位置:首页 > 蛋白库 > HEM6_BRUA1
HEM6_BRUA1
ID   HEM6_BRUA1              Reviewed;         303 AA.
AC   B2S710;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 78.
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=BAbS19_I14640;
OS   Brucella abortus (strain S19).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=430066;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S19;
RX   PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA   Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S.,
RA   Bricker B., Yu G., Du L., Sobral B.W.;
RT   "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT   virulent strains yields candidate virulence genes.";
RL   PLoS ONE 3:E2193-E2193(2008).
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; CP000887; ACD72957.1; -; Genomic_DNA.
DR   RefSeq; WP_002964654.1; NC_010742.1.
DR   AlphaFoldDB; B2S710; -.
DR   SMR; B2S710; -.
DR   EnsemblBacteria; ACD72957; ACD72957; BAbS19_I14640.
DR   GeneID; 45052547; -.
DR   GeneID; 55591189; -.
DR   KEGG; bmc:BAbS19_I14640; -.
DR   HOGENOM; CLU_026169_0_1_5; -.
DR   OMA; HDKGTLF; -.
DR   UniPathway; UPA00251; UER00322.
DR   Proteomes; UP000002565; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004109; F:coproporphyrinogen oxidase activity; IEA:UniProtKB-UniRule.
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; 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.
FT   CHAIN           1..303
FT                   /note="Oxygen-dependent coproporphyrinogen-III oxidase"
FT                   /id="PRO_1000119786"
FT   REGION          43..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          268..303
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   ACT_SITE        130
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         116
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         120
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         130
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         132..134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         168
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         199
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         286..288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   SITE            199
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
SQ   SEQUENCE   303 AA;  35111 MW;  65C4C1B754D13CE0 CRC64;
     MKREDIPAII PADIEEKKKA AQSWFEELRD RICASYEQLE DELQGPLSDR EPGRFVRTPW
     QKDDGNGGGV MSIMHGRVFE KVGVHVSTVH GEFSPEFRKQ IPGAEEDPRY WASGISLIAH
     PQNPNVPAVH MNTRMIVTTR QWFAGGADLT PVLDRRRTQE DPDTLAFHKA FRFICEKHKD
     IVDYQRLKEW CDEYFFLPHR DEPRGIGGIF YDWLHSPEEK GGWDSDFAFT RDVGRGFSVV
     YPHLVRQNFN KDWTEADRDE QLIRRGRYVE FNLLYDRGTI FGLKTGGNMN AILSSMPPVV
     KWP
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024