Reviewed,
UniProtKB/Swiss-Prot P52904 (ODPB_PEA)
Last modified
September 22, 2009.
Version 61.
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 | Pisum sativum (Garden pea) |
| Taxonomic identifier | 3888 [NCBI] |
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Fabales › Fabaceae › Papilionoideae › Fabeae › Pisum |
Protein attributes
| Sequence length | 359 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
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). |
| Catalytic activity | Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. |
| 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 |
| Domain | Transit peptide |
| Ligand | Pyruvate Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| 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
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References
| [1] | Luethy M.H., Miernyk J.A., Randall D.D. Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
Cross-references
Sequence databases | |
|---|---|
| U56697 mRNA. Translation: AAB01223.1. | |
| PIR | T06532. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NI4 based on UniProtKB P11177. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P52904. 1 interaction. |
Enzyme and pathway databases | |
| BRENDA | 1.2.4.1. 287. |
Family and domain databases | |
| InterPro | IPR015941. Transketolase-like_C. IPR005475. Transketolase-like_Pyr-bd. IPR005476. Transketolase_C. [Graphical view] |
| Gene3D | G3DSA:3.40.50.920. Transketo_C_like. 1 hit. |
| Pfam | PF02779. Transket_pyr. 1 hit. PF02780. Transketolase_C. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ODPB_PEA | ||||||||
| Accession | Primary (citable) accession number: P52904 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | PPAP (Plant Proteome Annotation Project) | ||||||||

Clusters with


