ID   HEM6_RICRS              Reviewed;         279 AA.
AC   A8GU63;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, 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}; OrderedLocusNames=A1G_07495;
OS   Rickettsia rickettsii (strain Sheila Smith).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=392021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheila Smith;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia rickettsii.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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 + 2 H(+) + O2 = 2 CO2 + 2 H2O +
CC         protoporphyrinogen IX; 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=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000255|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: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}.
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DR   EMBL; CP000848; ABV76938.1; -; Genomic_DNA.
DR   RefSeq; WP_012151472.1; NC_009882.1.
DR   AlphaFoldDB; A8GU63; -.
DR   SMR; A8GU63; -.
DR   EnsemblBacteria; ABV76938; ABV76938; A1G_07495.
DR   GeneID; 45539831; -.
DR   KEGG; rri:A1G_07495; -.
DR   HOGENOM; CLU_026169_0_1_5; -.
DR   OMA; HDKGTLF; -.
DR   UniPathway; UPA00251; UER00322.
DR   Proteomes; UP000006832; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.1500.10; -; 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   PANTHER; PTHR10755; PTHR10755; 1.
DR   Pfam; PF01218; Coprogen_oxidas; 1.
DR   PIRSF; PIRSF000166; Coproporphyri_ox; 1.
DR   PRINTS; PR00073; COPRGNOXDASE.
DR   SUPFAM; SSF102886; SSF102886; 1.
DR   PROSITE; PS01021; COPROGEN_OXIDASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Heme biosynthesis; Metal-binding; Oxidoreductase;
KW   Porphyrin biosynthesis.
FT   CHAIN           1..279
FT                   /note="Oxygen-dependent coproporphyrinogen-III oxidase"
FT                   /id="PRO_1000019494"
FT   REGION          244..279
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   ACT_SITE        116
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         106
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         116
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         118..120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         149
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         179
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   SITE            179
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
SQ   SEQUENCE   279 AA;  32041 MW;  99729A0A2D853958 CRC64;
     MNIENKEITS SWFTNLRDLL CKEFEKIEEE YAQTKGLKPA KFVRSSWQRN GGGGGVMSLM
     KGAVFEKVGV NISTVFGKIS PEFRNEIPGA ELDGKFFATG ISLVAHLKSP LIPAMHFNTR
     YIETSKSWFG GGGDLTPFYP EKNETVKFHA AFKEVCDKYD SSYYPKFKKQ CDEYFYLKHR
     KEPRGVGGIF YDYLNNGNFE QDFAFTQDVG KTLLSVYPEI VRSKLFLPWT AEQKEYQLIR
     RGRYVEFNLL YDRGTKFGLM TDGNVEAILM SLPPEVKFN