HAMAP rule MF_01608
General rule information
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| Accession | MF_01608 |
| Dates | 18-FEB-2005 (Created)
28-JUL-2023 (Last updated, Version 28) |
| Name | CoA_diS_reduct |
| Scope(s) |
Bacteria Staphylococcus |
| Template(s) | O52582 (CDR_STAA8); [ Recover all ] |
| Triggered by |
HAMAP; MF_01608 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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| Identifier | CDR |
| Protein name | RecName: Full=Coenzyme A disulfide reductase; Short=CoA-disulfide reductase; Short=CoADR; EC=1.8.1.14; |
| Gene name | Name=cdr; |
Comments
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| FUNCTION | Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide. |
| CATALYTIC ACTIVITY | Reaction=2 CoA + NADP(+) = CoA-disulfide + H(+) + NADPH; Xref=Rhea:RHEA:14705, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:62209; EC=1.8.1.14; |
| COFACTOR | Name=FAD; Xref=ChEBI:CHEBI:57692; 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
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Gene Ontology
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| GO:0050451; Molecular function:CoA-disulfide reductase (NADP) 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
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| Pfam | PF07992; Pyr_redox_2; 1; |
| Pfam | PF02852; Pyr_redox_dim; 1; |
| PRINTS | PR00368; FADPNR; 1; |
| PRINTS | PR00411; PNDRDTASEI; 1; |
| NCBIfam | TIGR03385; CoA_CoA_reduc; 1; |
Features
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| From: CDR_STAA8 (O52582) | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| BINDING | 8 | 33 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
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| BINDING | 151 | 166 | /ligand="NADP(+)" /ligand_id="ChEBI:CHEBI:58349" |
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| BINDING | 267 | 277 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
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| ACT_SITE | 43 | 43 | /note="Nucleophile" | C | ||||||||
| ACT_SITE | 43 | 43 | /note="Redox-active" | C | ||||||||
| BINDING | 15 | 15 | /ligand="substrate" | T | ||||||||
| BINDING | 19 | 19 | /ligand="substrate" | Q | ||||||||
| BINDING | 22 | 22 | /ligand="substrate" | R | ||||||||
| BINDING | 39 | 39 | /ligand="substrate" | S | ||||||||
| BINDING | 42 | 42 | /ligand="substrate" | N | ||||||||
| BINDING | 71 | 71 | /ligand="substrate" | K | ||||||||
| BINDING | 299 | 299 | /ligand="substrate" | H | ||||||||
| BINDING | 419 | 419 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
Y | ||||||||
| BINDING | 427 | 427 | /ligand="substrate" | K | ||||||||
Additional information
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| Size range | 438-440 amino acids |
| Related rules |
None |
| Fusion | Nter: None Cter: None |