Reviewed,
UniProtKB/Swiss-Prot Q8CUL8 (ODO1_OCEIH)
Last modified
June 16, 2009.
Version 38.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
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 | Oceanobacillus iheyensis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 182710 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Oceanobacillus |
Protein attributes
| Sequence length | 953 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 CO2. 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 + CO2. HAMAP MF_01169 |
| 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 – 953 | 953 | 2-oxoglutarate dehydrogenase E1 component HAMAP MF_01169 | PRO_0000162175 | |||
Sequences
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References
| [1] | "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge and its unexpected adaptive capabilities to extreme environments." Takami H., Takaki Y., Uchiyama I. Nucleic Acids Res. 30:3927-3935(2002) [PubMed: 12235376] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 14371 / JCM 11309 / KCTC 3954 / HTE831. |
Cross-references
Sequence databases | |
|---|---|
| BA000028 Genomic DNA. Translation: BAC13045.1. | |
| RefSeq | NP_692010.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1017056. |
| GenomeReviews | Gene locus OB1089 in contig BA000028_GR. |
| KEGG | oih:OB1089. |
| NMPDR | fig|221109.1.peg.1090. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8CUL8. |
| OMA | Q8CUL8. EGDEPAF. |
Enzyme and pathway databases | |
| BioCyc | OIHE221109:OB1089-MON. |
| BRENDA | 1.2.4.2. 278212. |
Family and domain databases | |
| HAMAP | MF_01169. [Tree] |
| InterPro | IPR011603. 2oxoglutarate_DH_E1. IPR001017. DH_E1. IPR005475. Transketolase_central-reg. [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_OCEIH | ||||||||
| Accession | Primary (citable) accession number: Q8CUL8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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