Reviewed,
UniProtKB/Swiss-Prot Q6GAV6 (CDR_STAAS)
Last modified
December 16, 2008.
Version 32.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Coenzyme A disulfide reductase Short name=CoA-disulfide reductase Short name=CoADR EC=1.8.1.14 | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus (strain MSSA476) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 282459 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 438 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide By similarity. |
| Catalytic activity | 2 CoA + NAD(P)(+) = CoA-disulfide + NAD(P)H. HAMAP MF_01608 |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Domain | Contains 2 FAD binding domains and a single NADPH binding domain By similarity. |
| 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 By similarity. |
| Sequence similarities | Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family. |
Ontologies
Keywords | |
|---|---|
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | cell redox homeostasis Inferred from electronic annotation. Source: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW protein thiol-disulfide exchangeInferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | CoA-disulfide reductase activity Inferred from electronic annotation. Source: HAMAP FAD bindingInferred from electronic annotation. Source: HAMAP NADP bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 438 | 437 | Coenzyme A disulfide reductase HAMAP MF_01608 | PRO_0000184693 | |||||
Regions | |||||||||
| Nucleotide binding | 8 – 33 | 26 | FAD By similarity | ||||||
| Nucleotide binding | 151 – 166 | 16 | NADP By similarity | ||||||
| Nucleotide binding | 267 – 277 | 11 | FAD By similarity | ||||||
Sites | |||||||||
| Active site | 43 | 1 | Nucleophile By similarity | ||||||
| Active site | 43 | 1 | Redox-active By similarity | ||||||
| Binding site | 15 | 1 | Substrate By similarity | ||||||
| Binding site | 19 | 1 | Substrate By similarity | ||||||
| Binding site | 22 | 1 | Substrate By similarity | ||||||
| Binding site | 39 | 1 | Substrate By similarity | ||||||
| Binding site | 42 | 1 | Substrate By similarity | ||||||
| Binding site | 71 | 1 | Substrate By similarity | ||||||
| Binding site | 299 | 1 | Substrate By similarity | ||||||
| Binding site | 419 | 1 | FAD; via carbonyl oxygen By similarity | ||||||
| Binding site | 427 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "Complete genomes of two clinical Staphylococcus aureus strains: evidence for the rapid evolution of virulence and drug resistance." Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J., Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A., Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C., Clark L., Corton C.  Parkhill J.Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004) [PubMed: 15213324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| BX571857 Genomic DNA. Translation: CAG42615.1. | |
| RefSeq | YP_042967.1. |
3D structure databases | |
| SMR | Q6GAV6. Positions 1-437, 2-438. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2863373. |
| GenomeReviews | Gene locus SAS0840 in contig BX571857_GR. |
| KEGG | sas:SAS0840. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q6GAV6. |
Enzyme and pathway databases | |
| BioCyc | SAUR282459:SAS0840-MON. |
Family and domain databases | |
| HAMAP | MF_01608. [Tree] |
| InterPro | IPR017758. CoA_disulphide_reductase. IPR013027. FAD_pyr_nucl-diS_OxRdtase. IPR001100. Pyr_nuc-diS_OxRdtase. IPR004099. Pyr_nucl-diS_OxRdtase_dimer. IPR001327. Pyr_OxRdtase_NAD_bd. [Graphical view] |
| Gene3D | G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit. |
| Pfam | PF00070. Pyr_redox. 1 hit. PF07992. Pyr_redox_2. 1 hit. PF02852. Pyr_redox_dim. 1 hit. [Graphical view] |
| PRINTS | PR00368. FADPNR. PR00411. PNDRDTASEI. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| ProtoNet | Search... |
Entry information
| Entry name | CDR_STAAS | ||||||||
| Accession | Primary (citable) accession number: Q6GAV6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
