Reviewed,
UniProtKB/Swiss-Prot Q92J42 (ODO1_RICCN)
Last modified
November 25, 2008.
Version 40.
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 |
| ||||
| Organism | Rickettsia conorii [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 781 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Rickettsiaceae › Rickettsieae › Rickettsia › spotted fever group |
Protein attributes
| Sequence length | 928 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: InterPro oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: InterPro thiamin pyrophosphate 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 – 928 | 928 | 2-oxoglutarate dehydrogenase E1 component | PRO_0000162195 | |||
Sequences
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References
| [1] | "Mechanisms of evolution in Rickettsia conorii and R. prowazekii." Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D. Science 293:2093-2098(2001) [PubMed: 11557893] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC VR-613 / Malish 7. |
Cross-references
Sequence databases | |
|---|---|
| AE008590 Genomic DNA. Translation: AAL02765.1. | |
| PIR | C97728. |
| RefSeq | NP_359864.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 927961. |
| GenomeReviews | Gene locus RC0227 in contig AE006914_GR. |
| KEGG | rco:RC0227. |
| NMPDR | fig|272944.1.peg.227. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q92J42. |
Enzyme and pathway databases | |
| BioCyc | RCON272944:RC0227-MON. |
Family and domain databases | |
| 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_RICCN | ||||||||
| Accession | Primary (citable) accession number: Q92J42 | ||||||||
| 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
| Rickettsia conorii (strain Malish 7): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

Clusters with


