CDR_STAEQ
ID CDR_STAEQ Reviewed; 438 AA.
AC Q5HQI9;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=SERP0560;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW53947.1; -; Genomic_DNA.
DR RefSeq; WP_001829263.1; NC_002976.3.
DR AlphaFoldDB; Q5HQI9; -.
DR SMR; Q5HQI9; -.
DR STRING; 176279.SERP0560; -.
DR EnsemblBacteria; AAW53947; AAW53947; SERP0560.
DR KEGG; ser:SERP0560; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_3_9; -.
DR OMA; DKNHTNY; -.
DR OrthoDB; 1149616at2; -.
DR Proteomes; UP000000531; 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;
KW Reference proteome.
FT CHAIN 1..438
FT /note="Coenzyme A disulfide reductase"
FT /id="PRO_0000184696"
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
