SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P16387

- ODPA_YEAST

UniProt

P16387 - ODPA_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
Gene
PDA1, YER178W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - 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

Thiamine pyrophosphate.

Enzyme regulationi

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

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: SGD
Complete GO annotation...

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: SGD
  2. glycolytic process Source: UniProtKB-KW
  3. 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.

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
ProteomesiUP000002311: Chromosome V

Organism-specific databases

CYGDiYER178w.
SGDiS000000980. PDA1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial nucleoid Source: SGD
  2. mitochondrial pyruvate dehydrogenase complex Source: SGD
  3. mitochondrion Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333Mitochondrion1 Publication
Add
BLAST
Chaini34 – 420387Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial
PRO_0000020452Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei313 – 3131Phosphoserine; by PDK1 and PDK26 Publications

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.
PeptideAtlasiP16387.

Expressioni

Gene expression databases

GenevestigatoriP16387.

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. 215 interactions.
DIPiDIP-5117N.
IntActiP16387. 15 interactions.
MINTiMINT-480200.
STRINGi4932.YER178W.

Structurei

3D structure databases

ProteinModelPortaliP16387.
SMRiP16387. Positions 41-391.

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1071.
GeneTreeiENSGT00530000063174.
HOGENOMiHOG000281336.
KOiK00161.
OMAiRGPNQWI.
OrthoDBiEOG7QZGMC.

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

MLAASFKRQP SQLVRGLGAV LRTPTRIGHV RTMATLKTTD KKAPEDIEGS    50
DTVQIELPES SFESYMLEPP DLSYETSKAT LLQMYKDMVI IRRMEMACDA 100
LYKAKKIRGF CHLSVGQEAI AVGIENAITK LDSIITSYRC HGFTFMRGAS 150
VKAVLAELMG RRAGVSYGKG GSMHLYAPGF YGGNGIVGAQ VPLGAGLAFA 200
HQYKNEDACS FTLYGDGASN QGQVFESFNM AKLWNLPVVF CCENNKYGMG 250
TAASRSSAMT EYFKRGQYIP GLKVNGMDIL AVYQASKFAK DWCLSGKGPL 300
VLEYETYRYG GHSMSDPGTT YRTRDEIQHM RSKNDPIAGL KMHLIDLGIA 350
TEAEVKAYDK SARKYVDEQV ELADAAPPPE AKLSILFEDV YVKGTETPTL 400
RGRIPEDTWD FKKQGFASRD 420
Length:420
Mass (Da):46,343
Last modified:February 1, 1995 - v2
Checksum:i37019BD9E84D0002
GO

Sequence cautioni

The sequence AAB64705.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761T → S in AAA34847. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
PIRi A36743. DEBYPA.
RefSeqi NP_011105.4. NM_001179068.3.

3D structure databases

ProteinModelPortali P16387.
SMRi P16387. Positions 41-391.
ModBasei Search...

Protein-protein interaction databases

BioGridi 36931. 215 interactions.
DIPi DIP-5117N.
IntActi P16387. 15 interactions.
MINTi MINT-480200.
STRINGi 4932.YER178W.

Proteomic databases

MaxQBi P16387.
PaxDbi P16387.
PeptideAtlasi P16387.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YER178W ; YER178W ; YER178W .
GeneIDi 856925.
KEGGi sce:YER178W.

Organism-specific databases

CYGDi YER178w.
SGDi S000000980. PDA1.

Phylogenomic databases

eggNOGi COG1071.
GeneTreei ENSGT00530000063174.
HOGENOMi HOG000281336.
KOi K00161.
OMAi RGPNQWI.
OrthoDBi EOG7QZGMC.

Enzyme and pathway databases

BioCyci YEAST:YER178W-MONOMER.

Miscellaneous databases

NextBioi 983395.
PROi P16387.

Gene expression databases

Genevestigatori P16387.

Family and domain databases

Gene3Di 3.40.50.970. 1 hit.
InterProi IPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
IPR029061. THDP-binding.
[Graphical view ]
Pfami PF00676. E1_dh. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
TIGRFAMsi TIGR03182. PDH_E1_alph_y. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide and deduced amino acid sequence of the alpha subunit of yeast pyruvate dehydrogenase."
    Behal R.H., Browning K.S., Andreed L.J.
    Biochem. Biophys. Res. Commun. 164:941-946(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-53 AND 309-322.
  2. "Promoter analysis of the PDA1 gene encoding the E1 alpha subunit of the pyruvate dehydrogenase complex from Saccharomyces cerevisiae."
    Wenzel T.J., Zuurmond A.M., Bergmans A., van den Berg J.A., Steensma H.Y.
    Yeast 10:297-308(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 26109 / X2180.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "DMC1: a meiosis-specific yeast homolog of E. coli recA required for recombination, synaptonemal complex formation, and cell cycle progression."
    Bishop D.K., Park D., Xu L., Kleckner N.
    Cell 69:439-456(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 335-420.
  6. "Isolation and characterization of a yeast gene that is homologous with a meiosis-specific cDNA from a plant."
    Kobayashi T., Hotta Y., Tabata S.
    Mol. Gen. Genet. 237:225-232(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 357-420.
    Strain: SK1.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
    Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
    Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  11. "Yeast pyruvate dehydrogenase complex is regulated by a concerted activity of two kinases and two phosphatases."
    Gey U., Czupalla C., Hoflack B., Rodel G., Krause-Buchholz U.
    J. Biol. Chem. 283:9759-9767(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-313 BY PKP1/PKP2.
  12. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: September 3, 2014
This is version 153 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.

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

External Data

Dasty 3

Similar proteinsi