Reviewed,
UniProtKB/Swiss-Prot Q9V035 (AOR_PYRAB)
Last modified
June 16, 2009.
Version 53.
History...
Clusters with 100%,
90%,
50% identity |
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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: Tungsten-containing aldehyde ferredoxin oxidoreductase EC=1.2.7.5 | ||||||
| Gene names |
| ||||||
| Organism | Pyrococcus abyssi [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 29292 [NCBI] | ||||||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus |
Protein attributes
| Sequence length | 607 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | An aldehyde + H2O + 2 oxidized ferredoxin = an acid + 2 H+ + 2 reduced ferredoxin. |
| Cofactor | Binds 1 4Fe-4S cluster per subunit By similarity. Binds 1 tungstopterin cofactor per subunit By similarity. |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the AOR/FOR family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | 4Fe-4S Iron Iron-sulfur Metal-binding Tungsten |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW aldehyde ferredoxin oxidoreductase activityInferred from electronic annotation. Source: EC electron carrier activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 607 | 607 | Tungsten-containing aldehyde ferredoxin oxidoreductase | PRO_0000064605 | |||
Sequences
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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 | |
|---|---|
| AJ248286 Genomic DNA. Translation: CAB49871.1. | |
| PIR | B75071. |
| RefSeq | NP_126640.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AOR based on UniProtKB Q51739. |
| SMR | Q9V035. Positions 1-606. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1496313. |
| GenomeReviews | Gene locus PYRAB09630 in contig AL096836_GR. |
| KEGG | pab:PAB0647. |
| NMPDR | fig|272844.1.peg.1006. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9V035. |
| OMA | Q9V035. CTIACGR. |
Enzyme and pathway databases | |
| BioCyc | PABY272844:PAB0647-MON. |
| BRENDA | 1.2.7.5. 262861. |
Family and domain databases | |
| InterPro | IPR013985. Ald_Fedxn_OxRdtase_3. IPR013983. Ald_Fedxn_OxRdtase_N. IPR001203. OxRdtase_Ald_Fedxn_C. [Graphical view] |
| Gene3D | G3DSA:1.10.599.10. Oxred_Ald_Fedxn_3. 1 hit. G3DSA:3.60.9.10. Oxred_Ald_Fedxn_N. 1 hit. |
| Pfam | PF01314. AFOR_C. 1 hit. PF02730. AFOR_N. 1 hit. [Graphical view] |
| SMART | SM00790. AFOR_N. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AOR_PYRAB | ||||||||
| Accession | Primary (citable) accession number: Q9V035 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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