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CDR_STAAC
ID   CDR_STAAC               Reviewed;         438 AA.
AC   Q5HHB4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 113.
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=SACOL0975;
OS   Staphylococcus aureus (strain COL).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93062;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=COL;
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; CP000046; AAW37942.1; -; Genomic_DNA.
DR   RefSeq; WP_001124519.1; NC_002951.2.
DR   AlphaFoldDB; Q5HHB4; -.
DR   SMR; Q5HHB4; -.
DR   EnsemblBacteria; AAW37942; AAW37942; SACOL0975.
DR   KEGG; sac:SACOL0975; -.
DR   HOGENOM; CLU_003291_1_3_9; -.
DR   OMA; DKNHTNY; -.
DR   Proteomes; UP000000530; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..438
FT                   /note="Coenzyme A disulfide reductase"
FT                   /id="PRO_0000184689"
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;  49291 MW;  673D6F6BEEE8EEF8 CRC64;
     MPKIVVVGAV AGGATCASQI RRLDKESDII IFEKDRDMSF ANCALPYVIG EVVEDRRYAL
     AYTPEEFYDR KQITVKTYHE VIAINDERQT VSVLNRKTNE QFEESYDKLI LSPGASANSL
     GFESDITFTL RNLEDTDAID QFIKANQVDK VLVVGAGYVS LEVLENLYER GLHPTLIHRS
     DKINKLMDAD MNQPILDELD KREIPYRLNE EINAINGNEI TFKSGKVEHY DMIIEGVGTH
     PNSKFIESSN IKLDRKGFIP VNDKFETNVP NIYAIGDIAT SHYRHVDLPA SVPLAWGAHR
     AASIVAEQIA GNDTIEFKGF LGNNIVKFFD YTFASVGVKP NELKQFDYKM VEVTQGAHAN
     YYPGNSPLHL RVYYDTSNRQ ILRAAAVGKE GADKRIDVLS MAMMNQLTVD ELTEFEVAYA
     PPYSHPKDLI NMIGYKAK
 
 
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