Reviewed,
UniProtKB/Swiss-Prot P26284 (ODPA_RAT)
Last modified
June 16, 2009.
Version 75.
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 alpha, somatic form, mitochondrial EC=1.2.4.1 Alternative name(s): PDHE1-A type I | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 390 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein 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. |
| Enzyme regulation | E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit. |
| Subunit structure | Tetramer of 2 alpha and 2 beta subunits. |
| Subcellular location | |
| Tissue specificity | In all tissues, but in very low amount in testis. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Pyruvate Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | acetyl-CoA biosynthetic process from pyruvate Inferred from direct assay. Source: RGD glycolysisInferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | mitochondrial pyruvate dehydrogenase complex Ref.2 Traceable author statement. Source: RGD |
| Molecular function | pyruvate dehydrogenase (acetyl-transferring) activity Ref.2 Inferred from direct assay. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Transit peptide | 1 – 29 | 29 | Mitochondrion By similarity | ||||||
| Chain | 30 – 390 | 361 | Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial | PRO_0000020445 | |||||
Amino acid modifications | |||||||||
| Modified residue | 232 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 289 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 293 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 295 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 300 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 301 | 1 | Phosphotyrosine Ref.4 | ||||||
Experimental info | |||||||||
| Sequence conflict | 10 | 1 | R → H in CAA78146. Ref.2 | ||||||
| Sequence conflict | 126 | 1 | N → T in CAA78146. Ref.2 | ||||||
| Sequence conflict | 129 – 130 | 2 | HA → LP in CAA78146. Ref.2 | ||||||
| Sequence conflict | 134 | 1 | I → V Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The alpha-ketoacid dehydrogenase complexes. Sequence similarity of rat pyruvate dehydrogenase with Escherichia coli and Azotobacter vinelandii alpha-ketoglutarate dehydrogenase." Matuda S., Nakano K., Ohta S., Saheki T., Kawanishi Y., Miyata T. Biochim. Biophys. Acta 1089:1-7(1991) [PubMed: 2025639] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "The pyruvate dehydrogenase complex: cloning of the rat somatic E1 alpha subunit and its coordinate expression with the mRNAs for the E1 beta, E2, and E3 catalytic subunits in developing rat brain." Cullingford T.E., Clark J.B., Phillips I.R. J. Neurochem. 62:1682-1690(1994) [PubMed: 8158120] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: Sprague-Dawley. Tissue: Liver. |
| [3] | Lubec G., Diao W., Chen W.-Q. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 133-141; 216-226; 245-253; 289-302 AND 324-343, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Hippocampus. |
| [4] | "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites." Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A. Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed: 16641100] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-295; SER-300 AND TYR-301, MASS SPECTROMETRY. Tissue: Kidney. |
Cross-references
Sequence databases | |
|---|---|
| Z12158 mRNA. Translation: CAA78146.1. | |
| IPI | IPI00191707. |
| PIR | DERTPA. S15891. DERTP1. S21553. |
| UniGene | Rn.3655 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1NI4 based on UniProtKB P08559. |
| SMR | P26284. Positions 29-390. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P26284. |
Proteomic databases | |
| PRIDE | P26284. |
Genome annotation databases | |
| Ensembl | ENSRNOG00000025383. Rattus norvegicus. [Contig view] |
Organism-specific databases | |
| RGD | 3286. Pdha1. |
Phylogenomic databases | |
| HOVERGEN | P26284. |
Enzyme and pathway databases | |
| BRENDA | 1.2.4.1. 248. |
Gene expression databases | |
| ArrayExpress | P26284. |
| GermOnline | ENSRNOG00000025383. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR001017. DH_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view] |
| Pfam | PF00676. E1_dh. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03182. PDH_E1_alph_y. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ODPA_RAT | ||||||||
| Accession | Primary (citable) accession number: P26284 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


