Reviewed,
UniProtKB/Swiss-Prot Q59097 (ODP1_RALEH)
Last modified
November 4, 2008.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
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 | Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 381666 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus |
Protein attributes
| Sequence length | 895 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 CO(2). 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 + CO(2). |
| 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 – 895 | 895 | Pyruvate dehydrogenase E1 component | PRO_0000162238 | |||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Biochemical and molecular characterization of the Alcaligenes eutrophus pyruvate dehydrogenase complex and identification of a new type of dihydrolipoamide dehydrogenase." Hein S., Steinbuechel A. J. Bacteriol. 176:4394-4408(1994) [PubMed: 8021225] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16." Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B. Nat. Biotechnol. 24:1257-1262(2006) [PubMed: 16964242] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| U09865 Genomic DNA. Translation: AAA21598.1. AM260479 Genomic DNA. Translation: CAJ92510.1. | |
| PIR | A55514. |
| RefSeq | YP_725878.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1L8A based on UniProtKB P06958. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4250135. |
| GenomeReviews | Gene locus H16_A1374 in contig AM260479_GR. |
| KEGG | reh:H16_A1374. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q59097. |
Family and domain databases | |
| InterPro | IPR004660. 2-oxoA_DHase_E1. IPR005474. Transketo_N. IPR015941. Transketolase_C-like. [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_RALEH | ||||||||
| Accession | Primary (citable) accession number: Q59097 Secondary accession number(s): Q0KBW1 | ||||||||
| 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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