Reviewed,
UniProtKB/Swiss-Prot Q8CPT6 (CDR_STAES)
Last modified
June 16, 2009.
Version 42.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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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 epidermidis (strain ATCC 12228) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 176280 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 438 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 or NADPH bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 438 | 438 | Coenzyme A disulfide reductase HAMAP MF_01608 | PRO_0000184695 | |||||
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] | "Genome-based analysis of virulence genes in a non-biofilm-forming Staphylococcus epidermidis strain (ATCC 12228)." Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M. Mol. Microbiol. 49:1577-1593(2003) [PubMed: 12950922] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AE015929 Genomic DNA. Translation: AAO04266.1. | |
| RefSeq | NP_764224.1. |
3D structure databases | |
| SMR | Q8CPT6. Positions 3-438. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1057913. |
| GenomeReviews | Gene locus SE_0669 in contig AE015929_GR. |
| KEGG | sep:SE0669. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8CPT6. |
| OMA | Q8CPT6. IVTEYNF. |
Enzyme and pathway databases | |
| BioCyc | SEPI176280:SE_0669-MON. |
Family and domain databases | |
| HAMAP | MF_01608. [Tree] |
| InterPro | IPR017758. CoA_disulphide_reductase. IPR013027. FAD_pyr_nucl-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. |
| ProDom | PD000139. FAD_pyr_redox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR03385. CoA_CoA_reduc. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | CDR_STAES | ||||||||
| Accession | Primary (citable) accession number: Q8CPT6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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