Reviewed,
UniProtKB/Swiss-Prot Q8K9T9 (ODP1_BUCAP)
Last modified
November 3, 2009.
Version 51.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Pyruvate dehydrogenase E1 component EC=1.2.4.1 | ||||
| Gene names |
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| Organism | Buchnera aphidicola subsp. Schizaphis graminum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 98794 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera |
Protein attributes
| Sequence length | 888 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) By similarity. |
| Catalytic activity | Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. |
| Cofactor | Thiamine pyrophosphate By similarity. |
| Subunit structure | Homodimer By similarity. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | Pyruvate Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 888 | 888 | Pyruvate dehydrogenase E1 component | PRO_0000162241 | |||
Sequences
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References
| [1] | "50 million years of genomic stasis in endosymbiotic bacteria." Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E. Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| AE013218 Genomic DNA. Translation: AAM67763.1. | |
| RefSeq | NP_660552.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1L8A based on UniProtKB P06958. |
| SMR | Q8K9T9. Positions 59-888. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1005396. |
| GenomeReviews | Gene locus BUsg_199 in contig AE013218_GR. |
| KEGG | bas:BUsg199. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q8K9T9. |
| OMA | REISTTQ. |
Enzyme and pathway databases | |
| BioCyc | BAPH198804:BUSG199-MON. |
Family and domain databases | |
| InterPro | IPR004660. 2-oxoA_DH_E1. IPR015941. Transketolase-like_C. IPR005474. Transketolase_N. [Graphical view] |
| Gene3D | G3DSA:3.40.50.920. Transketo_C_like. 1 hit. |
| Pfam | PF00456. Transketolase_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000156. Pyruvate_dh_E1. 1 hit. |
| TIGRFAMs | TIGR00759. aceE. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ODP1_BUCAP | ||||||||
| Accession | Primary (citable) accession number: Q8K9T9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Buchnera aphidicola (subsp. Schizaphis graminum) Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names |

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