ID Q3SPB7_NITWN Unreviewed; 300 AA. AC Q3SPB7; DT 11-OCT-2005, integrated into UniProtKB/TrEMBL. DT 11-OCT-2005, sequence version 1. DT 02-SEP-2026, entry version 137. DE RecName: Full=Oxygen-dependent coproporphyrinogen-III oxidase {ECO:0000256|HAMAP-Rule:MF_00333}; DE Short=CPO {ECO:0000256|HAMAP-Rule:MF_00333}; DE Short=Coprogen oxidase {ECO:0000256|HAMAP-Rule:MF_00333}; DE Short=Coproporphyrinogenase {ECO:0000256|HAMAP-Rule:MF_00333}; DE EC=1.3.3.3 {ECO:0000256|HAMAP-Rule:MF_00333}; GN Name=hemF {ECO:0000256|HAMAP-Rule:MF_00333}; GN OrderedLocusNames=Nwi_2621 {ECO:0000313|EMBL:ABA05874.1}; OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 / OS NCIMB 11846 / Nb-255). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Nitrobacteraceae; Nitrobacter. OX NCBI_TaxID=323098 {ECO:0000313|EMBL:ABA05874.1, ECO:0000313|Proteomes:UP000002531}; RN [1] {ECO:0000313|EMBL:ABA05874.1, ECO:0000313|Proteomes:UP000002531} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255 RC {ECO:0000313|Proteomes:UP000002531}; RX PubMed=16517654; DOI=10.1128/AEM.72.3.2050-2063.2006; RA Starkenburg S.R., Chain P.S., Sayavedra-Soto L.A., Hauser L., Land M.L., RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J., RA Hickey W.J.; RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium RT Nitrobacter winogradskyi Nb-255."; RL Appl. Environ. Microbiol. 72:2050-2063(2006). 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:0000256|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:0000256|HAMAP-Rule:MF_00333}; CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-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:0000256|ARBA:ARBA00005168, ECO:0000256|HAMAP- CC Rule:MF_00333}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP- CC Rule:MF_00333}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00333}. CC -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase CC family. {ECO:0000256|ARBA:ARBA00010644, ECO:0000256|HAMAP- CC 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; CP000115; ABA05874.1; -; Genomic_DNA. DR RefSeq; WP_011315824.1; NC_007406.1. DR AlphaFoldDB; Q3SPB7; -. DR STRING; 323098.Nwi_2621; -. DR KEGG; nwi:Nwi_2621; -. DR eggNOG; COG0408; Bacteria. DR HOGENOM; CLU_026169_0_1_5; -. DR OrthoDB; 9777553at2; -. DR UniPathway; UPA00251; UER00322. DR Proteomes; UP000002531; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0042803; F:protein homodimerization activity; IEA:UniProtKB-UniRule. DR GO; GO:0006783; P:heme biosynthetic process; IEA:UniProtKB-UniRule. DR FunFam; 3.40.1500.10:FF:000005; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00333}; KW Heme biosynthesis {ECO:0000256|ARBA:ARBA00023133, ECO:0000256|HAMAP- KW Rule:MF_00333}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00333}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00333}; KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244, ECO:0000256|HAMAP- KW Rule:MF_00333}; Reference proteome {ECO:0000313|Proteomes:UP000002531}. FT REGION 265..300 FT /note="Important for dimerization" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00333" FT ACT_SITE 131 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00333" FT BINDING 117 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00333" FT BINDING 121 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00333" FT BINDING 131 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00333" FT BINDING 133..135 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00333" FT BINDING 169 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00333" FT BINDING 200 FT /ligand="a divalent metal cation" FT /ligand_id="ChEBI:CHEBI:60240" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00333" FT BINDING 283..285 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00333" FT SITE 200 FT /note="Important for dimerization" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00333" SQ SEQUENCE 300 AA; 33871 MW; 40F83A5B2C281026 CRC64; MEATRLEDRT LEDRKARARS WFEQLRDDIC SAFEKLEDDA PASLYPGSAG RFVRTPWERT DHTGKPGGGG VMSMMHGRLF EKVGVHCSTV HGEFAPEFRA QIPGAADDPN FWASGISLIA HMRNPHIPAV HMNTRFVVTT KAWFGGGGDL TPVLMRRRTQ EDPDSVAFHA AMKAACDAHA AIAPYDKYKT WCDEYFHLPH RKEARGIGGI FYDWHDSGDW NADLAFTQDV GRALLKVYPE LVRRNFSTPW TAADREEQLI RRGRYAEFNL LYDRGTIFGL KTGGNVESIL SSMPPEVKWP //