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Protein

Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

Gene

PDA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.

Miscellaneous

Present with 100000 molecules/cell in log phase SD medium.1 Publication

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.

GO - Molecular functioni

  • pyruvate dehydrogenase (acetyl-transferring) activity Source: SGD

GO - Biological processi

  • acetyl-CoA biosynthetic process from pyruvate Source: SGD
  • glycolytic process Source: UniProtKB-KW
  • pseudohyphal growth Source: SGD

Keywordsi

Molecular functionOxidoreductase
Biological processGlycolysis
LigandPyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciYEAST:YER178W-MONOMER
ReactomeiR-SCE-204174 Regulation of pyruvate dehydrogenase (PDH) complex
R-SCE-389661 Glyoxylate metabolism and glycine degradation
R-SCE-5362517 Signaling by Retinoic Acid
R-SCE-70268 Pyruvate metabolism
R-SCE-70895 Branched-chain amino acid catabolism

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial (EC:1.2.4.1)
Alternative name(s):
Pyruvate dehydrogenase complex component E1 alpha
Short name:
PDHE1-A
Gene namesi
Name:PDA1
Ordered Locus Names:YER178W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YER178W
SGDiS000000980 PDA1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 33Mitochondrion1 PublicationAdd BLAST33
ChainiPRO_000002045234 – 420Pyruvate dehydrogenase E1 component subunit alpha, mitochondrialAdd BLAST387

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei313Phosphoserine; by PDK1 and PDK2Combined sources1 Publication1

Post-translational modificationi

Phosphorylated at Ser-313 by pyruvate dehydrogenase kinases PKP1 (PDK1) and PKP2 (PDK2), and dephosphorylated by pyruvate dehydrogenase phosphatases PTC5 and PTC6.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP16387
PaxDbiP16387
PRIDEiP16387

PTM databases

iPTMnetiP16387

Interactioni

Subunit structurei

Pyruvate dehydrogenase (E1) is a tetramer of 2 alpha and 2 beta subunits. Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds.

Protein-protein interaction databases

BioGridi36931, 460 interactors
DIPiDIP-5117N
IntActiP16387, 37 interactors
MINTiP16387
STRINGi4932.YER178W

Structurei

3D structure databases

ProteinModelPortaliP16387
SMRiP16387
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00530000063174
HOGENOMiHOG000281336
InParanoidiP16387
KOiK00161
OMAiRRFEDKC
OrthoDBiEOG092C2YBO

Family and domain databases

InterProiView protein in InterPro
IPR001017 DH_E1
IPR017597 Pyrv_DH_E1_asu_subgrp-y
IPR029061 THDP-binding
PfamiView protein in Pfam
PF00676 E1_dh, 1 hit
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.

P16387-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLAASFKRQP SQLVRGLGAV LRTPTRIGHV RTMATLKTTD KKAPEDIEGS
60 70 80 90 100
DTVQIELPES SFESYMLEPP DLSYETSKAT LLQMYKDMVI IRRMEMACDA
110 120 130 140 150
LYKAKKIRGF CHLSVGQEAI AVGIENAITK LDSIITSYRC HGFTFMRGAS
160 170 180 190 200
VKAVLAELMG RRAGVSYGKG GSMHLYAPGF YGGNGIVGAQ VPLGAGLAFA
210 220 230 240 250
HQYKNEDACS FTLYGDGASN QGQVFESFNM AKLWNLPVVF CCENNKYGMG
260 270 280 290 300
TAASRSSAMT EYFKRGQYIP GLKVNGMDIL AVYQASKFAK DWCLSGKGPL
310 320 330 340 350
VLEYETYRYG GHSMSDPGTT YRTRDEIQHM RSKNDPIAGL KMHLIDLGIA
360 370 380 390 400
TEAEVKAYDK SARKYVDEQV ELADAAPPPE AKLSILFEDV YVKGTETPTL
410 420
RGRIPEDTWD FKKQGFASRD
Length:420
Mass (Da):46,343
Last modified:February 1, 1995 - v2
Checksum:i37019BD9E84D0002
GO

Sequence cautioni

The sequence AAB64705 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti76T → S in AAA34847 (PubMed:2684159).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M29582 mRNA Translation: AAA34847.1
X71664 Genomic DNA Translation: CAA50657.1
U18922 Genomic DNA Translation: AAB64705.1 Different initiation.
M87549 Genomic DNA Translation: AAA34572.1
D10865 Genomic DNA Translation: BAA01636.1
BK006939 Genomic DNA Translation: DAA07841.1
PIRiA36743 DEBYPA
RefSeqiNP_011105.4, NM_001179068.3

Genome annotation databases

EnsemblFungiiYER178W; YER178W; YER178W
GeneIDi856925
KEGGisce:YER178W

Entry informationi

Entry nameiODPA_YEAST
AccessioniPrimary (citable) accession number: P16387
Secondary accession number(s): D3DM87
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1995
Last modified: May 23, 2018
This is version 190 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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