ID   CDR_STAA9               Reviewed;         438 AA.
AC   A5IRE8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 18.
DE   RecName: Full=Coenzyme A disulfide reductase;
DE            Short=CoA-disulfide reductase;
DE            Short=CoADR;
DE            EC=1.8.1.14;
GN   Name=cdr; OrderedLocusNames=SaurJH9_0970;
OS   Staphylococcus aureus (strain JH9).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=359786;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Tomasz A., Richardson P.;
RT   "Complete sequence of chromosome of Staphylococcus aureus subsp.
RT   aureus JH9.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes specifically the NADPH-dependent reduction of
CC       coenzyme A disulfide (By similarity).
CC   -!- CATALYTIC ACTIVITY: 2 CoA + NAD(P)(+) = CoA-disulfide + NAD(P)H.
CC   -!- COFACTOR: Binds 1 FAD per subunit (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- DOMAIN: Contains 2 FAD binding domains and a single NADPH binding
CC       domain (By similarity).
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
CC       catalysis (By similarity).
CC   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family.
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DR   EMBL; CP000703; ABQ48771.1; -; Genomic_DNA.
DR   RefSeq; YP_001246347.1; -.
DR   GeneID; 5167147; -.
DR   GenomeReviews; CP000703_GR; SaurJH9_0970.
DR   KEGG; saj:SaurJH9_0970; -.
DR   OMA; A5IRE8; IVTEYNF.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0050451; F:CoA-disulfide reductase activity; IEA:HAMAP.
DR   GO; GO:0050660; F:FAD binding; IEA:HAMAP.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:HAMAP.
DR   GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006467; P:protein thiol-disulfide exchange; IEA:HAMAP.
DR   HAMAP; MF_01608; -; 1.
DR   InterPro; IPR017758; CoA_disulphide_reductase.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   Gene3D; G3DSA:3.30.390.30; Pyr_redox_dim; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   Pfam; PF02852; Pyr_redox_dim; 1.
DR   PRINTS; PR00368; FADPNR.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR03385; CoA_CoA_reduc; 1.
PE   3: Inferred from homology;
KW   Complete proteome; FAD; Flavoprotein; NADP; Oxidoreductase;
KW   Redox-active center.
FT   CHAIN         1    438       Coenzyme A disulfide reductase.
FT                                /FTId=PRO_1000088036.
FT   NP_BIND       8     33       FAD (By similarity).
FT   NP_BIND     151    166       NADP (By similarity).
FT   NP_BIND     267    277       FAD (By similarity).
FT   ACT_SITE     43     43       Nucleophile (By similarity).
FT   ACT_SITE     43     43       Redox-active (By similarity).
FT   BINDING      15     15       Substrate (By similarity).
FT   BINDING      19     19       Substrate (By similarity).
FT   BINDING      22     22       Substrate (By similarity).
FT   BINDING      39     39       Substrate (By similarity).
FT   BINDING      42     42       Substrate (By similarity).
FT   BINDING      71     71       Substrate (By similarity).
FT   BINDING     299    299       Substrate (By similarity).
FT   BINDING     419    419       FAD; via carbonyl oxygen (By similarity).
FT   BINDING     427    427       Substrate (By similarity).
SQ   SEQUENCE   438 AA;  49285 MW;  FD8651CB1B6E37FE CRC64;
     MPKIVVVGAV AGGATCASQI RRLDKESDII IFEKDRDMSF ANCALPYVIG EVVEDRKYAL
     VYTPEKFYDR KQITVKTYHE VIAINDERQT VTVLNRKTNE QFEESYDKLI LSPGASANSL
     GFESDITFTL RNLEDTDAID QFIKANQVDK VLVIGAGYVS LEVLENLYER GLHPTLIHRS
     DKINKLMDAD MNQPILDELD KREIPYRLNE EIDAINGNEI TFKSGKVEHY DMIIEGVGTH
     PNSKLIESSN IKLDRKGFIP VNDKFETNVP NIYAIGDIAT SHYRHVDLPA SVPLAWGAHR
     AASIVAEQIA GNDTIEFKGF LGNNIVKFFD YTFASVGVKP NELKQFDYKM VEVTQGAHAN
     YYPGNSPLHL RVYYDTSNRQ ILRAAAVGKE GADKRIDVLS MAMMNQLTVD ELTEFEVAYA
     PPYSHPKDLI NMIGYKAK
//