Reviewed,
UniProtKB/Swiss-Prot Q8HXW9 (ODPA_MACFA)
Last modified
February 9, 2010.
Version 42.
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 | Macaca fascicularis (Crab eating macaque) (Cynomolgus monkey) | ||||
| Taxonomic identifier | 9541 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Cercopithecinae › Macaca |
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 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) By similarity. |
| Catalytic activity | Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. |
| Cofactor | Thiamine pyrophosphate By similarity. |
| Enzyme regulation | E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit By similarity. |
| Subunit structure | Tetramer of 2 alpha and 2 beta subunits By similarity. |
| Subcellular location | Mitochondrion matrix By similarity. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Pyruvate Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| PTM | Acetylation Phosphoprotein |
| 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)
| 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_0000020441 | |||||
Amino acid modifications | |||||||||
| Modified residue | 77 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 83 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 231 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 232 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 289 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 293 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 295 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 300 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 301 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 321 | 1 | N6-acetyllysine By similarity | ||||||
| Modified residue | 336 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | "Isolation and characterization of cDNA for macaque neurological disease genes." Kusuda J., Osada N., Hida M., Sugano S., Hashimoto K. Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB083322 mRNA. Translation: BAC20601.1. |
3D structure databases | |
| SMR | Q8HXW9. Positions 29-390. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q8HXW9. |
Enzyme and pathway databases | |
| BRENDA | 1.2.4.1. 3438. |
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_MACFA | ||||||||
| Accession | Primary (citable) accession number: Q8HXW9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||

Clusters with


