ID HEM6_ECOBW Reviewed; 299 AA. AC C4ZX09; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 28-JUL-2009, sequence version 1. DT 02-SEP-2026, entry version 76. DE RecName: Full=Oxygen-dependent coproporphyrinogen-III oxidase {ECO:0000255|HAMAP-Rule:MF_00333}; DE Short=CPO {ECO:0000255|HAMAP-Rule:MF_00333}; DE Short=Coprogen oxidase {ECO:0000255|HAMAP-Rule:MF_00333}; DE Short=Coproporphyrinogenase {ECO:0000255|HAMAP-Rule:MF_00333}; DE EC=1.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00333}; GN Name=hemF {ECO:0000255|HAMAP-Rule:MF_00333}; GN OrderedLocusNames=BWG_2198; OS Escherichia coli (strain K12 / MC4100 / BW2952). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Enterobacteriaceae; Escherichia. OX NCBI_TaxID=595496; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MC4100 / BW2952; RX PubMed=19376874; DOI=10.1128/jb.00118-09; RA Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R., RA Wang L.; RT "Genomic sequencing reveals regulatory mutations and recombinational events RT in the widely used MC4100 lineage of Escherichia coli K-12."; RL J. Bacteriol. 191:4025-4029(2009). CC -!- FUNCTION: Involved in the heme biosynthesis. Catalyzes the aerobic CC oxidative decarboxylation of propionate groups of rings A and B of CC coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen- CC IX. {ECO:0000255|HAMAP-Rule:MF_00333}. CC -!- CATALYTIC ACTIVITY: CC Reaction=coproporphyrinogen III + O2 + 2 H(+) = protoporphyrinogen IX + CC 2 CO2 + 2 H2O; Xref=Rhea:RHEA:18257, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:57307, ChEBI:CHEBI:57309; EC=1.3.3.3; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00333}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00333}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX CC biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00333}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00333}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00333}. CC -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase CC family. {ECO:0000255|HAMAP-Rule:MF_00333}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001396; ACR62610.1; -; Genomic_DNA. DR RefSeq; WP_000801365.1; NC_012759.1. DR AlphaFoldDB; C4ZX09; -. DR SMR; C4ZX09; -. DR KEGG; ebw:BWG_2198; -. DR HOGENOM; CLU_026169_0_1_6; -. DR UniPathway; UPA00251; UER00322. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 3.40.1500.10:FF:000001; Oxygen-dependent coproporphyrinogen-III oxidase; 1. DR Gene3D; 3.40.1500.10; Coproporphyrinogen III oxidase, aerobic; 1. DR HAMAP; MF_00333; Coprogen_oxidas; 1. DR InterPro; IPR001260; Coprogen_oxidase_aer. DR InterPro; IPR036406; Coprogen_oxidase_aer_sf. DR InterPro; IPR018375; Coprogen_oxidase_CS. DR NCBIfam; NF003727; PRK05330.1; 1. DR PANTHER; PTHR10755; COPROPORPHYRINOGEN III OXIDASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR10755:SF0; OXYGEN-DEPENDENT COPROPORPHYRINOGEN-III OXIDASE, MITOCHONDRIAL; 1. DR Pfam; PF01218; Coprogen_oxidas; 1. DR PIRSF; PIRSF000166; Coproporphyri_ox; 1. DR PRINTS; PR00073; COPRGNOXDASE. DR SUPFAM; SSF102886; Coproporphyrinogen III oxidase; 1. DR PROSITE; PS01021; COPROGEN_OXIDASE; 1. PE 3: Inferred from homology; KW Cytoplasm; Heme biosynthesis; Manganese; Metal-binding; Oxidoreductase; KW Porphyrin biosynthesis. FT CHAIN 1..299 FT /note="Oxygen-dependent coproporphyrinogen-III oxidase" FT /id="PRO_1000205202" FT REGION 240..275 FT /note="Important for dimerization" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333" FT ACT_SITE 106 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333" FT BINDING 92 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333" FT BINDING 96 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333" FT BINDING 106 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333" FT BINDING 108..110 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333" FT BINDING 145 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333" FT BINDING 175 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333" FT BINDING 258..260 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333" FT SITE 175 FT /note="Important for dimerization" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333" 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 //