Reviewed,
UniProtKB/Swiss-Prot Q2YLS2 (ODO1_BRUA2)
Last modified
November 4, 2008.
Version 23.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
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 abortus (strain 2308) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 359391 [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_1000065698 | |||
Sequences
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References
| [1] | "Whole-genome analyses of speciation events in pathogenic Brucellae." Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E. Infect. Immun. 73:8353-8361(2005) [PubMed: 16299333] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AM040264 Genomic DNA. Translation: CAJ11879.1. | |
| RefSeq | YP_415263.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3788974. |
| GenomeReviews | Gene locus BAB1_1923 in contig AM040264_GR. |
| KEGG | bmf:BAB1_1923. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q2YLS2. |
Enzyme and pathway databases | |
| BioCyc | BMEL359391:BAB1_1923-MON. |
Family and domain databases | |
| HAMAP | MF_01169. [Tree] |
| InterPro | IPR011603. 2oxoglutarate_DHase_E1. IPR001017. DHase_E1. IPR005475. Transketo_Cen_R. [Graphical view] |
| PANTHER | PTHR23152. 2oxoglutarate_DH_E1. 1 hit. |
| Pfam | PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view] |
| PIRSF | PIRSF000157. Oxoglu_dh_E1. 1 hit. |
| TIGRFAMs | TIGR00239. 2oxo_dh_E1. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ODO1_BRUA2 | ||||||||
| Accession | Primary (citable) accession number: Q2YLS2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Brucella abortus strain 2308 Brucella abortus (strain 2308): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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