CDR_STAAN
ID CDR_STAAN Reviewed; 438 AA.
AC Q7A6H1;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
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=SA0831;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=N315;
RX PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017;
RA Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y.,
RA Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C.,
RA Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.;
RT "Correlation of proteomic and transcriptomic profiles of Staphylococcus
RT aureus during the post-exponential phase of growth.";
RL J. Microbiol. Methods 60:247-257(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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; BA000018; BAB42070.1; -; Genomic_DNA.
DR PIR; C89864; C89864.
DR RefSeq; WP_001124506.1; NC_002745.2.
DR AlphaFoldDB; Q7A6H1; -.
DR SMR; Q7A6H1; -.
DR SWISS-2DPAGE; Q7A6H1; -.
DR EnsemblBacteria; BAB42070; BAB42070; BAB42070.
DR KEGG; sau:SA0831; -.
DR HOGENOM; CLU_003291_1_3_9; -.
DR OMA; DKNHTNY; -.
DR Proteomes; UP000000751; 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 1: Evidence at protein level;
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_0000184691"
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; 3970317541CFF013 CRC64;
MPKIVVVGAV AGGATCASQI RRLDKESDII IFEKDRDMSF ANCALPYVIG EVVEDRKYAL
AYTPEKFYDR KQITVKTYHE VIAINDERQT VTVLNRKTNE QFEESYDKLI LSPGASANSL
GFESDITFTL RNLEDTDAID QFIKANQVDK VLVIGAGYVS LEVLENLYER GLHPTLIHRS
DKINKLMDAD MNQPILDELD KREIPYRLNE EIDAINGNEI TFKSGKVEHY DMIIEGVGTH
PNSKFIESSN IKLDRKGFIP VNDKFETNVP NIYAIGDIAT SHYRHVDLPA SVPLAWGAHR
AASIVAEQIA GNDTIEFKGF LGNNIVKFFD YTFASVGVKP NELKQFDYKM VEVTQGAHAN
YYPGNSPLHL RVYYDTSNRQ ILRAAAVGKE GADKRIDVLS MAMMNQLTVD ELTEFEVAYA
PPYSHPKDLI NMIGYKAK
