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P16387

- ODPA_YEAST

UniProt

P16387 - ODPA_YEAST

Protein

Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial

Gene

PDA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
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    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

    GO - Biological processi

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

    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

    Keywords - Cellular componenti

    Mitochondrion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3333Mitochondrion1 PublicationAdd
    BLAST
    Chaini34 – 420387Pyruvate dehydrogenase E1 component subunit alpha, mitochondrialPRO_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 PTC6.6 Publications

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti76 – 761T → S in AAA34847. (PubMed:2684159)Curated

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 154 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

    External Data

    Dasty 3