O61199 (ODO1_CAEEL) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 90.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·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 |
| ||
| Organism | Caenorhabditis elegans [Reference proteome] | ||
| Taxonomic identifier | 6239 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Ecdysozoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis![]() |
Protein attributes
| Sequence length | 1029 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
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 Direct protein sequencing 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 | ? – 1029 | 2-oxoglutarate dehydrogenase, mitochondrial | PRO_0000234100 | |||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2. |
| [2] | Bienvenut W.V. Submitted (MAR-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 126-146; 297-317; 320-328; 372-391; 504-514; 548-565; 622-633; 673-680; 910-918; 975-984 AND 992-1002, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | FO081256 Genomic DNA. Translation: CCD70240.1. |
| PIR | T15098. |
| RefSeq | NP_500617.1. NM_068216.4. |
| UniGene | Cel.17820. |
3D structure databases | |
| ProteinModelPortal | O61199. |
| SMR | O61199. Positions 138-1019. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O61199. 1 interaction. |
| STRING | 6239.T22B11.5. |
Proteomic databases | |
| PaxDb | O61199. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblMetazoa | T22B11.5.1; T22B11.5.1; T22B11.5. T22B11.5.2; T22B11.5.2; T22B11.5. |
| GeneID | 177235. |
| KEGG | cel:CELE_T22B11.5. |
| UCSC | T22B11.5. c. elegans. |
Organism-specific databases | |
| CTD | 177235. |
| WormBase | T22B11.5; CE28486; WBGene00020679. |
Phylogenomic databases | |
| eggNOG | COG0567. |
| GeneTree | ENSGT00530000063092. |
| HOGENOM | HOG000259586. |
| InParanoid | O61199. |
| 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... |
Other | |
| NextBio | 895922. |
Entry information
| Entry name | ODO1_CAEEL | ||||||||
| Accession | Primary (citable) accession number: O61199 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Caenorhabditis annotation project | ||||||||
Relevant documents
| Caenorhabditis elegans Caenorhabditis elegans: entries, gene names and cross-references to WormBase |
| SIMILARITY comments Index of protein domains and families |

Clusters with
