C8MKR0 (C8MKR0_STAAU) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 9.
History...
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: 2-oxoglutarate dehydrogenase E1 component HAMAP MF_01169 EC=1.2.4.2 HAMAP MF_01169 Alternative name(s): Alpha-ketoglutarate dehydrogenase HAMAP MF_01169 | ||||
| Gene names |
| ||||
| Organism | Staphylococcus aureus A9719 EMBL EEV67908.1 | ||||
| Taxonomic identifier | 553588 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 932 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 MF_01169 SAAS SAAS011603 |
| Catalytic activity | 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO2. SAAS SAAS011603 HAMAP MF_01169 |
| Cofactor | Thiamine pyrophosphate By similarity. SAAS SAAS023784 HAMAP MF_01169 |
| Subunit structure | Homodimer By similarity. HAMAP MF_01169 SAAS SAAS011603 |
| Sequence similarities | Belongs to the alpha-ketoglutarate dehydrogenase family. HAMAP MF_01169 |
| Caution | The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis SAAS SAAS011603 HAMAP MF_01169 |
| Ligand | Thiamine pyrophosphate SAAS SAAS001017 HAMAP MF_01169 |
| Molecular function | Oxidoreductase SAAS SAAS023784 HAMAP MF_01169 |
| 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... | |
Sequences
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References
| [1] | "The Genome Sequence of Staphylococcus aureus strain A9719." The Broad Institute Genome Sequencing Platform Ward D., Young S.K., Zeng Q., Koehrsen M., Godfrey P., Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C. Birren B.Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: A9719 EMBL EEV67908.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | ACKJ01000028 Genomic DNA. Translation: EEV67908.1. |
3D structure databases | |
| ProteinModelPortal | C8MKR0. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| PATRIC | 26185881. VBIStaAur45793_0876. |
Family and domain databases | |
| HAMAP | MF_01169. SucA_OdhA. [Tree] |
| InterPro | IPR011603. 2oxoglutarate_DH_E1. IPR023784. 2oxoglutarate_DH_E1_bac. IPR001017. DH_E1. IPR005475. Transketolase-like_Pyr-bd. [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. |
| SMART | SM00861. Transket_pyr. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00239. 2oxo_dh_E1. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | C8MKR0_STAAU | ||||||||
| Accession | Primary (citable) accession number: C8MKR0 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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