Reviewed,
UniProtKB/Swiss-Prot O58778 (AOR_PYRHO)
Last modified
November 25, 2008.
Version 51.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
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 horikoshii [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 53953 [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 + H(2)O + 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_0000064607 | |||
Sequences
| ||||||||||||||||||
References
| [1] | "Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3." Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. Kikuchi H.DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: OT3. |
Cross-references
Sequence databases | |
|---|---|
| BA000001 Genomic DNA. Translation: BAA30116.1. | |
| PIR | F71094. |
| RefSeq | NP_142931.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AOR based on UniProtKB Q51739. |
| SMR | O58778. Positions 1-606. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1443341. |
| GenomeReviews | Gene locus PH1019 in contig BA000001_GR. |
| KEGG | pho:PH1019. |
| NMPDR | fig|70601.1.peg.994. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O58778. |
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_PYRHO | ||||||||
| Accession | Primary (citable) accession number: O58778 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


