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Annotation rule MF_01608 |
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) |
Triggered by |
Identifier |
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Protein name |
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Gene name |
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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. |
Pfam | PF07992; Pyr_redox_2; 1; |
PF02852; Pyr_redox_dim; 1; | |
PRINTS | PR00368; FADPNR; 1; |
PR00411; PNDRDTASEI; 1; | |
TIGRFAMs | TIGR03385; CoA_CoA_reduc; 1; |
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 |
Size range | 438-440 amino acids |
Related rules | None |
Fusion | None |