P52901 (ODPA1_ARATH) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 109.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial Short name=PDHE1-A EC=1.2.4.1 | ||||||
| Gene names |
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| Organism | Arabidopsis thaliana (Mouse-ear cress) [Reference proteome] | ||||||
| Taxonomic identifier | 3702 [NCBI] | ||||||
| Taxonomic lineage | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis![]() |
Protein attributes
| Sequence length | 389 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 By similarity. |
| Subunit structure | Tetramer of 2 alpha and 2 beta subunits By similarity. |
| Subcellular location | |
| Tissue specificity | Expressed in roots, rosettes and flowers. Ref.1 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Cellular component | Mitochondrion |
| Domain | Transit peptide |
| Ligand | Pyruvate Thiamine pyrophosphate |
| Molecular function | Oxidoreductase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred from electronic annotation. Source: UniProtKB-KW response to cadmium ionInferred from expression pattern PubMed 16502469PubMed 20005002. Source: TAIR |
| Cellular_component | cytosol Inferred from direct assay PubMed 18433157. Source: TAIR mitochondrial matrixInferred from electronic annotation. Source: UniProtKB-SubCell mitochondrionInferred from direct assay PubMed 11743115Ref.6PubMed 18385124. Source: TAIR nucleusInferred from direct assay PubMed 18433157. Source: TAIR |
| 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 – 32 | 32 | Mitochondrion Potential | ||||||
| Chain | 33 – 389 | 357 | Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial | PRO_0000020453 | |||||
Experimental info | |||||||||
| Sequence conflict | 83 – 84 | 2 | KL → NV in AAA86507. Ref.1 | ||||||
| Sequence conflict | 362 | 1 | E → D in AAK26016. Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The mitochondrial pyruvate dehydrogenase complex: nucleotide and deduced amino-acid sequences of a cDNA encoding the Arabidopsis thaliana E1 alpha-subunit." Luethy M.H., Miernyk J.A., Randall D.D. Gene 164:251-254(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: cv. Columbia. |
| [2] | "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. Davis R.W.Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia. |
| [3] | The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia. |
| [4] | "Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. Ecker J.R.Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia. |
| [5] | "Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [6] | "Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins." Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H. Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Strain: cv. Landsberg erecta. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U21214 mRNA. Translation: AAA86507.1. AC007258 Genomic DNA. Translation: AAD39331.1. CP002684 Genomic DNA. Translation: AEE33638.1. AF360306 mRNA. Translation: AAK26016.1. BT000974 mRNA. Translation: AAN41374.1. AY087667 mRNA. Translation: AAM65205.1. |
| IPI | IPI00531318. |
| PIR | B96623. JC4358. |
| RefSeq | NP_176198.1. NM_104682.2. |
| UniGene | At.23186. |
3D structure databases | |
| ProteinModelPortal | P52901. |
| SMR | P52901. Positions 47-368. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P52901. 1 interaction. |
2D gel databases | |
| SWISS-2DPAGE | P52901. |
Proteomic databases | |
| PaxDb | P52901. |
| PRIDE | P52901. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblPlants | AT1G59900.1; AT1G59900.1; AT1G59900. |
| GeneID | 842284. |
| KEGG | ath:AT1G59900. |
Organism-specific databases | |
| GeneFarm | 4372. 441. |
| TAIR | At1g59900. |
Phylogenomic databases | |
| eggNOG | COG1071. |
| HOGENOM | HOG000281336. |
| InParanoid | P52901. |
| KO | K00161. |
| OMA | DRMLSNN. |
| PhylomeDB | P52901. |
| ProtClustDB | PLN02269. |
Gene expression databases | |
| ArrayExpress | P52901. |
| Genevestigator | P52901. |
| GermOnline | AT1G59900. Arabidopsis thaliana. |
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 | ODPA1_ARATH | ||||||||
| Accession | Primary (citable) accession number: P52901 Secondary accession number(s): Q9C5E3, Q9SXC2 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Plant Protein Annotation Program | ||||||||
Relevant documents
| Arabidopsis thaliana Arabidopsis thaliana: entries and gene names |

Clusters with
