Reviewed,
UniProtKB/Swiss-Prot A9M8Q9 (ODO1_BRUC2)
Last modified
November 4, 2008.
Version 9.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 2-oxoglutarate dehydrogenase E1 component EC=1.2.4.2 Alternative name(s): Alpha-ketoglutarate dehydrogenase | ||||||
| Gene names |
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| Organism | Brucella canis (strain ATCC 23365 / NCTC 10854) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 483179 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 1004 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. |
| Catalytic activity | 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO(2). |
| Cofactor | Thiamine pyrophosphate By similarity. |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the alpha-ketoglutarate dehydrogenase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: HAMAP oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: HAMAP thiamin pyrophosphate 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 – 1004 | 1004 | 2-oxoglutarate dehydrogenase E1 component | PRO_1000085385 | |||
Sequences
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References
| [1] | "Brucella canis ATCC 23365 whole genome shotgun sequencing project." Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M., Snyder E.E. Brettin T.S.Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000872 Genomic DNA. Translation: ABX62957.1. | |
| RefSeq | YP_001593728.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 5784073. |
| GenomeReviews | Gene locus BCAN_A1967 in contig CP000872_GR. |
| KEGG | bcs:BCAN_A1967. |
Organism-specific databases | |
| CMR | Search... |
Family and domain databases | |
| HAMAP | MF_01169. [Tree] |
| InterPro | IPR011603. 2oxoglutarate_DHase_E1. [Graphical view] |
| PANTHER | PTHR23152. 2oxoglutarate_DH_E1. 1 hit. |
| PIRSF | PIRSF000157. Oxoglu_dh_E1. 1 hit. |
| TIGRFAMs | TIGR00239. 2oxo_dh_E1. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ODO1_BRUC2 | ||||||||
| Accession | Primary (citable) accession number: A9M8Q9 | ||||||||
| 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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