位置:首页 > 蛋白库 > HEM6_BURP6
HEM6_BURP6
ID   HEM6_BURP6              Reviewed;         307 AA.
AC   A3N7F7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=BURPS668_1229;
OS   Burkholderia pseudomallei (strain 668).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320373;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=668;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000570; ABN85031.1; -; Genomic_DNA.
DR   RefSeq; WP_004526433.1; NC_009074.1.
DR   AlphaFoldDB; A3N7F7; -.
DR   SMR; A3N7F7; -.
DR   EnsemblBacteria; ABN85031; ABN85031; BURPS668_1229.
DR   GeneID; 56526699; -.
DR   KEGG; bpd:BURPS668_1229; -.
DR   HOGENOM; CLU_026169_0_1_4; -.
DR   OMA; HDKGTLF; -.
DR   UniPathway; UPA00251; UER00322.
DR   Proteomes; UP000002153; Chromosome I.
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..307
FT                   /note="Oxygen-dependent coproporphyrinogen-III oxidase"
FT                   /id="PRO_1000019462"
FT   REGION          247..282
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   ACT_SITE        113
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         103
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         113
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         115..117
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         152
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         182
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   BINDING         265..267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
FT   SITE            182
FT                   /note="Important for dimerization"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00333"
SQ   SEQUENCE   307 AA;  34569 MW;  7A5FCC82FA3139A1 CRC64;
     MTDSTYDVNR VRAYLQGLQM RIADALGAFD GTPLAADTWR RGPGERLRGG GCTRILEAGG
     FFERAGIGFS DVAGDALPPS ASASRPQLAG RGFEALGVSL VLHPRNPYCP TVHMNVRMLI
     ATKPGEAPVF WFGGGMDLTP IYGFEEDARH FHRTCRAALE PFGAELYPRF KKWCDDYFFL
     KHRNEARGIG GIFFDDFSEL GFERSFEMLQ SVGDAFLPSY LPIVERRRDT PYGERERAFQ
     AYRRGRYVEF NLVFDRGTLF GLQSGGRTES ILLSMPPTAG WRYDWHPDPG TPEARLQSEF
     LVPRDWA
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024