Reviewed,
UniProtKB/Swiss-Prot Q9UYU5 (CDR_PYRAB)
Last modified
June 16, 2009.
Version 47.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
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 | Pyrococcus abyssi [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 29292 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus |
Protein attributes
| Sequence length | 446 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 2 CoA + NAD(P)+ = CoA-disulfide + NAD(P)H. |
| Cofactor | Binds 1 FAD per subunit By similarity. |
| Subunit structure | Homotetramer By similarity. |
| Sequence similarities | Belongs to the class-III pyridine nucleotide-disulfide oxidoreductase family. |
Ontologies
| Keywords | |
|---|---|
| Domain | Redox-active center |
| Ligand | FAD Flavoprotein NAD |
| 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: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular function | CoA-disulfide reductase activity Inferred from electronic annotation. Source: EC FAD bindingInferred from electronic annotation. Source: InterPro NADP or NADPH bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 446 | 446 | Coenzyme A disulfide reductase | PRO_0000184697 | |||||
Regions | |||||||||
| Nucleotide binding | 14 – 39 | 26 | FAD By similarity | ||||||
| Nucleotide binding | 155 – 170 | 16 | NADP By similarity | ||||||
| Nucleotide binding | 274 – 284 | 11 | FAD By similarity | ||||||
Sites | |||||||||
| Active site | 49 | 1 | Nucleophile By similarity | ||||||
| Active site | 49 | 1 | Redox-active By similarity | ||||||
| Binding site | 21 | 1 | Substrate | ||||||
| Binding site | 25 | 1 | Substrate | ||||||
| Binding site | 28 | 1 | Substrate By similarity | ||||||
| Binding site | 45 | 1 | Substrate By similarity | ||||||
| Binding site | 76 | 1 | Substrate | ||||||
| Binding site | 426 | 1 | FAD; via carbonyl oxygen By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi." Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P. Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GE5 / Orsay. |
Cross-references
Sequence databases | |
|---|---|
| AJ248287 Genomic DNA. Translation: CAB50317.1. | |
| PIR | H75052. |
| RefSeq | NP_127087.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NHP based on UniProtKB P37062. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1496802. |
| GenomeReviews | Gene locus PYRAB14120 in contig AL096836_GR. |
| KEGG | pab:PAB0936. |
| NMPDR | fig|272844.1.peg.1495. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9UYU5. |
| OMA | Q9UYU5. DVAETKH. |
Enzyme and pathway databases | |
| BioCyc | PABY272844:PAB0936-MON. |
| BRENDA | 1.8.1.14. 262861. |
Family and domain databases | |
| 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_PYRAB | ||||||||
| Accession | Primary (citable) accession number: Q9UYU5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


