HEM6_SHESA
ID HEM6_SHESA Reviewed; 302 AA.
AC A0KR67;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Shewana3_0041;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) 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; CP000469; ABK46286.1; -; Genomic_DNA.
DR RefSeq; WP_011715331.1; NC_008577.1.
DR AlphaFoldDB; A0KR67; -.
DR SMR; A0KR67; -.
DR STRING; 94122.Shewana3_0041; -.
DR EnsemblBacteria; ABK46286; ABK46286; Shewana3_0041.
DR KEGG; shn:Shewana3_0041; -.
DR eggNOG; COG0408; Bacteria.
DR HOGENOM; CLU_026169_0_1_6; -.
DR OMA; HDKGTLF; -.
DR OrthoDB; 1086432at2; -.
DR UniPathway; UPA00251; UER00322.
DR Proteomes; UP000002589; 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..302
FT /note="Oxygen-dependent coproporphyrinogen-III oxidase"
FT /id="PRO_1000019501"
FT REGION 242..277
FT /note="Important for dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 98
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 108
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 110..112
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 147
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 177
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 260..262
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT SITE 177
FT /note="Important for dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
SQ SEQUENCE 302 AA; 34136 MW; E7A1510B8AD33E1C CRC64;
MSVPDATVVK AFLLDLQNRI CAGLEQLDGQ ASFAADSWTR TEGGGGTSRV LTQGAVFEQA
GVNFSHVTGA AMPASATAHR PELAGRSFEA MGVSLVIHPK NPYIPTTHAN VRFFIAHKDG
ADPVWWFGGG FDLTPYYPFE EDVREWHQTA KNLCLPFGDD VYPKYKKWCD EYFFLPHRNE
TRGVGGLFFD DLNQAGFDKS FDFMQAVGNG FLTAYAPIVE RRKETPYGER ERDFQLYRRG
RYVEFNLVYD RGTLFGLQTG GRTESILMSM PPLVRWQYAY TPEAGSPEAE LYDNYLKPRD
WV
