ID   HEM6_ECOK1              Reviewed;         299 AA.
AC   A1ADV0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   16-JUN-2009, entry version 21.
DE   RecName: Full=Coproporphyrinogen-III oxidase, aerobic;
DE            Short=Coproporphyrinogenase;
DE            Short=Coprogen oxidase;
DE            EC=1.3.3.3;
GN   Name=hemF; OrderedLocusNames=Ecok1_23460; ORFNames=APECO1_4112;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/JB.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P.,
RA   Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R.,
RA   Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain
RT   O1:K1:H7 shares strong similarities with human extraintestinal
RT   pathogenic E. coli genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
CC   -!- CATALYTIC ACTIVITY: Coproporphyrinogen-III + O(2) + 2 H(+) =
CC       protoporphyrinogen-IX + 2 CO(2) + 2 H(2)O.
CC   -!- COFACTOR: Manganese (By similarity).
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis;
CC       protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step
CC       1/1.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the aerobic coproporphyrinogen-III oxidase
CC       family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000468; ABJ01840.1; -; Genomic_DNA.
DR   RefSeq; YP_853554.1; -.
DR   GeneID; 4495748; -.
DR   GenomeReviews; CP000468_GR; Ecok1_23460.
DR   KEGG; ecv:APECO1_4112; -.
DR   OMA; A1ADV0; VKAYLLD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:HAMAP.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006779; P:porphyrin biosynthetic process; IEA:HAMAP.
DR   HAMAP; MF_00333; -; 1.
DR   InterPro; IPR001260; Coprogen_oxidas.
DR   InterPro; IPR018375; Coproporphyrinogen-3_ox_CS.
DR   Gene3D; G3DSA:3.40.1500.10; Coprogen_oxidas; 1.
DR   PANTHER; PTHR10755; Coprogen_oxidas; 1.
DR   Pfam; PF01218; Coprogen_oxidas; 1.
DR   PIRSF; PIRSF000166; Coproporphyri_ox; 1.
DR   PRINTS; PR00073; COPRGNOXDASE.
DR   PROSITE; PS01021; COPROGEN_OXIDASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Manganese; Oxidoreductase;
KW   Porphyrin biosynthesis.
FT   CHAIN         1    299       Coproporphyrinogen-III oxidase, aerobic.
FT                                /FTId=PRO_1000019468.
SQ   SEQUENCE   299 AA;  34304 MW;  DC689C92CD71AE9B CRC64;
     MKPDAHQVKQ FLLNLQDTIC QQLSAVDGAE FVEDSWQREA GGGGRSRVLR NGGVFEQAGV
     NFSHVHGEAM PASATAHRPE LAGRSFEAMG VSLVVHPHNP YVPTSHANVR FFIAEKPGAE
     PVWWFGGGFD LTPFYGFEED AIHWHRTARD LCLPFGEDVY PRYKKWCDEY FYLKHRNEQR
     GIGGLFFDDL NTPDFDHCFA FMQAVGKGYT DAYLPIVERR KAMAYGERER NFQLYRRGRY
     VEFNLVWDRG TLFGLQTGGR TESILMSMPP LVRWEYDYQP KDGSPEAALS EFIKVRDWV
//