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Protein

Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

Enzyme regulationi

E1 activity is regulated by phosphorylation (inactivation) and dephosphorylation (activation) of the alpha subunit.By similarity

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

BRENDAi1.2.4.1. 5757.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial (EC:1.2.4.1)
Short name:
PDHE1-A
OrganismiSolanum tuberosum (Potato)
Taxonomic identifieri4113 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
ProteomesiUP000011115 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626Mitochondrion1 PublicationAdd
BLAST
Chaini27 – 391365Pyruvate dehydrogenase E1 component subunit alpha, mitochondrialPRO_0000020455Add
BLAST

Keywords - PTMi

Phosphoprotein

Proteomic databases

ProMEXiP52903.

Interactioni

Subunit structurei

Tetramer of 2 alpha and 2 beta subunits.By similarity

Protein-protein interaction databases

IntActiP52903. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliP52903.
SMRiP52903. Positions 32-379.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

InParanoidiP52903.
OMAiMVLCREF.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52903-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALSTSRAIN HIMKPLSAAV CATRRLSSDS TATITVETSL PFTSHNIDPP
60 70 80 90 100
SRSVETSPKE LMTFFKDMTE MRRMEIAADS LYKAKLIRGF CHLYDGQEAV
110 120 130 140 150
AVGMEAAITK KDCIITAYRD HCIFLGRGGT LVEAFAELMG RRDGCSRGKG
160 170 180 190 200
GSMHFYKKES GFYGGHGIVG AQVPLGIGLA FAQKYKKEDY VTFAMYGDGA
210 220 230 240 250
ANQGQLFEAL NMAALWDLPA ILVCENNHYG MGTAEWRAAK SPAYYKRGDY
260 270 280 290 300
VPGLRVDGMD VFAVKQACTF AKQHALKNGP IILEMDTYRY HGHSMSDPGS
310 320 330 340 350
TYRTRDEISG VRQERDPVER IRSLILAHNI ATEAELKDIE KENRKVVDEA
360 370 380 390
IAKAKESPMP DPSELFTNVY VKGFGVEAYG ADRKELRATL P
Length:391
Mass (Da):43,228
Last modified:September 30, 1996 - v1
Checksum:iF9110B374B022F0D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26949 mRNA. Translation: CAA81558.1.
PIRiT07372.
UniGeneiStu.18026.

Genome annotation databases

EnsemblPlantsiPGSC0003DMT400058223; PGSC0003DMT400058223; PGSC0003DMG400022607.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26949 mRNA. Translation: CAA81558.1.
PIRiT07372.
UniGeneiStu.18026.

3D structure databases

ProteinModelPortaliP52903.
SMRiP52903. Positions 32-379.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP52903. 1 interaction.

Proteomic databases

ProMEXiP52903.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiPGSC0003DMT400058223; PGSC0003DMT400058223; PGSC0003DMG400022607.

Phylogenomic databases

InParanoidiP52903.
OMAiMVLCREF.

Enzyme and pathway databases

BRENDAi1.2.4.1. 5757.

Family and domain databases

Gene3Di3.40.50.970. 1 hit.
InterProiIPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view]
PfamiPF00676. E1_dh. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
TIGRFAMsiTIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1994) [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(2010) [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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-42.
    Strain: cv. Romano.
    Tissue: Tuber.

Entry informationi

Entry nameiODPA_SOLTU
AccessioniPrimary (citable) accession number: P52903
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1996
Last sequence update: September 30, 1996
Last modified: March 31, 2015
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.