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CDR_STAES
ID   CDR_STAES               Reviewed;         438 AA.
AC   Q8CPT6;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Coenzyme A disulfide reductase {ECO:0000255|HAMAP-Rule:MF_01608};
DE            Short=CoA-disulfide reductase {ECO:0000255|HAMAP-Rule:MF_01608};
DE            Short=CoADR {ECO:0000255|HAMAP-Rule:MF_01608};
DE            EC=1.8.1.14 {ECO:0000255|HAMAP-Rule:MF_01608};
GN   Name=cdr {ECO:0000255|HAMAP-Rule:MF_01608}; OrderedLocusNames=SE_0669;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: Catalyzes specifically the NADPH-dependent reduction of
CC       coenzyme A disulfide. {ECO:0000255|HAMAP-Rule:MF_01608}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 CoA + NADP(+) = CoA-disulfide + H(+) + NADPH;
CC         Xref=Rhea:RHEA:14705, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62209; EC=1.8.1.14;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01608};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01608};
CC       Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01608};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01608}.
CC   -!- DOMAIN: Contains 2 FAD binding domains and a single NADPH binding
CC       domain. {ECO:0000255|HAMAP-Rule:MF_01608}.
CC   -!- MISCELLANEOUS: Reduction of disulfides occurs by a thiol-disulfide
CC       exchange reaction, but involves only a single catalytic cysteine
CC       residue that forms a stable mixed disulfide with CoA during catalysis.
CC       {ECO:0000255|HAMAP-Rule:MF_01608}.
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family. {ECO:0000255|HAMAP-Rule:MF_01608}.
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DR   EMBL; AE015929; AAO04266.1; -; Genomic_DNA.
DR   RefSeq; NP_764224.1; NC_004461.1.
DR   RefSeq; WP_001829263.1; NZ_WBME01000074.1.
DR   AlphaFoldDB; Q8CPT6; -.
DR   SMR; Q8CPT6; -.
DR   STRING; 176280.SE_0669; -.
DR   EnsemblBacteria; AAO04266; AAO04266; SE_0669.
DR   KEGG; sep:SE_0669; -.
DR   PATRIC; fig|176280.10.peg.644; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_003291_1_3_9; -.
DR   OMA; DKNHTNY; -.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0050451; F:CoA-disulfide reductase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003756; F:protein disulfide isomerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   Gene3D; 3.30.390.30; -; 1.
DR   Gene3D; 3.50.50.60; -; 2.
DR   HAMAP; MF_01608; CoA_diS_reduct; 1.
DR   InterPro; IPR017758; CoA_disulphide_reductase.
DR   InterPro; IPR023536; CoA_disulphide_reductase_staph.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer_sf.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   SUPFAM; SSF55424; SSF55424; 1.
DR   TIGRFAMs; TIGR03385; CoA_CoA_reduc; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; NADP; Oxidoreductase; Redox-active center.
FT   CHAIN           1..438
FT                   /note="Coenzyme A disulfide reductase"
FT                   /id="PRO_0000184695"
FT   ACT_SITE        43
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   ACT_SITE        43
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         8..33
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         22
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         151..166
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         267..277
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         299
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         419
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
FT   BINDING         427
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01608"
SQ   SEQUENCE   438 AA;  49366 MW;  5B27C5462208D91A CRC64;
     MNKIIIVGAV AGGATCASQI RRLDKESEII VFEKDRDMSF ANCALPYYIG NVIEDRRKVL
     AYTPNQFYDK KQITVKTYHE VIQINDERQT VTVLNHQTNQ TFEESYDTLI LSPGASANRL
     NTHSDISFTV RNLEDTETID TFITNTKAQR ALVVGAGYIS LEVLENLHHR GLDVTWIHRS
     TNINKLMDQD MNQPIIDEIE KRNITYRFNE EISHVNGHEV TFTSGKVENF DLIIEGVGTH
     PNSQFIKSSN VILNDKGYIP VNHNFQTNIP NIYALGDVIT SHYRHVNLPA QVPLAWGAHR
     GASIIAEQLS GNSSIHFKGY LGNNIVKFFD YTLASVGIKP NELKNFDYDM VEVKQGAHAG
     YYPGNSPLHL RVYFEKDSRK LIRAAAVGKQ GADKRIDVLS MAMMNNATVD DLTEFEVAYA
     PPYSHPKDLI NLIGYKAQ
 
 
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