVQGFGHLVPSSEDPGVLGIVYDSVAFPEQDGSP PGLRVTVMLGGSWLQTLEASGCVLSQELFQQRAQEAAATQLGLKEMPSHCLVHLHKNCIP QYTLGHWQKLESARQFLTAHRLPLTLAGASYEGVAVNDCIESGRQAAVSVLGTEPNS SWISSPROT:HEMK_SALTY ID HEMK_SALTY STANDARD; PRT; 77 AA. AC P40816; DT 01-FEB-1995 (REL. 31, CREATED) DT 01-FEB-1995 (REL. 31, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE POSSIBLE PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.-) (FRAGMENT). GN HEMK. OS SALMONELLA TYPHIMURIUM. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 89291746. RA ELLIOTT T.; RL J. BACTERIOL. 171:3948-3960(1989). CC -!- FUNCTION: COULD BE INVOLVED IN THE OXIDATION OF PROTOPORPHYRINOGEN CC INTO PROTOPORPHYRIN IX. CC -!- PATHWAY: INVOLVED IN PORPHYRIN BIOSYNTHESIS. DR EMBL; J04243; G1196945; -. DR PIR; C32890; C32890. DR STYGENE; SG10534; HEMK. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE. FT NON_TER 77 77 SQ SEQUENCE 77 AA; 9006 MW; 7C896CB6 CRC32; >HEMK_SALTY MDFQHWLHEAVNQLRDSDSPRRDAEILLEYVTGKGRTYIMAFGETPLTDVQQQQLADLLQ RRKQGEPIAYLTGLREF SWISSPROT:HEMK_MYCTU ID HEMK_MYCTU STANDARD; PRT; 325 AA. AC Q10602; 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 POSSIBLE PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.-). GN HEMK OR MTCY373.20. OS MYCOBACTERIUM TUBERCULOSIS. OC PROKARYOTA; FIRMICUTES; ACTINOMYCETALES; MYCOBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=H37RV; RA OLIVER K., HARRIS D., BARRELL B.G., RAJANDREAM M.A., WALSH S.V.; RL SUBMITTED (MAY-1996) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: COULD BE INVOLVED IN THE OXIDATION OF PROTOPORPHYRINOGEN CC INTO PROTOPORPHYRIN IX (BY SIMILARITY). CC -!- PATHWAY: INVOLVED IN PORPHYRIN BIOSYNTHESIS. DR EMBL; Z73419; E243644; -. KW HYPOTHETICAL PROTEIN; PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE. SQ SEQUENCE 325 AA; 34589 MW; 67EA11DB CRC32; >HEMK_MYCTU MTSAPATMRWGNLPLAGESGTMTLRQAIDLAAALLAEAGVDSARCDAEQLAAHLAGTDRG RLPLFEPPGDEFFGRYRDIVTARARRVPLQHLIGTVSFGPVVLHVGPGVFVPRPETEAIL AWATAQSLPARPLIVDACTGSGALAVALAQHRANLGLKARIIGIDDSDCALDYARRNAAG TPVELVRADVTTPRLLPELDGQVDLMVSNPPYIPDAAVLEPEVAQHDPHHALFGGPDGMT VISAVVGLAGRWLRPGGLFAVEHDDTTSSSTVDLVSSTKLFVDVQARKDLAGRPRFVTAM RWGHLPLAGENGAIDPRQRRCRAKR SWISSPROT:HEMK_MYCLE ID HEMK_MYCLE STANDARD; PRT; 191 AA. AC P45832; 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 POSSIBLE PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.-). GN HEMK. OS MYCOBACTERIUM LEPRAE. OC PROKARYOTA; FIRMICUTES; ACTINOMYCETALES; MYCOBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RA SMITH D.R., ROBISON K.; RL SUBMITTED (SEP-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: COULD BE INVOLVED IN THE OXIDATION OF PROTOPORPHYRINOGEN CC INTO PROTOPORPHYRIN IX (BY SIMILARITY). CC -!- PATHWAY: INVOLVED IN PORPHYRIN BIOSYNTHESIS. DR EMBL; U15186; G699335; -. KW HYPOTHETICAL PROTEIN; PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE. SQ SEQUENCE 191 AA; 20497 MW; 716929F7 CRC32; >HEMK_MYCLE MMIRLRRAIDSAVTQLEEAGIGSARCDAEQLAAHLAGTDRGRLALLDTPGEEFFRRYSDA VAARSRRVPLQHLIGTVSFGPVVLHVGPDVFIPRPETEAILAWVMAQRLPERPVIVDACT GSGALAVALAHHRPAARVIGIDDSDSALDYARRNAEGTAVECVRADVTTPALLPELDGCV DLFVAQPTLRS SWISSPROT:HEMK_HAEIN ID HEMK_HAEIN STANDARD; PRT; 292 AA. AC P45253; 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 POSSIBLE PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.-). GN HEMK OR HI1559. OS HAEMOPHILUS INFLUENZAE. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC PASTEURELLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=RD / KW20; RX MEDLINE; 95350630. RA FLEISCHMANN R.D., ADAMS M.D., WHITE O., CLAYTON R.A., KIRKNESS E.F., RA KERLAVAGE A.R., BULT C.J., TOMB J.-F., DOUGHERTY B.A., MERRICK J.M., RA MCKENNEY K., SUTTON G., FITZHUGH W., FIELDS C.A., GOCAYNE J.D., RA SCOTT J.D., SHIRLEY R., LIU L.-I., GLODEK A., KELLEY J.M., RA WEIDMAN J.F., PHILLIPS C.A., SPRIGGS T., HEDBLOM E., COTTON M.D., RA UTTERBACK T.R., HANNA M.C., NGUYEN D.T., SAUDEK D.M., BRANDON R.C., RA FINE L.D., FRITCHMAN J.L., FUHRMANN J.L., GEOGHAGEN N.S.M., RA GNEHM C.L., MCDONALD L.A., SMALL K.V., FRASER C.M., SMITH H.O., RA VENTER J.C.; RL SCIENCE 269:496-512(1995). CC -!- FUNCTION: COULD BE INVOLVED IN THE OXIDATION OF PROTOPORPHYRINOGEN CC INTO PROTOPORPHYRIN IX (BY SIMILARITY). CC -!- PATHWAY: INVOLVED IN PORPHYRIN BIOSYNTHESIS. DR EMBL; L46190; G1007773; -. DR EMBL; U32830; G926640; -. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE. SQ SEQUENCE 292 AA; 33054 MW; 49344C09 CRC32; >HEMK_HAEIN MNYKEWLAQAIADLAKKNPTENSKIDALVLLQHATGKSRTQILAFDDTEIDEKVRLKLTA LLDRRLKGEPIAYILGEKEFWSLPLNVSKGTLIPRPDTEILVEKALQIALEKLEENPPHF RILDLGTGTGAIALALASELAPICQKRHIPLEIIGVDLMSDVVALAQSNAERNQLNVEFL QSRWFDNITGKFDLIVSNPPYIDAQDEHLHQGDVRFEPLSALVANDEGYADLRHIIELAS SYLNSNGVLLLEHGWQQGEKVRSIFQENHWEMVETVRDYSDNERVTLGFWKK SWISSPROT:HEMK_ECOLI ID HEMK_ECOLI STANDARD; PRT; 225 AA. AC P37186; 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 POSSIBLE PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.-). GN HEMK. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 95189105. RA NAKAYASHIKI T., NISHIMURA K., INOKUCHI H.; RL GENE 153:67-70(1995). CC -!- FUNCTION: COULD BE INVOLVED IN THE OXIDATION OF PROTOPORPHYRINOGEN CC INTO PROTOPORPHYRIN IX. CC -!- PATHWAY: INVOLVED IN PORPHYRIN BIOSYNTHESIS. DR EMBL; D28567; G466533; -. DR ECOGENE; EG12424; HEMK. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE. SQ SEQUENCE 225 AA; 25357 MW; ED807A29 CRC32; >HEMK_ECOLI MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLT RRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQALARLPEQPCRILDLGTGT GAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALAGQQFAMI VSNPPYIDEQDPHLQQGDVRFEPRHCAGCGRQWNGRHRAYHRTVA SWISSPROT:HEMK_BACSU ID HEMK_BACSU STANDARD; PRT; 288 AA. AC P45873; 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 POSSIBLE PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.-). GN YWKE. OS BACILLUS SUBTILIS. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=168; RA GLASER P., DE LA FUENTE V., DANCHIN A.; RL SUBMITTED (MAY-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. CC -!- FUNCTION: COULD BE INVOLVED IN THE OXIDATION OF PROTOPORPHYRINOGEN CC INTO PROTOPORPHYRIN IX (BY SIMILARITY). CC -!- PATHWAY: INVOLVED IN PORPHYRIN BIOSYNTHESIS. DR EMBL; Z49782; G853777; -. DR SUBTILIST; BG11316; YWKE. KW HYPOTHETICAL PROTEIN; PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE. SQ SEQUENCE 288 AA; 32383 MW; C7A66B1A CRC32; >HEMK_BACSU MKTIFEALKWASSYLTEAGREENAAELLLLYDTGMERSKLLASLQEPIGEDELYRFKRHV EMHKEGVPVQYIIGKEFFYGREFMVNDDVLIPRPETEEVVFHLLEKYRSVFSEDGKLEVV DVGTGSGAIAVTLALENQSFSVSAVDISKEALQVASANAEKLGANVRFYQGDLLEPFIKA GKKADIIVSNPPYISEEEMADLSEIVRFHEPLHALTDGGDGLKFYKRFMEDIPLVMKDKV FVVFEIGWKQGAAVKDLILKAFKGAEVEVLKDINGKDRTICALIHKNK SWISSPROT:HEMG_ECOLI ID HEMG_ECOLI STANDARD; PRT; 181 AA. AC P27863; DT 01-AUG-1992 (REL. 23, CREATED) DT 01-AUG-1992 (REL. 23, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.4) (PPO). GN HEMG. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] 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 [2] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 91057145. RA NAKAHIGASHI K., INOKUCHI H.; RL NUCLEIC ACIDS RES. 18:6439-6439(1990). RN [3] RP SEQUENCE FROM N.A., SEQUENCE OF 1-18, AND CHARACTERIZATION. RC STRAIN=K12; RX MEDLINE; 94177529. RA SASARMAN A., LETOWSKI J., CZAIKA G., RAMIREZ V., NEAD M.A., RA JACOBS J.M., MORAIS R.; RL CAN. J. MICROBIOL. 39:1155-1161(1993). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE; 95308321. RA NISHIMURA K., NAKAHIGASHI K., INOKUCHI H.; RL DNA RES. 2:1-8(1995). CC -!- FUNCTION: CATALYZES THE 6-ELECTRON OXIDATION OF PROTOPORPHYRINOGEN CC IX TO FORM PROTOPORPHYRIN IX. CC -!- CATALYTIC ACTIVITY: PROTOPORPHYRINOGEN-IX + O(2) = PROTOPORPHYRIN- CC IX + H(2)O. CC -!- PATHWAY: PENULTIMATE STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- COFACTOR: FMN FLAVOPROTEIN (POTENTIAL). CC -!- CAUTION: REF.2 SEQUENCE DIFFERS FROM THAT SHOWN DUE TO CC FRAMESHIFTS. DR EMBL; M87049; G148250; ALT_SEQ. DR EMBL; X54687; -; NOT_ANNOTATED_CDS. DR EMBL; X68660; G581103; -. DR PIR; S30741; S30741. DR PIR; S41629; S41629. DR ECOGENE; EG11485; HEMG. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; FLAVOPROTEIN; FMN. SQ SEQUENCE 181 AA; 21226 MW; FF3382BD CRC32; >HEMG_ECOLI MKTLILFSTRDGQTREIASYLASELKELGIQADVANVHRIEEPQWENYDRVVIGASIRYG HYHSAFQEFVKKHATRLNSMPSAFYSVNLVARKPEKRTPQTNSYARKFLMNSQWRPDRCA VIAGALRYPRYRWYDRFMIKLIMKMSGGETDTRKEVVYTDWEQVANFAREIAHLTDKPTL K SWISSPROT:HEMG_BACSU ID HEMG_BACSU STANDARD; PRT; 470 AA. AC P32397; DT 01-OCT-1993 (REL. 27, CREATED) DT 01-OCT-1993 (REL. 27, LAST SEQUENCE UPDATE) DT 01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE) DE PROTOPORPHYRINOGEN OXIDASE (EC 1.3.3.4) (PPO). GN HEMG OR HEMY. OS BACILLUS SUBTILIS. OC PROKARYOTA; FIRMICUTES; ENDOSPORE-FORMING RODS AND COCCI; BACILLACEAE. RN [1] RP SEQUENCE FROM N.A. RX MEDLINE; 93094140. RA HANSSON M., HEDERSTEDT L.; RL J. BACTERIOL. 174:8081-8093(1992). RN [2] RP CHARACTERIZATION. RX MEDLINE; 94117488. RA DAILEY T.A., MEISSNER P., DAILEY H.A.; RL J. BIOL. CHEM. 269:813-815(1994). CC -!- FUNCTION: CATALYZES THE 6-ELECTRON OXIDATION OF PROTOPORPHYRINOGEN CC IX TO FORM PROTOPORPHYRIN IX. CC -!- CATALYTIC ACTIVITY: PROTOPORPHYRINOGEN-IX + O(2) = PROTOPORPHYRIN- CC IX + H(2)O. CC -!- PATHWAY: PENULTIMATE STEP IN PORPHYRIN BIOSYNTHESIS. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- COFACTOR: FMN FLAVOPROTEIN (POTENTIAL). CC -!- SIMILARITY: OTHER SPECIES PROTOPORPHYRINOGEN OXIDASE. DR EMBL; M97208; G143045; -. DR PIR; D47045; D47045. DR SUBTILIST; BG10431; HEMG. KW PORPHYRIN BIOSYNTHESIS; OXIDOREDUCTASE; FLAVOPROTEIN; FMN. SQ SEQUENCE 470 AA; 51203 MW; E87BF0C9 CRC32; >HEMG_BACSU MSDGKKHVVIIGGGITGLAAAFYMEKEIKEKNLPLELTLVEASPRVGGKIQTVKKDGYII ERGPDSFLERKKSAPQLVKDLGLEHLLVNNATGQSYVLVNRTLHPMPKGAVMGIPTKIAP FVSTGLFSLSGKARAAMDFILPASKTKDDQSLGEFFRRRVGDEVVENLIEPLLSGIYAGD IDKLSLMSTFPQFYQTEQKHRSLILGMKKTRPQGSGQQLTAKKQGQFQTLSTGLQTLVEE IEKQLKLTKVYKGTKVTKLSHSGSCYSLELDNGVTLDADSVIVTAPHKAAAGMLSELPAI SHLKNMHSTSVANVALGFPEGSVQMEHEGTGFVISRNSDFAITACTWTNKKWPHAAPEGK TLLRAYVGKAGDESIVDLSDNDIINIVLEDLKKVMNINGEPEMTCVTRWHESMPQYHVGH KQRIKELREALASAYPGVYMTGASFEGVGIPDCIDQGKAAVSDALTYLFS TREMBL:Q49404 ID Q49404 PRELIMINARY; PRT; 456 AA. AC Q49404; 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 PROTOPORPHYRINOGEN OXIDASE. GN HEMK. OS MYCOPLASMA GENITALIUM. OC PROKARYOTA; TENERICUTES; MOLLICUTES; MYCOPLASMA; MYCOPLASMATALES; OC MYCOPLASMATACEAE. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=G37; RX MEDLINE; 96026346. RA FRASER C.M., GOCAYNE J.D., WHITE O., ADAMS M.D., CLAYTON R.A., RA FLEISCHMANN R.D., BULT C.J., KERLAVAGE A.R., SUTTON G., RA KELLEY J.M., FRITCHMAN J.L., WEIDMAN J.F., SMALL K.V., RA SANDUSKY M., FUHRMANN J.L., NGUYEN D.T., UTTERBACK T.R., RA SAUDEK D.M., PHILLIPS C.A., MERRICK J.M., TOMB J.F., RA DOUGHERTY B.A., BOTT K.F., HU P.C., LUCIER T.S., PETERSON S.N., RA SMITH H.O., HUTCHISON C.A., III VENTER J.C.; RL SCIENCE 270:397-403(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=G37; RA FRASER C.M., GOCAYNE J.D., WHITE O., ADAMS M.D., CLAYTON R.A., RA FLEISCHMANN R.D., BULT C.J., KERLAVAGE A.R., SUTTON G., RA KELLEY J.M., FRITSCHMAN J.L., WEIDMAN J.F., SMALL K.V., RA SANDUSKY M., FUHRMANN J.L., NGUYEN D.T., UTTERBACK T.R., RA SAUDEK D.M., PHILLIPS C.A., MERRICK J.M., TOMB J.F., RA DOUGHERTY B.A., BOTT K.F., HU P.C., LUCIER T.S., PETERSON S.N., RA SMITH H.O., HUTCHINSON C.A., VENTER J.C.; RL SUBMITTED (OCT-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. DR EMBL; U39704; G1045951; -. SQ SEQUENCE 456 AA; 52808 MW; 135825B2 CRC32; >Q49404 MTLYEFFLNQKLVYQSSPHFNGVFLTILEHYGFQFKTIDKLWKSKLLITSELTDKIKQQL KCYFIEKIPLPYLLGTIQLRKLTFKTKKGVFIPRIDSLALIASVNLKKIKTALDLCCGSG TLAIALKKKCDTLDVYGSDIDIQALKLAQQNALINNVSINWIEADWFDCFNKIKTPIDLI VTNPPYLKKTQLNKTLNYEPKHSLVFQNKNSYFAYKQLFNLLLTKRSIKQLIFECSLFQK ERLLNLFSIFKSRPIFNFQKQFIGMKVDNQKLPVVDIKNTKTIKQLLKMGLAGIVNTDTQ MGLISYSESTLDKIKQRALNKHYVSMFGLEELKKLPKKLQQIASYFWPGSYTFIKNNKSY RVPKNLGLLNLFNAIGRVFCTSANISNQKPYTKLSDYQNDSYWIKQPCFIIRSTSKVQSN NTPSLVYNLDTKQLVRTTAKQTKQFHKLITKHQLAI TREMBL:Q46754 ID Q46754 PRELIMINARY; PRT; 277 AA. AC Q46754; 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 POSSIBLE PROTOPORPHYRINOGEN OXIDASE. GN HEMK. OS ESCHERICHIA COLI. OC PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS; OC ENTEROBACTERIACEAE. RN [1] RP SEQUENCE FROM N.A. RA REMLER P., WOISETSCHLAEGER M., STROHMAIER H.; RL SUBMITTED (OCT-1995) TO EMBL/GENBANK/DDBJ DATA BANKS. RN [2] RP SEQUENCE OF 222-277 FROM N.A. RX MEDLINE; 95362678. RA STROHMAIER H., REMLER P., RENNER W., HOEGENAUER G.; RL J. BACTERIOL. 177:4488-4500(1995). RN [3] RP SEQUENCE FROM N.A. RA REMLER P.; RL SUBMITTED (DEC-1994) TO EMBL/GENBANK/DDBJ DATA BANKS. DR EMBL; U18555; G968931; -. SQ SEQUENCE 277 AA; 30975 MW; F34BE435 CRC32; >Q46754 MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLT RRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQALARLPEQPCRILDLGTGT GAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALAGQQFAMI VSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEHGW QQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ 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 TREMBLNEW:MPAE47_3 ID MPAE47_3 standard; PRT; 453 AA. AC AE000047; DR EMBL; AE000047; MPAE47. DE product: "possible protoporphyrinogen oxidase"; DE Mycoplasma pneumoniae from bases 587077 to 607293 (section 47 of DE 63) of the complete genome. OS Mycoplasma pneumoniae OC Eubacteria; Firmicutes; Low G+C gram-positive bacteria; OC Mycoplasmas and walled relatives; Mycoplasmatales; OC Mycoplasmataceae; Mycoplasma. OG Mitochondrion FT CDS complement(2714..4075) FT /note="similar to GenBank Accession Number U18555_6, from FT E. coli" FT /codon_start=1 FT /product="possible protoporphyrinogen oxidase" FT /transl_table=4 FT /db_xref="PID:g1674165" FT /translation="MNLYELFLNQKLLYGTDPHFNGVFLTLLEKFGLHFKDLTALWKHA FT KTITDFDEQGIVNALKAYFVDQLPLPYITGSVKLGSLTFKTQPGVFIPRADSLALLKVV FT KAQNLKTAVDLCCGSGTLAIALKKRFPHLNVYGSDLNPQALQLAAQNARLNMVEVQWIE FT ADFLAALAQVNTPIDLIITNPPYLNESQLDQTLNHEPRNSLVADGNGILFYQKLYNFLL FT GNRQVKQVILECSPTQKKEFLALFSIFKTSEIYTSHKQFIGLSIDNTKLPVLKIAQTKQ FT IKALLDKGMTAIIPTDTQIGLMSYCQQDLDHIKQRDPNKHYVQFLAPSQINQLPKQLQK FT LAKLFWPGAYTFIVDGQSYRLPNSPQLLKLLKTVGLIYCTSANQAKQKPFGKLSAYQND FT PYWVQQNCFIVQNSFKSNNEPSLIYNLDTKQIVRGSSTQLQRFQALLAKHKLRH" SQ Sequence 453 BP; >MPAE47_3 MNLYELFLNQKLLYGTDPHFNGVFLTLLEKFGLHFKDLTALWKHAKTITDFDEQGIVNAL KAYFVDQLPLPYITGSVKLGSLTFKTQPGVFIPRADSLALLKVVKAQNLKTAVDLCCGSG TLAIALKKRFPHLNVYGSDLNPQALQLAAQNARLNMVEVQWIEADFLAALAQVNTPIDLI ITNPPYLNESQLDQTLNHEPRNSLVADGNGILFYQKLYNFLLGNRQVKQVILECSPTQKK EFLALFSIFKTSEIYTSHKQFIGLSIDNTKLPVLKIAQTKQIKALLDKGMTAIIPTDTQI GLMSYCQQDLDHIKQRDPNKHYVQFLAPSQINQLPKQLQKLAKLFWPGAYTFIVDGQSYR LPNSPQLLKLLKTVGLIYCTSANQAKQKPFGKLSAYQNDPYWVQQNCFIVQNSFKSNNEP SLIYNLDTKQIVRGSSTQLQRFQALLAKHKLRH TREMBLNEW:ECAE219_10 ID ECAE219_10 standard; PRT; 277 AA. AC AE000219; DR EMBL; AE000219; ECAE219. DE gene: "hemK"; product: "possibly protoporphyrinogen oxidase"; DE Escherichia coli from bases 1255530 to 1269135 (section 109 of 400) DE of the complete genome. OS Escherichia coli OC Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OG Chloroplast FT CDS 9788..10621 FT /gene="hemK" FT /note="o277; 99 pct identical to PIR: I83570; 99 pct FT identical to 202 residues of HEMK_ECOLI SW: P37186 but FT differs at C-terminus" FT /codon_start=1 FT /product="possibly protoporphyrinogen oxidase" FT /transl_table=11 FT /db_xref="PID:g1787463" FT /translation="MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGET FT QLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQALA FT RLPEQPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHI FT LQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIE FT QSRNALVSGGFLLLEHGWQQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ" SQ Sequence 277 BP; >ECAE219_10 MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLT RRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQALARLPEQPCRILDLGTGT GAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALAGQQFAMI VSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEHGW QQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ TREMBLNEW:ECD757_3 ID ECD757_3 standard; PRT; 277 AA. AC D90757; DR EMBL; D90757; ECD757. DE gene: "hemK"; product: "Possible protoporphyrinogen oxidase"; DE Escherichia coli genomic DNA (27.2-27.6 min). OS Escherichia coli OC Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OG Chloroplast FT CDS 1218..2051 FT /gene="hemK" FT /codon_start=1 FT /product="Possible protoporphyrinogen oxidase" FT /transl_table=11 FT /db_xref="PID:g1651610" FT /translation="MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGET FT QLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQALA FT RLPEQPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHI FT LQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIE FT QSRNALVSGGFLLLEHGWQQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ" SQ Sequence 277 BP; >ECD757_3 MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLT RRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQALARLPEQPCRILDLGTGT GAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALAGQQFAMI VSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEHGW QQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ TREMBLNEW:ECD756_6 ID ECD756_6 standard; PRT; 277 AA. AC D90756; DR EMBL; D90756; ECD756. DE gene: "hemK"; product: "Possible protoporphyrinogen oxidase"; DE Escherichia coli genomic DNA.(27.0 -27.4 min). OS Escherichia coli OC Eubacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OG Chloroplast FT CDS 10356..11189 FT /gene="hemK" FT /codon_start=1 FT /product="Possible protoporphyrinogen oxidase" FT /transl_table=11 FT /db_xref="PID:g1651602" FT /translation="MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGET FT QLTDEQCQQLDALLTRRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQALA FT RLPEQPCRILDLGTGTGAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHI FT LQSDWFSALAGQQFAMIVSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIE FT QSRNALVSGGFLLLEHGWQQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ" SQ Sequence 277 BP; >ECD756_6 MEYQHWLREAISQLQASESPRRDAEILLEHVTGRGRTFILAFGETQLTDEQCQQLDALLT RRRDGEPIAHLTGVREFWSLPLFVSPATLIPRPDTECLVEQALARLPEQPCRILDLGTGT GAIALALASERPDCEIIAVDRMPDAVSLAQRNAQHLAIKNIHILQSDWFSALAGQQFAMI VSNPPYIDEQDPHLQQGDVRFEPLTALVAADSGMADIVHIIEQSRNALVSGGFLLLEHGW QQGEAVRQAFILAGYHDVETCRDYGDNERVTLGRYYQ TREMBLNEW:MMPO1_1 ID MMPO1_1 standard; PRT; 477 AA. AC D45185; DR EMBL; D45185; MMPO1. DE product: "protoporphyrinogen oxidase"; DE Mouse mRNA for protoporphyrinogen oxidase, complete cds. OS Mus musculus (house mouse) OC Eukaryotae; mitochondrial eukaryotes; Metazoa; Chordata; OC Vertebrata; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; OC Mus. OG Mitochondrion FT CDS 49..1482 FT /codon_start=1 FT /product="protoporphyrinogen oxidase" FT /db_xref="PID:g1786169" FT /translation="MGRTVIVLGGGISGLAASYHLIRGPSPPKVILVEGSKRLGGWIRS FT IRGSDGAIFELGPRGIRPTGPLGARTLLLVSELGLESEVLPVRGDHPAAQNRFLYVGGT FT LHPSPSGLRGLLRPSPPFSKPLFWAGLRELLKPRGKEPDETVHSFAQRRLGPEVASLAM FT DSLCRGVFAGNSRELSIRSCFPSLFQAEQTHRSILLGLLLGAGQSPQPDSSLIRQARAE FT RWSQWSLRGGLEVLPQALHNHLASKGVTVLSGQPVCGLSLQPEGRWKVSLGDSSLEADH FT IISAIPASELSKLLPAEAAPLARILSTIKAVSVAVVNLQYRGACLPVQGFGHLVPSSED FT PTVLGIVYDSVAFPEQDGNPPSLRVTVMLGGYWLQKLKAAGHQLSPELFQQQAQEAAAT FT QLGLKEPPSHCLVHLHKNCIPQYTIGHCQKLDSAMQFLTAQRLPLTLAGASYEGVAVND FT CIESGRQAAVAVLGTESNS" SQ Sequence 477 BP; >MMPO1_1 MGRTVIVLGGGISGLAASYHLIRGPSPPKVILVEGSKRLGGWIRSIRGSDGAIFELGPRG IRPTGPLGARTLLLVSELGLESEVLPVRGDHPAAQNRFLYVGGTLHPSPSGLRGLLRPSP PFSKPLFWAGLRELLKPRGKEPDETVHSFAQRRLGPEVASLAMDSLCRGVFAGNSRELSI RSCFPSLFQAEQTHRSILLGLLLGAGQSPQPDSSLIRQARAERWSQWSLRGGLEVLPQAL HNHLASKGVTVLSGQPVCGLSLQPEGRWKVSLGDSSLEADHIISAIPASELSKLLPAEAA PLARILSTIKAVSVAVVNLQYRGACLPVQGFGHLVPSSEDPTVLGIVYDSVAFPEQDGNP PSLRVTVMLGGYWLQKLKAAGHQLSPELFQQQAQEAAATQLGLKEPPSHCLVHLHKNCIP QYTIGHCQKLDSAMQFLTAQRLPLTLAGASYEGVAVNDCIESGRQAAVAVLGTESNS TREMBLNEW:SSD911_75 ID SSD911_75 standard; PRT; 299 AA. AC D90911; DR EMBL; D90911; SSD911. DE gene: "hemK"; product: "protoporphyrinogen oxidase"; DE Synechocystis sp. PCC6803 complete genome, 13/27, 1576593-1719643. OS Synechocystis sp. OC Eubacteria; Cyanobacteria; Chroococcales; Synechocystis. OG Mitochondrion FT CDS complement(75805..76704) FT /gene="hemK" FT /note="ORF_ID:sll1237" FT /codon_start=1 FT /product="protoporphyrinogen oxidase" FT /transl_table=11 FT /db_xref="PID:g1653158" FT /translation="MNKGFVSGEEFARWYATARQMAIAHGIETGELNWLLQGWTDLDRL FT TLRLQDFAHREIALQETWENIQRGWRRRVEEKYPVQYLLGQTQWRDFVIKVTDDVLIPR FT PETELIIDIVQHEHSALSPSNCADHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSAL FT AIARENAQLNQFGDRIQFHQGYWWEPLEHLKGQVQGMVSNPPYIPQRELAQLQPEVIKH FT EPLLALDGGPDGLQAVEQLIRRSPTYLKPGGFWLVEIMTGQAPMVAELLRASGAYQDIQ FT IHRDLASIERFVSARTLS" SQ Sequence 299 BP; >SSD911_75 MNKGFVSGEEFARWYATARQMAIAHGIETGELNWLLQGWTDLDRLTLRLQDFAHREIALQ ETWENIQRGWRRRVEEKYPVQYLLGQTQWRDFVIKVTDDVLIPRPETELIIDIVQHEHSA LSPSNCADHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQLNQFGDRIQ FHQGYWWEPLEHLKGQVQGMVSNPPYIPQRELAQLQPEVIKHEPLLALDGGPDGLQAVEQ LIRRSPTYLKPGGFWLVEIMTGQAPMVAELLRASGAYQDIQIHRDLASIERFVSARTLS