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Annotation rule MF_01608
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General rule information [?]

Accession MF_01608
Dates 18-FEB-2005 (Created)
19-NOV-2019 (Last updated, Version 24)
Name CoA_diS_reduct
Scope
Bacteria; Staphylococcus
Template O52582 (CDR_STAA8)

Propagated annotation [?]


Identifier, protein and gene names [?]

Identifier
CDR
Protein name
RecName: Full=Coenzyme A disulfide reductase;
Short=CoA-disulfide reductase;
Short=CoADR;
EC 1.8.1.14;
Gene name
cdr

Comments [?]

Function Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide.
Catalytic activity RHEA:14705: 2 CoA + NADP(+) = CoA-disulfide + H(+) + NADPH
EC 1.8.1.14
Cofactor FAD
Note: Binds 1 FAD per subunit.
Subunit Homodimer.
Domain Contains 2 FAD binding domains and a single NADPH binding domain.
Miscellaneous Reduction of disulfides occurs by a thiol-disulfide exchange reaction, but involves only a single catalytic cysteine residue that forms a stable mixed disulfide with CoA during catalysis.
Similarity Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family.

Keywords [?]


Gene Ontology [?]

GO:0050451; Molecular function: CoA-disulfide reductase activity.
GO:0050660; Molecular function: flavin adenine dinucleotide binding.
GO:0050661; Molecular function: NADP binding.
GO:0003756; Molecular function: protein disulfide isomerase activity.

Cross-references [?]

Pfam PF07992; Pyr_redox_2; 1;
PF02852; Pyr_redox_dim; 1;
PRINTS PR00368; FADPNR; 1;
PR00411; PNDRDTASEI; 1;
TIGRFAMs TIGR03385; CoA_CoA_reduc; 1;

Features [?]

From: CDR_STAA8 (O52582)
Key     From     To       Description   Tag   Condition   FTGroup
NP_BIND     8     33       FAD        
NP_BIND     151     166       NADP        
NP_BIND     267     277       FAD        
ACT_SITE     43     43       Nucleophile     C  
ACT_SITE     43     43       Redox-active     C  
BINDING     15     15       Substrate     T  
BINDING     19     19       Substrate     Q  
BINDING     22     22       Substrate     R  
BINDING     39     39       Substrate     S  
BINDING     42     42       Substrate     N  
BINDING     71     71       Substrate     K  
BINDING     299     299       Substrate     H  
BINDING     419     419       FAD; via carbonyl oxygen     Y  
BINDING     427     427       Substrate     K  

Additional information [?]

Size range 438-440 amino acids
Related rules None
Fusion None