ID HEM6_ECOHS Reviewed; 299 AA. AC A8A2T4; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 1. DT 16-JUN-2009, entry version 13. DE RecName: Full=Coproporphyrinogen-III oxidase, aerobic; DE Short=Coproporphyrinogenase; DE Short=Coprogen oxidase; DE EC=1.3.3.3; GN Name=hemF; OrderedLocusNames=EcHS_A2573; OS Escherichia coli O9:H4 (strain HS). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=331112; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=18676672; DOI=10.1128/JB.00619-08; RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., RA Henderson I.R., Sperandio V., Ravel J.; RT "The pangenome structure of Escherichia coli: comparative genomic RT analysis of E. coli commensal and pathogenic isolates."; RL J. Bacteriol. 190:6881-6893(2008). CC -!- CATALYTIC ACTIVITY: Coproporphyrinogen-III + O(2) + 2 H(+) = CC protoporphyrinogen-IX + 2 CO(2) + 2 H(2)O. CC -!- COFACTOR: Manganese (By similarity). CC -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; CC protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step CC 1/1. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000802; ABV06838.1; -; Genomic_DNA. DR RefSeq; YP_001459221.1; -. DR GeneID; 5592296; -. DR GenomeReviews; CP000802_GR; EcHS_A2573. DR KEGG; ecx:EcHS_A2573; -. DR OMA; A8A2T4; VKAYLLD. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0006779; P:porphyrin biosynthetic process; IEA:HAMAP. DR HAMAP; MF_00333; -; 1. DR InterPro; IPR001260; Coprogen_oxidas. DR InterPro; IPR018375; Coproporphyrinogen-3_ox_CS. DR Gene3D; G3DSA:3.40.1500.10; Coprogen_oxidas; 1. DR PANTHER; PTHR10755; Coprogen_oxidas; 1. DR Pfam; PF01218; Coprogen_oxidas; 1. DR PIRSF; PIRSF000166; Coproporphyri_ox; 1. DR PRINTS; PR00073; COPRGNOXDASE. DR PROSITE; PS01021; COPROGEN_OXIDASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Manganese; Oxidoreductase; KW Porphyrin biosynthesis. FT CHAIN 1 299 Coproporphyrinogen-III oxidase, aerobic. FT /FTId=PRO_1000059705. SQ SEQUENCE 299 AA; 34323 MW; 53667E5C7B6D0198 CRC64; MKPDAHQVKQ FLLNLQDTIC QQLTAVDGAE FVEDSWQREA GGGGRSRVLR NGGVFEQAGV NFSHVHGEAM PASATAHRPE LAGRSFEAMG VSLVVHPHNP YVPTSHANVR FFIAEKPGAD PVWWFGGGFD LTPFYGFEED AIHWHRTARD LCLPFGEDVY PRYKKWCDEY FYLKHRNEQR GIGGLFFDDL NTPDFDRCFA FMQAVGKGYT DAYLPIVERR KAMAYGERER NFQLYRRGRY VEFNLVWDRG TLFGLQTGGR TESILMSMPP LVRWEYDYQP KDGSPEAALS EFIKVRDWV //