Q5R490 (ODPA_PONAB) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 48.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames 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 | Pongo abelii (Sumatran orangutan) | ||
| Taxonomic identifier | 9601 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo |
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 |
| 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_0000020444 | |||||
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] | The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain cortex. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CR861366 mRNA. Translation: CAH93426.1. |
| RefSeq | NP_001127663.1. NM_001134191.1. |
| UniGene | Pab.18473. |
3D structure databases | |
| ProteinModelPortal | Q5R490. |
| SMR | Q5R490. Positions 29-390. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 100174745. |
| KEGG | pon:100174745. |
Organism-specific databases | |
| CTD | 5160. |
Phylogenomic databases | |
| HOVERGEN | HBG001863. |
| InParanoid | Q5R490. |
Family and domain databases | |
| InterPro | IPR001017. DH_E1. IPR017597. Pyrv_DH_E1_asu_subgrp-y. [Graphical view] |
| KO | K00161. |
| Pfam | PF00676. E1_dh. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03182. PDH_E1_alph_y. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | ODPA_PONAB | ||||||||
| Accession | Primary (citable) accession number: Q5R490 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||

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