HAMAP rule MF_01608
General rule information
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Accession | MF_01608 |
Dates | 18-FEB-2005 (Created)
25-APR-2024 (Last updated, Version 29) |
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 (NADPH) 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 |