 |
|
| Annotation rule MF_01608 |
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) |
| Triggered by |
Propagated annotation
[?]
Identifier, protein and gene names
[?]
| Identifier |
|
| Protein name |
|
||||||||||||||||
| Gene name |
|
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.
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 |