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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: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

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
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Pyruvate, 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

GO - Cellular componenti

  • mitochondrial nucleoid Source: SGD
  • mitochondrial pyruvate dehydrogenase complex Source: SGD
  • mitochondrion Source: SGD
Complete GO annotation...

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.
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. 218 interactors.
DIPiDIP-5117N.
IntActiP16387. 17 interactors.
MINTiMINT-480200.

Structurei

3D structure databases

ProteinModelPortaliP16387.
SMRiP16387.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

GeneTreeiENSGT00530000063174.
HOGENOMiHOG000281336.
InParanoidiP16387.
KOiK00161.
OMAiTEWCRAG.
OrthoDBiEOG092C2YBO.

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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP16387.
SMRiP16387.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36931. 218 interactors.
DIPiDIP-5117N.
IntActiP16387. 17 interactors.
MINTiMINT-480200.

PTM databases

iPTMnetiP16387.

Proteomic databases

MaxQBiP16387.
PRIDEiP16387.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER178W; YER178W; YER178W.
GeneIDi856925.
KEGGisce:YER178W.

Organism-specific databases

EuPathDBiFungiDB:YER178W.
SGDiS000000980. PDA1.

Phylogenomic databases

GeneTreeiENSGT00530000063174.
HOGENOMiHOG000281336.
InParanoidiP16387.
KOiK00161.
OMAiTEWCRAG.
OrthoDBiEOG092C2YBO.

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.

Miscellaneous databases

PROiP16387.

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...

Entry informationi

Entry nameiODPA_YEAST
AccessioniPrimary (citable) accession number: P16387
Secondary accession number(s): D3DM87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1995
Last modified: November 2, 2016
This is version 176 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

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 one 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.