(data stored in ACNUC7421 zone)

SWISSPROT: HEM6_SHESH

ID   HEM6_SHESH              Reviewed;         306 AA.
AC   A8FP82;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 67.
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=Ssed_0042;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-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
CC       protoporphyrinogen-IX. {ECO:0000255|HAMAP-Rule:MF_00333}.
CC   -!- CATALYTIC ACTIVITY: Coproporphyrinogen-III + O(2) + 2 H(+) =
CC       protoporphyrinogen-IX + 2 CO(2) + 2 H(2)O. {ECO:0000255|HAMAP-
CC       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-
CC       IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III
CC       (O2 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}.
DR   EMBL; CP000821; ABV34655.1; -; Genomic_DNA.
DR   RefSeq; WP_012004181.1; NC_009831.1.
DR   ProteinModelPortal; A8FP82; -.
DR   SMR; A8FP82; -.
DR   STRING; 425104.Ssed_0042; -.
DR   EnsemblBacteria; ABV34655; ABV34655; Ssed_0042.
DR   KEGG; sse:Ssed_0042; -.
DR   eggNOG; ENOG4105DBS; Bacteria.
DR   eggNOG; COG0408; LUCA.
DR   HOGENOM; HOG000262768; -.
DR   KO; K00228; -.
DR   OMA; MDLTPYY; -.
DR   OrthoDB; POG091H03H2; -.
DR   UniPathway; UPA00251; UER00322.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:UniProtKB-EC.
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; 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;
DR   PRODOM; A8FP82.
DR   SWISS-2DPAGE; A8FP82.
KW   Complete proteome; Cytoplasm; Heme biosynthesis; Metal-binding;
KW   Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN         1    306       Oxygen-dependent coproporphyrinogen-III
FT                                oxidase.
FT                                /FTId=PRO_1000079264.
FT   REGION      110    112       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   REGION      242    277       Important for dimerization.
FT                                {ECO:0000255|HAMAP-Rule:MF_00333}.
FT   REGION      260    262       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   ACT_SITE    108    108       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   METAL        98     98       Divalent cation. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   METAL       108    108       Divalent cation. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   METAL       147    147       Divalent cation. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   METAL       177    177       Divalent cation. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   BINDING      94     94       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   SITE        177    177       Important for dimerization.
FT                                {ECO:0000255|HAMAP-Rule:MF_00333}.
SQ   SEQUENCE   306 AA;  34941 MW;  C602D7F5EAE1988D CRC64;
     MSVPDTSAVK AFLLDLQQRI CEGLEQLDGK GTFEADSWKR EEGGGGTSRV LTNGKVFEQA
     GVNFSHVTGA AMPASATANR SELEGRSFEA MGVSLVIHPK NPFLPTTHAN VRFFIAKKEG
     ADPVWWFGGG FDLTPYYPFE EDVIEWHQNA HDLCQPFGES VYPKYKKWCD EYFFLPHRNE
     TRGVGGLFFD DLNQDGFEKS FEFMQAVGNG FLTSYAPIVE RRKDTEYGEK EREFQLYRRG
     RYVEFNLVYD RGTLFGLQTG GRTESILMSM PPLVRWQYAY TPEENSAEAL LYTDFLKPKD
     WLNLDE
//

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