HEM6_SERP5
ID HEM6_SERP5 Reviewed; 306 AA.
AC A8GHH2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Spro_3464;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
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; CP000826; ABV42562.1; -; Genomic_DNA.
DR RefSeq; WP_012146176.1; NC_009832.1.
DR AlphaFoldDB; A8GHH2; -.
DR SMR; A8GHH2; -.
DR STRING; 399741.Spro_3464; -.
DR EnsemblBacteria; ABV42562; ABV42562; Spro_3464.
DR KEGG; spe:Spro_3464; -.
DR eggNOG; COG0408; Bacteria.
DR HOGENOM; CLU_026169_0_1_6; -.
DR OMA; HDKGTLF; -.
DR OrthoDB; 1086432at2; -.
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: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..306
FT /note="Oxygen-dependent coproporphyrinogen-III oxidase"
FT /id="PRO_1000059708"
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 306 AA; 34886 MW; A6EF5DBEC6EFEC22 CRC64;
MSLSTIAEVK TFLLALQDRI CTQLAQADGS AVFNEDRWTR EEGGGGRSRV LTEGAVFEQA
GVNFSHVSGA TLPASATAHR PELAGRSFQA MGVSLVIHPR SPYIPTSHAN VRFFIAEKPG
EEPVWWFGGG FDLTPFYGFE EDAVHWHRTA ERLCAPFGEQ VYPKYKKWCD DYFFIKHRNE
ARGIGGLFFD DLNTPDFATC FAFTQAVGEG FLEAYLPIVE KRKTLSWGDH ERQFQLYRRG
RYVEFNLVWD RGTLFGLQTG GRTESILMSM PPLVRWEYNY QPAEDSPEAA LYRDFLPVRD
WLKEPE
