HEM6_BRADU
ID HEM6_BRADU Reviewed; 316 AA.
AC Q89SC2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=bll2481;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000040; BAC47746.1; -; Genomic_DNA.
DR RefSeq; NP_769121.1; NC_004463.1.
DR AlphaFoldDB; Q89SC2; -.
DR SMR; Q89SC2; -.
DR STRING; 224911.27350737; -.
DR EnsemblBacteria; BAC47746; BAC47746; BAC47746.
DR KEGG; bja:bll2481; -.
DR PATRIC; fig|224911.5.peg.2434; -.
DR eggNOG; COG0408; Bacteria.
DR HOGENOM; CLU_026169_0_1_5; -.
DR InParanoid; Q89SC2; -.
DR OMA; HDKGTLF; -.
DR PhylomeDB; Q89SC2; -.
DR UniPathway; UPA00251; UER00322.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004109; F:coproporphyrinogen oxidase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..316
FT /note="Oxygen-dependent coproporphyrinogen-III oxidase"
FT /id="PRO_0000109886"
FT REGION 281..316
FT /note="Important for dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 137
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
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 149..151
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 185
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 216
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT BINDING 299..301
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT SITE 216
FT /note="Important for dimerization"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
SQ SEQUENCE 316 AA; 35498 MW; 8698744018E989CF CRC64;
MVGTAQGRLC PPYGRSVREL NMDVSTIEDR KTRARAWFEA LRDDICASFE RLEDDAPQGL
YPGEAGRFTR TPWQRTDHSG AAGGGGVMSM MSGRLFEKVG VHCSTVHGEF APEFRAQIPG
AADDPRFWAS GISLIAHLRN PHVPAVHMNT RFVVTTKAWF GGGADLTPVL DRRRTQDDAD
SIAFHAAMKE ACVQPNGVAD YDKYKKWCDE YFYLPHRKEA RGIGGIFYDW HDSGDWDADL
AFTQDVGRAF LKIYPDIVRR NFASAWTAAD REEQLIRRGR YVEFNLLYDR GTIFGLKTGG
NVDSILSSLP PEVKWP
