Q81GF2 (ODO1_BACCR) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 68.
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 E1 component EC=1.2.4.2 Alternative name(s): Alpha-ketoglutarate dehydrogenase | ||||
| Gene names |
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| Organism | Bacillus cereus (strain ATCC 14579 / DSM 31) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 226900 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › ![]() |
Protein attributes
| Sequence length | 955 AA. |
| Sequence status | Complete. |
| 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. HAMAP-Rule MF_01169 |
| Catalytic activity | 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2. HAMAP-Rule MF_01169 |
| Cofactor | Thiamine pyrophosphate By similarity. HAMAP-Rule MF_01169 |
| Subunit structure | Homodimer By similarity. HAMAP-Rule MF_01169 |
| Sequence similarities | Belongs to the alpha-ketoglutarate dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred from electronic annotation. Source: HAMAP tricarboxylic acid cycleInferred from electronic annotation. Source: InterPro |
| Molecular_function | oxoglutarate dehydrogenase (succinyl-transferring) activity Inferred from electronic annotation. Source: HAMAP thiamine 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 – 955 | 955 | 2-oxoglutarate dehydrogenase E1 component HAMAP-Rule MF_01169 | PRO_0000162163 | |||
Sequences
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References
| [1] | "Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. Kyrpides N.C.Nature 423:87-91(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14579 / DSM 31. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016877 Genomic DNA. Translation: AAP08237.1. |
| RefSeq | NP_831036.1. NC_004722.1. |
3D structure databases | |
| ProteinModelPortal | Q81GF2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 226900.BC1252. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAP08237; AAP08237; BC_1252. |
| GeneID | 1203601. |
| KEGG | bce:BC1252. |
| PATRIC | 32598227. VBIBacCer54481_1225. |
Phylogenomic databases | |
| eggNOG | COG0567. |
| KO | K00164. |
| OMA | IIKRGGA. |
| ProtClustDB | PRK09404. |
Enzyme and pathway databases | |
| BioCyc | BCER226900:GJEU-1252-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01169. SucA_OdhA. |
| InterPro | IPR011603. 2oxoglutarate_DH_E1. IPR023784. 2oxoglutarate_DH_E1_bac. 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_BACCR | ||||||||
| Accession | Primary (citable) accession number: Q81GF2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
