(data stored in ACNUC7421 zone)

SWISSPROT: HEM6_PSEAB

ID   HEM6_PSEAB              Reviewed;         305 AA.
AC   Q02V57;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   07-JUN-2017, entry version 68.
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=PA14_00280;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(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
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; CP000438; ABJ14980.1; -; Genomic_DNA.
DR   RefSeq; WP_003097311.1; NC_008463.1.
DR   ProteinModelPortal; Q02V57; -.
DR   SMR; Q02V57; -.
DR   EnsemblBacteria; ABJ14980; ABJ14980; PA14_00280.
DR   KEGG; pau:PA14_00280; -.
DR   HOGENOM; HOG000262768; -.
DR   KO; K00228; -.
DR   OMA; MDLTPYY; -.
DR   UniPathway; UPA00251; UER00322.
DR   Proteomes; UP000000653; 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; Q02V57.
DR   SWISS-2DPAGE; Q02V57.
KW   Complete proteome; Cytoplasm; Heme biosynthesis; Metal-binding;
KW   Oxidoreductase; Porphyrin biosynthesis.
FT   CHAIN         1    305       Oxygen-dependent coproporphyrinogen-III
FT                                oxidase.
FT                                /FTId=PRO_1000019484.
FT   REGION      109    111       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   REGION      241    276       Important for dimerization.
FT                                {ECO:0000255|HAMAP-Rule:MF_00333}.
FT   REGION      259    261       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   ACT_SITE    107    107       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   METAL        97     97       Divalent cation. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   METAL       107    107       Divalent cation. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   METAL       146    146       Divalent cation. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   METAL       176    176       Divalent cation. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   BINDING      93     93       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00333}.
FT   SITE        176    176       Important for dimerization.
FT                                {ECO:0000255|HAMAP-Rule:MF_00333}.
SQ   SEQUENCE   305 AA;  34806 MW;  240BD06FEA37EAE3 CRC64;
     MTDRIAAVKT YLLDLQDRIC AALEAEDGKA RFAEDAWERP AGGGGRTRVI GDGALIEKGG
     VNFSHVFGDS LPPSASAHRP ELAGRGFQAL GVSLVIHPEN PHVPTSHANV RFFCAEKEGE
     EPVWWFGGGF DLTPYYAHEE DCVHWHRVAR DACAPFGADV YPRYKEWCDR YFHLKHRNEP
     RGIGGLFFDD LNQWDFDTCF AFIRAIGDAY IDAYLPIVQR RKHTPFDERQ REFQAYRRGR
     YVEFNLVFDR GTLFGLQSGG RTESILMSLP PQVRWGYDWK PEPGSEEARL TEYFLADRDW
     LAGQP
//

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