ID B9DIS5_STACT Unreviewed; 440 AA.
AC B9DIS5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Coenzyme A disulfide reductase {ECO:0000256|HAMAP-Rule:MF_01608};
DE Short=CoA-disulfide reductase {ECO:0000256|HAMAP-Rule:MF_01608};
DE Short=CoADR {ECO:0000256|HAMAP-Rule:MF_01608};
DE EC=1.8.1.14 {ECO:0000256|HAMAP-Rule:MF_01608};
GN Name=cdr {ECO:0000256|HAMAP-Rule:MF_01608,
GN ECO:0000313|EMBL:CAL27492.1};
GN OrderedLocusNames=Sca_0578 {ECO:0000313|EMBL:CAL27492.1};
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513 {ECO:0000313|EMBL:CAL27492.1, ECO:0000313|Proteomes:UP000000444};
RN [1] {ECO:0000313|EMBL:CAL27492.1, ECO:0000313|Proteomes:UP000000444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300 {ECO:0000313|EMBL:CAL27492.1,
RC ECO:0000313|Proteomes:UP000000444};
RX PubMed=19060169; DOI=10.1128/AEM.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
CC -!- FUNCTION: Catalyzes specifically the NADPH-dependent reduction of
CC coenzyme A disulfide. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01608};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01608};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01608};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01608}.
CC -!- DOMAIN: Contains 2 FAD binding domains and a single NADPH binding
CC domain. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01608}.
CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00009130,
CC ECO:0000256|HAMAP-Rule:MF_01608}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01608}.
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DR EMBL; AM295250; CAL27492.1; -; Genomic_DNA.
DR RefSeq; WP_015899836.1; NC_012121.1.
DR AlphaFoldDB; B9DIS5; -.
DR KEGG; sca:SCA_0578; -.
DR eggNOG; COG0446; Bacteria.
DR HOGENOM; CLU_003291_1_3_9; -.
DR OrthoDB; 9802028at2; -.
DR BioCyc; SCAR396513:SCA_RS02955-MONOMER; -.
DR Proteomes; UP000000444; Chromosome.
DR GO; GO:0050451; F:CoA-disulfide reductase (NADP) 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 Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR HAMAP; MF_01608; CoA_diS_reduct; 1.
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 PANTHER; PTHR43429:SF1; COENZYME A DISULFIDE REDUCTASE; 1.
DR PANTHER; PTHR43429; PYRIDINE NUCLEOTIDE-DISULFIDE OXIDOREDUCTASE DOMAIN-CONTAINING; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR Pfam; PF02852; Pyr_redox_dim; 1.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF55424; FAD/NAD-linked reductases, dimerisation (C-terminal) domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01608};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP-
KW Rule:MF_01608};
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_01608};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01608}; Redox-active center {ECO:0000256|HAMAP-Rule:MF_01608}.
FT DOMAIN 3..286
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
FT DOMAIN 325..424
FT /note="Pyridine nucleotide-disulphide oxidoreductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF02852"
FT ACT_SITE 43
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01608"
FT ACT_SITE 43
FT /note="Redox-active"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01608"
FT BINDING 8..33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01608"
FT BINDING 15
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01608"
FT BINDING 19
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01608"
FT BINDING 22
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01608"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01608"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01608"
FT BINDING 151..166
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01608"
FT BINDING 267..277
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01608"
FT BINDING 299
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01608"
FT BINDING 419
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01608"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01608"
SQ SEQUENCE 440 AA; 49654 MW; ECA7A3AA3385E50A CRC64;
MTKIIIIGGV AGGATFASQL RRLDPDCDIT IFEKDRDVTF ANCGLPYYLG NIIDDRSELL
HFTPEQFKEN KGVTAKVFHE VIQVDPNNQT VTVKNLKTDE VFTEDYDYLV MSPGCRANQL
PLNSDMAFTL RNLEDTDDIE SYISNNNVKK APIIGAGYIS LEVLENLYNR GIQTTLIHRS
EQINKLMDQD MNKVIFDEMD KRQIDYRLNE EVDSVDGHTV HFKSGNTEDF DIIIEGIGIK
PNTEFLEGAG IEEDDAGYIP VNEYFQTNYR NVYAIGDIVS NYYRHVNIPT HVPLAWGAHR
GASIVAEHIT QTRNVPFKGF LASNAVKFFD YTLTSVGVSP SDLKHFDYTM VETEQMNHAG
YYPGAEPLHL RVYFENKSRK ILRAAAAGKS GADKRIDILS MAMQNDMTVD ELTEFESAYA
PPFSSPKDII NMIGYKAQNK
//
