P86231 (ODO1_MESAU) Reviewed, UniProtKB/Swiss-Prot
Last modified
October 3, 2012.
Version 10.
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 | Mesocricetus auratus (Golden hamster) | ||
| Taxonomic identifier | 10036 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Cricetidae › Cricetinae › Mesocricetus![]() |
Protein attributes
| Sequence length | 180 AA. |
| Sequence status | Fragments. |
| 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 |
| Enzyme regulation | Catabolite repressed By similarity. UniProtKB Q02218 |
| Subcellular location | Mitochondrion matrix By similarity UniProtKB Q02218. |
| Sequence similarities | Belongs to the alpha-ketoglutarate dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Mitochondrion |
| Ligand | Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred 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 |
| Molecular_function | oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: EC 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›180 | ›180 | 2-oxoglutarate dehydrogenase, mitochondrial | PRO_0000394738 | |||||
Experimental info | |||||||||
| Non-adjacent residues | 10 – 11 | 2 | |||||||
| Non-adjacent residues | 41 – 42 | 2 | |||||||
| Non-adjacent residues | 54 – 55 | 2 | |||||||
| Non-adjacent residues | 64 – 65 | 2 | |||||||
| Non-adjacent residues | 75 – 76 | 2 | |||||||
| Non-adjacent residues | 84 – 85 | 2 | |||||||
| Non-adjacent residues | 94 – 95 | 2 | |||||||
| Non-adjacent residues | 102 – 103 | 2 | |||||||
| Non-adjacent residues | 142 – 143 | 2 | |||||||
| Non-adjacent residues | 149 – 150 | 2 | |||||||
| Non-adjacent residues | 158 – 159 | 2 | |||||||
| Non-terminal residue | 180 | 1 | |||||||
Sequences
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References
| [1] | "Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa." Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S. Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY. |
Cross-references
Entry information
| Entry name | ODO1_MESAU | ||||||||
| Accession | Primary (citable) accession number: P86231 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
