HEM6_ECOLU
ID HEM6_ECOLU Reviewed; 299 AA.
AC B7N626;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=ECUMN_2757;
OS Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585056;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMN026 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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=Mn(2+); Xref=ChEBI:CHEBI:29035;
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; CU928163; CAR13935.1; -; Genomic_DNA.
DR RefSeq; WP_001309639.1; NC_011751.1.
DR RefSeq; YP_002413462.1; NC_011751.1.
DR AlphaFoldDB; B7N626; -.
DR SMR; B7N626; -.
DR STRING; 585056.ECUMN_2757; -.
DR EnsemblBacteria; CAR13935; CAR13935; ECUMN_2757.
DR KEGG; eum:ECUMN_2757; -.
DR PATRIC; fig|585056.7.peg.2938; -.
DR HOGENOM; CLU_026169_0_1_6; -.
DR OMA; HDKGTLF; -.
DR UniPathway; UPA00251; UER00322.
DR Proteomes; UP000007097; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
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; Manganese; Metal-binding; Oxidoreductase;
KW Porphyrin biosynthesis.
FT CHAIN 1..299
FT /note="Oxygen-dependent coproporphyrinogen-III oxidase"
FT /id="PRO_1000119800"
FT REGION 240..275
FT /note="Important for dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 96
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 106
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 108..110
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 145
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 175
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 258..260
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT SITE 175
FT /note="Important for dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
SQ SEQUENCE 299 AA; 34342 MW; 9377036AFB72975D CRC64;
MKPDAHQVKQ FLLNLQDTIC QQLSAVDGAE FVEDSWQREA GGGGRSRVLR NGGVFEQAGV
NFSHVHGEAM PASATAHRPE LAGRSFEAMG ISLVVHPHNP YVPTSHANVR FFIAEKPGAE
PVWWFGGGFD LTPFYGFEED AIHWHRTARD LCQPFGEDVY PRYKKWCDEY FYLKHRNEQR
GIGGLFFDDL NTPDFDHCFA FMQAVGKGYT NAYLPIVERR KAMAYGERER NFQLYRRGRY
VEFNLVWDRG TLFGLQTGGR TESILMSMPP LVRWEYDYHP EDGSPEAALS EFIKVRDWV
