AC   MF_01608;
DC   Protein; auto
TR   HAMAP; MF_01608; -; 1; level=0
XX
Names: CoA_diS_reduct
XX
ID   CDR
DE   RecName: Full=Coenzyme A disulfide reductase;
DE            Short=CoA-disulfide reductase;
DE            Short=CoADR;
DE            EC=1.8.1.14;
GN   Name=cdr;
XX
CC   -!- FUNCTION: Catalyzes specifically the NADPH-dependent reduction of
CC       coenzyme A disulfide.
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   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC       Note=Binds 1 FAD per subunit.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- DOMAIN: Contains 2 FAD binding domains and a single NADPH binding
CC       domain.
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   -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide
CC       oxidoreductase family.
XX
DR   Pfam; PF07992; Pyr_redox_2; 1; trigger=no
DR   Pfam; PF02852; Pyr_redox_dim; 1; trigger=no
DR   PRINTS; PR00368; FADPNR; 1; trigger=no
DR   PRINTS; PR00411; PNDRDTASEI; 1; trigger=no
DR   NCBIfam; TIGR03385; CoA_CoA_reduc; 1; trigger=no
XX
KW   FAD
KW   Flavoprotein
KW   NADP
KW   Oxidoreductase
KW   Redox-active center
XX
GO   GO:0050451; F:CoA-disulfide reductase (NADP) activity
GO   GO:0050660; F:flavin adenine dinucleotide binding
GO   GO:0050661; F:NADP binding
GO   GO:0003756; F:protein disulfide isomerase activity
XX
FT   From: CDR_STAA8 (O52582)
FT   BINDING         8..33
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   BINDING         151..166
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT   BINDING         267..277
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   ACT_SITE        43
FT                   /note="Nucleophile"
FT   Condition: C
FT   ACT_SITE        43
FT                   /note="Redox-active"
FT   Condition: C
FT   BINDING         15
FT                   /ligand="substrate"
FT   Condition: T
FT   BINDING         19
FT                   /ligand="substrate"
FT   Condition: Q
FT   BINDING         22
FT                   /ligand="substrate"
FT   Condition: R
FT   BINDING         39
FT                   /ligand="substrate"
FT   Condition: S
FT   BINDING         42
FT                   /ligand="substrate"
FT   Condition: N
FT   BINDING         71
FT                   /ligand="substrate"
FT   Condition: K
FT   BINDING         299
FT                   /ligand="substrate"
FT   Condition: H
FT   BINDING         419
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT   Condition: Y
FT   BINDING         427
FT                   /ligand="substrate"
FT   Condition: K
XX
Size: 438-440;
Related: None;
Template: O52582;
Scope:
 Bacteria; Staphylococcus
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.28 2023/07/28
//