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P52903 (ODPA_SOLTU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

Short name=PDHE1-A
EC=1.2.4.1
OrganismSolanum tuberosum (Potato) [Reference proteome]
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length391 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Mitochondrion matrix.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandPyruvate
Thiamine pyrophosphate
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglycolytic process

Inferred from electronic annotation. Source: UniProtKB-KW

response to salt stress

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Cellular_componentcytosol

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

mitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

   Molecular_functioncobalt ion binding

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

pyruvate dehydrogenase (acetyl-transferring) activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: EnsemblPlants/Gramene

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Mitochondrion Ref.3
Chain27 – 391365Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
PRO_0000020455

Sequences

Sequence LengthMass (Da)Tools
P52903 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: F9110B374B022F0D

FASTA39143,228
        10         20         30         40         50         60 
MALSTSRAIN HIMKPLSAAV CATRRLSSDS TATITVETSL PFTSHNIDPP SRSVETSPKE 

        70         80         90        100        110        120 
LMTFFKDMTE MRRMEIAADS LYKAKLIRGF CHLYDGQEAV AVGMEAAITK KDCIITAYRD 

       130        140        150        160        170        180 
HCIFLGRGGT LVEAFAELMG RRDGCSRGKG GSMHFYKKES GFYGGHGIVG AQVPLGIGLA 

       190        200        210        220        230        240 
FAQKYKKEDY VTFAMYGDGA ANQGQLFEAL NMAALWDLPA ILVCENNHYG MGTAEWRAAK 

       250        260        270        280        290        300 
SPAYYKRGDY VPGLRVDGMD VFAVKQACTF AKQHALKNGP IILEMDTYRY HGHSMSDPGS 

       310        320        330        340        350        360 
TYRTRDEISG VRQERDPVER IRSLILAHNI ATEAELKDIE KENRKVVDEA IAKAKESPMP 

       370        380        390 
DPSELFTNVY VKGFGVEAYG ADRKELRATL P 

« Hide

References

« Hide 'large scale' references
[1]"Mitochondrial pyruvate dehydrogenase. Molecular cloning of the E1 alpha subunit and expression analysis."
Grof C.P., Winning B.M., Scaysbrook T.P., Hill S.A., Leaver C.J.
Plant Physiol. 108:1623-1629(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: cv. Desiree.
Tissue: Leaf.
[2]"Genome sequence and analysis of the tuber crop potato."
The Potato Genome Sequencing Consortium
Nature 475:189-195(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. DM1-3 516 R44.
[3]"Plant mitochondrial pyruvate dehydrogenase complex: purification and identification of catalytic components in potato."
Millar A.H., Knorpp C., Leaver C.J., Hill S.A.
Biochem. J. 334:571-576(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-42.
Strain: cv. Romano.
Tissue: Tuber.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z26949 mRNA. Translation: CAA81558.1.
PIRT07372.
UniGeneStu.18026.

3D structure databases

ProteinModelPortalP52903.
SMRP52903. Positions 32-379.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP52903. 1 interaction.

Proteomic databases

ProMEXP52903.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsPGSC0003DMT400058223; PGSC0003DMT400058223; PGSC0003DMG400022607.

Family and domain databases

Gene3D3.40.50.970. 1 hit.
InterProIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMSSF52518. SSF52518. 1 hit.
TIGRFAMsTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetSearch...

Entry information

Entry nameODPA_SOLTU
AccessionPrimary (citable) accession number: P52903
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program