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CDR_STAS1
ID   CDR_STAS1               Reviewed;         440 AA.
AC   Q49WB0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=SSP1804;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18949.1; -; Genomic_DNA.
DR   RefSeq; WP_011303499.1; NZ_MTGA01000039.1.
DR   AlphaFoldDB; Q49WB0; -.
DR   SMR; Q49WB0; -.
DR   STRING; 342451.SSP1804; -.
DR   EnsemblBacteria; BAE18949; BAE18949; SSP1804.
DR   GeneID; 66867978; -.
DR   KEGG; ssp:SSP1804; -.
DR   eggNOG; COG0446; Bacteria.
DR   HOGENOM; CLU_003291_1_3_9; -.
DR   OMA; DKNHTNY; -.
DR   OrthoDB; 1149616at2; -.
DR   Proteomes; UP000006371; 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; 3.50.50.60; -; 3.
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..440
FT                   /note="Coenzyme A disulfide reductase"
FT                   /id="PRO_0000289963"
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   440 AA;  49473 MW;  86317B7DB21F669D CRC64;
     MNKIVVVGAV AGGATVASQI RRLDQESEIV VFEKDRDMSF ANCALPYYLG NVVDSRNKVL
     EATPESFYEA KNIVVKPCHK VTSINDTENT ITVYDRIQDT YFETHYDTLI LSPGCSANSL
     NLDSPIAFTL RNMEDTDAIE TFIKENQVKN ALVVGTGYIG LEILDNLYER GISPTLIHRS
     THINKLMDQD MNQAILDEMD KRDIHYRFNE EISKVVGNAV HFESGKVENY DLIIEGVGVK
     PNSEFIKNSN VTLDDKGYIP VNDQFQTNIP NIYALGDIIT SHYRHVDLNA HVPLAWGAHR
     GASVIAEQLA GDHKIHFKGY LGSNIVKFFD YTFASVGVSP KELSNFDYAM VEANQGEHAG
     YYPGNTKLHL RVYFDKTNRR IIRAAAVGMK GVDKRIDVLS MAMMHKLTID ELVEFEVAYA
     PPYSRPKDII NMIGYKARNK
 
 
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