Reviewed,
UniProtKB/Swiss-Prot P81419 (ODPB_SOLTU)
Last modified
November 4, 2008.
Version 40.
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 subunit beta, mitochondrial Short name=PDHE1-B EC=1.2.4.1 |
| Organism | Solanum tuberosum (Potato) |
| Taxonomic identifier | 4113 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum |
Protein attributes
| Sequence length | 16 AA. |
| Sequence status | Fragment. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
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). |
| Catalytic activity | Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2). |
| Cofactor | Thiamine pyrophosphate. |
| Subunit structure | Tetramer of 2 alpha and 2 beta subunits By similarity. |
| Subcellular location |
Ontologies
Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Mitochondrion |
| Ligand | Pyruvate Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Direct protein sequencing |
Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
References
| [1] | "Plant mitochondrial pyruvate dehydrogenase complex: purification and identification of catalytic components in potato." Millar A.H., Knorpp C., Leaver C.J., Hill S.A. Biochem. J. 334:571-576(1998) [PubMed: 9729464] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: cv. Romano. Tissue: Tuber. |
Cross-references
Entry information
| Entry name | ODPB_SOLTU | ||||||||
| Accession | Primary (citable) accession number: P81419 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


