Q623T0 (ODO1_CAEBR) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 58.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 2-oxoglutarate dehydrogenase, mitochondrial EC=1.2.4.2 Alternative name(s): 2-oxoglutarate dehydrogenase complex component E1 Short name=OGDC-E1 Alpha-ketoglutarate dehydrogenase | ||
| Gene names |
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| Organism | Caenorhabditis briggsae [Reference proteome] | ||
| Taxonomic identifier | 6238 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis |
Protein attributes
| Sequence length | 1027 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| 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 CO2. It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. UniProtKB Q02218 |
| Catalytic activity | 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2. UniProtKB Q02218 |
| Cofactor | Thiamine pyrophosphate By similarity. UniProtKB Q02218 |
| Subcellular location | Mitochondrion matrix By similarity. |
| Sequence similarities | Belongs to the alpha-ketoglutarate dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | generation of precursor metabolites and energy Inferred from sequence or structural similarity. Source: UniProtKB glycolysisInferred from electronic annotation. Source: UniProtKB-KW tricarboxylic acid cycleInferred from electronic annotation. Source: InterPro |
| Cellular_component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial membraneInferred from sequence or structural similarity. Source: UniProtKB |
| Molecular_function | oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from sequence or structural similarity. Source: UniProtKB thiamine 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 | ||||||
|---|---|---|---|---|---|---|
| Transit peptide | 1 – ? | Mitochondrion | ||||
| Chain | ? – 1027 | 2-oxoglutarate dehydrogenase, mitochondrial | PRO_0000234099 | |||
Sequences
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References
| [1] | "The genome sequence of Caenorhabditis briggsae: a platform for comparative genomics." Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N., Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P., Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W., Hillier L.W.  Waterston R.H.PLoS Biol. 1:166-192(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AF16. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | HE601298 Genomic DNA. Translation: CAP22897.1. |
| RefSeq | XP_002634170.1. XM_002634124.1. |
3D structure databases | |
| ProteinModelPortal | Q623T0. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 6238.CBG01737. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | CBG01737; CBG01737; CBG01737. |
| GeneID | 8576165. |
| KEGG | cbr:CBG01737. |
Organism-specific databases | |
| CTD | 8576165. |
| WormBase | CBG01737; CBP00459; WBGene00024926. |
Phylogenomic databases | |
| eggNOG | COG0567. |
| HOGENOM | HOG000259586. |
| KO | K00164. |
| OMA | IIKRGGA. |
Family and domain databases | |
| InterPro | IPR011603. 2oxoglutarate_DH_E1. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [Graphical view] |
| PANTHER | PTHR23152. PTHR23152. 1 hit. |
| Pfam | PF00676. E1_dh. 1 hit. PF02779. Transket_pyr. 1 hit. [Graphical view] |
| PIRSF | PIRSF000157. Oxoglu_dh_E1. 1 hit. |
| SMART | SM00861. Transket_pyr. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00239. 2oxo_dh_E1. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ODO1_CAEBR | ||||||||
| Accession | Primary (citable) accession number: Q623T0 Secondary accession number(s): A8WQY9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Caenorhabditis annotation project | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |