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P06169

- PDC1_YEAST

UniProt

P06169 - PDC1_YEAST

Protein

Pyruvate decarboxylase isozyme 1

Gene

PDC1

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 167 (01 Oct 2014)
      Sequence version 7 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids valine, isoleucine, phenylalanine, and tryptophan, whereas leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins.10 Publications

    Catalytic activityi

    A 2-oxo acid = an aldehyde + CO2.1 Publication
    3-(indol-3-yl)pyruvate = 2-(indol-3-yl)acetaldehyde + CO2.1 Publication
    Phenylpyruvate = phenylacetaldehyde + CO2.1 Publication
    Pyruvate = Acetaldehyde + CO2.1 Publication
    A 2-oxo acid + an aldehyde = A 2-hydroxy ketone + CO2.1 Publication
    An aldehyde + an aldehyde = A 2-hydroxy ketone.1 Publication

    Cofactori

    Binds 1 magnesium per subunit.
    Binds 1 thiamine pyrophosphate per subunit.

    Enzyme regulationi

    Allosterically activated by substrate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei28 – 281Substrate
    Binding sitei115 – 1151Substrate
    Binding sitei157 – 1571Substrate; allosteric site
    Metal bindingi444 – 4441Magnesium
    Metal bindingi471 – 4711Magnesium
    Metal bindingi473 – 4731Magnesium; via carbonyl oxygen
    Binding sitei477 – 4771Substrate

    GO - Molecular functioni

    1. branched-chain-2-oxoacid decarboxylase activity Source: SGD
    2. magnesium ion binding Source: InterPro
    3. pyruvate decarboxylase activity Source: SGD
    4. thiamine pyrophosphate binding Source: InterPro

    GO - Biological processi

    1. aromatic amino acid family catabolic process to alcohol via Ehrlich pathway Source: SGD
    2. branched-chain amino acid catabolic process Source: UniProtKB-KW
    3. glucose catabolic process to ethanol Source: SGD
    4. L-phenylalanine catabolic process Source: SGD
    5. pyruvate metabolic process Source: SGD
    6. tryptophan catabolic process Source: SGD

    Keywords - Molecular functioni

    Decarboxylase, Lyase

    Keywords - Biological processi

    Branched-chain amino acid catabolism, Phenylalanine catabolism, Tryptophan catabolism

    Keywords - Ligandi

    Magnesium, Metal-binding, Thiamine pyrophosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER3O-117.
    YEAST:MONOMER3O-117.
    BRENDAi4.1.1.1. 984.
    SABIO-RKP06169.
    UniPathwayiUPA00206.
    UPA00866.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Pyruvate decarboxylase isozyme 1 (EC:4.1.1.-, EC:4.1.1.1)
    Gene namesi
    Name:PDC1
    Ordered Locus Names:YLR044C
    ORF Names:L2104
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    SGDiS000004034. PDC1.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Biotechnological usei

    Fusel oils and acyloins are important flavor and aroma compounds in yeast-fermented products contributing to the quality of beverages and food, e.g. fusel oils in whiskey, contrary to common believe, seem to alleviate hangover. In general they are desirable at low concentrations, whereas high concentrations may spoil the product. By adjusting growth conditions and substrate their production is sought to be influenced. Due to their broad substrate tolerance pyruvate decarboxylases are important biocatalysts for chemoenzymatic syntheses, both by fermentation and in vitro, e.g. in the production of ephedrine, vitamin E, or phenylethanol (rose flavor).1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi291 – 2911D → N in PDC1-8; reduces catalytic activity to 10% but retains autoregulatory activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 563562Pyruvate decarboxylase isozyme 1PRO_0000090770Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei223 – 2231Phosphoserine3 Publications
    Modified residuei266 – 2661Phosphothreonine1 Publication
    Modified residuei336 – 3361Phosphothreonine1 Publication
    Modified residuei353 – 3531Phosphothreonine2 Publications
    Modified residuei522 – 5221Phosphothreonine1 Publication
    Modified residuei526 – 5261Phosphoserine1 Publication

    Post-translational modificationi

    Cleavage of N-terminal methionine and N-terminal acetylation by NAT1/ARD1.2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP06169.
    PaxDbiP06169.
    PeptideAtlasiP06169.

    2D gel databases

    COMPLUYEAST-2DPAGEP06169.
    SWISS-2DPAGEP06169.

    Expressioni

    Inductioni

    Protein expression is strongly induced by high concentrations of fermentable carbon sources and under anaerobic growth conditions and is repressed by ethanol. Protein expression level is also autoregulated through an unknown mechanism.

    Gene expression databases

    GenevestigatoriP06169.

    Interactioni

    Subunit structurei

    Homotetramer.3 Publications

    Protein-protein interaction databases

    BioGridi31319. 121 interactions.
    DIPiDIP-6773N.
    IntActiP06169. 79 interactions.
    MINTiMINT-667063.

    Structurei

    Secondary structure

    1
    563
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Helixi6 – 1611
    Beta strandi21 – 244
    Helixi28 – 303
    Helixi31 – 355
    Helixi36 – 394
    Helixi51 – 6515
    Beta strandi68 – 736
    Helixi76 – 9116
    Beta strandi95 – 1017
    Helixi104 – 1085
    Beta strandi109 – 1113
    Beta strandi114 – 1163
    Beta strandi118 – 1203
    Helixi124 – 1307
    Beta strandi134 – 1385
    Turni142 – 1443
    Helixi145 – 15915
    Beta strandi163 – 1686
    Helixi171 – 1733
    Beta strandi174 – 1774
    Helixi178 – 1825
    Helixi194 – 21017
    Beta strandi212 – 2187
    Helixi220 – 2245
    Helixi228 – 23811
    Beta strandi242 – 2443
    Turni246 – 2505
    Beta strandi259 – 2624
    Helixi265 – 2673
    Helixi270 – 2778
    Beta strandi280 – 2867
    Turni291 – 2977
    Beta strandi306 – 3094
    Beta strandi311 – 3166
    Beta strandi319 – 3224
    Helixi326 – 34015
    Turni341 – 3433
    Helixi367 – 3748
    Turni375 – 3773
    Beta strandi383 – 3864
    Helixi390 – 3945
    Helixi395 – 3973
    Beta strandi405 – 4073
    Turni410 – 4123
    Helixi417 – 43216
    Beta strandi438 – 4436
    Helixi444 – 4507
    Helixi451 – 4533
    Helixi454 – 4596
    Beta strandi465 – 4739
    Helixi475 – 4806
    Helixi486 – 4883
    Helixi495 – 4973
    Helixi498 – 5014
    Beta strandi505 – 5128
    Helixi515 – 5228
    Turni525 – 5284
    Beta strandi531 – 5399
    Helixi547 – 56115

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PVDX-ray2.30A/B2-556[»]
    1PYDX-ray2.40A/B1-556[»]
    1QPBX-ray2.40A/B1-563[»]
    2VK1X-ray1.71A/B/C/D1-563[»]
    2VK8X-ray1.42A/B/C/D1-563[»]
    2W93X-ray1.60A/B/C/D1-563[»]
    ProteinModelPortaliP06169.
    SMRiP06169. Positions 2-563.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06169.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni390 – 47687Thiamine pyrophosphate bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the TPP enzyme family.Curated

    Phylogenomic databases

    eggNOGiCOG3961.
    GeneTreeiENSGT00550000075465.
    KOiK01568.
    OMAiLADACCS.
    OrthoDBiEOG779P6S.

    Family and domain databases

    Gene3Di3.40.50.1220. 1 hit.
    3.40.50.970. 2 hits.
    InterProiIPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR029061. THDP-binding.
    IPR012000. Thiamin_PyroP_enz_cen_dom.
    IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
    IPR000399. TPP-bd_CS.
    IPR012110. TPP_enzyme.
    IPR011766. TPP_enzyme-bd_C.
    [Graphical view]
    PANTHERiPTHR18968:SF4. PTHR18968:SF4. 1 hit.
    PfamiPF02775. TPP_enzyme_C. 1 hit.
    PF00205. TPP_enzyme_M. 1 hit.
    PF02776. TPP_enzyme_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036565. Pyruvt_ip_decrb. 1 hit.
    SUPFAMiSSF52467. SSF52467. 1 hit.
    SSF52518. SSF52518. 2 hits.
    PROSITEiPS00187. TPP_ENZYMES. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P06169-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEITLGKYL FERLKQVNVN TVFGLPGDFN LSLLDKIYEV EGMRWAGNAN    50
    ELNAAYAADG YARIKGMSCI ITTFGVGELS ALNGIAGSYA EHVGVLHVVG 100
    VPSISAQAKQ LLLHHTLGNG DFTVFHRMSA NISETTAMIT DIATAPAEID 150
    RCIRTTYVTQ RPVYLGLPAN LVDLNVPAKL LQTPIDMSLK PNDAESEKEV 200
    IDTILALVKD AKNPVILADA CCSRHDVKAE TKKLIDLTQF PAFVTPMGKG 250
    SIDEQHPRYG GVYVGTLSKP EVKEAVESAD LILSVGALLS DFNTGSFSYS 300
    YKTKNIVEFH SDHMKIRNAT FPGVQMKFVL QKLLTTIADA AKGYKPVAVP 350
    ARTPANAAVP ASTPLKQEWM WNQLGNFLQE GDVVIAETGT SAFGINQTTF 400
    PNNTYGISQV LWGSIGFTTG ATLGAAFAAE EIDPKKRVIL FIGDGSLQLT 450
    VQEISTMIRW GLKPYLFVLN NDGYTIEKLI HGPKAQYNEI QGWDHLSLLP 500
    TFGAKDYETH RVATTGEWDK LTQDKSFNDN SKIRMIEIML PVFDAPQNLV 550
    EQAKLTAATN AKQ 563
    Length:563
    Mass (Da):61,495
    Last modified:January 23, 2007 - v7
    Checksum:i799F85C3AC3FCAB6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti55 – 551A → R in CAA54522. (PubMed:3537965)Curated
    Sequence conflicti106 – 1061A → S in CAA28380. (PubMed:3537965)Curated
    Sequence conflicti106 – 1061A → S in CAA54522. (PubMed:3537965)Curated
    Sequence conflicti106 – 1061A → S in CAA54518. (PubMed:3537965)Curated
    Sequence conflicti106 – 1061A → S in CAA54521. (PubMed:3537965)Curated
    Sequence conflicti115 – 1151Missing in CAA28380. (PubMed:3537965)Curated
    Sequence conflicti143 – 1431A → C in CAA54522. (PubMed:3537965)Curated
    Sequence conflicti143 – 1431A → C in CAA54518. (PubMed:3537965)Curated
    Sequence conflicti143 – 1431A → C in CAA54521. (PubMed:3537965)Curated
    Sequence conflicti145 – 1462AP → PQ in CAA28380. (PubMed:3537965)Curated
    Sequence conflicti206 – 2061A → V in CAA28380. (PubMed:3537965)Curated
    Sequence conflicti208 – 2081V → A in CAA54522. (PubMed:3537965)Curated
    Sequence conflicti253 – 2531D → S in CAA28380. (PubMed:3537965)Curated
    Sequence conflicti253 – 2531D → S in CAA54522. (PubMed:3537965)Curated
    Sequence conflicti253 – 2531D → S in CAA54518. (PubMed:3537965)Curated
    Sequence conflicti253 – 2531D → S in CAA54521. (PubMed:3537965)Curated
    Sequence conflicti336 – 3361T → N in CAA28380. (PubMed:3537965)Curated
    Sequence conflicti336 – 3361T → N in CAA54522. (PubMed:3537965)Curated
    Sequence conflicti336 – 3361T → N in CAA54518. (PubMed:3537965)Curated
    Sequence conflicti336 – 3361T → N in CAA54521. (PubMed:3537965)Curated
    Sequence conflicti538 – 5381I → V in CAA28380. (PubMed:3537965)Curated
    Sequence conflicti538 – 5381I → V in CAA54522. (PubMed:3537965)Curated
    Sequence conflicti538 – 5381I → V in CAA54518. (PubMed:3537965)Curated
    Sequence conflicti538 – 5381I → V in CAA54521. (PubMed:3537965)Curated
    Sequence conflicti545 – 56319APQNL…TNAKQ → CSTKLG in CAA28380. (PubMed:3537965)CuratedAdd
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04675 Genomic DNA. Translation: CAA28380.1.
    X77316 Genomic DNA. Translation: CAA54522.1.
    X94607 Genomic DNA. Translation: CAA64291.1.
    Z73216 Genomic DNA. Translation: CAA97573.1.
    Z73217 Genomic DNA. Translation: CAA97575.1.
    X77312 Genomic DNA. Translation: CAA54518.1.
    X77315 Genomic DNA. Translation: CAA54521.1.
    BK006945 Genomic DNA. Translation: DAA09362.1.
    PIRiS64871. DCBYP.
    RefSeqiNP_013145.1. NM_001181931.1.

    Genome annotation databases

    EnsemblFungiiYLR044C; YLR044C; YLR044C.
    GeneIDi850733.
    KEGGisce:YLR044C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04675 Genomic DNA. Translation: CAA28380.1 .
    X77316 Genomic DNA. Translation: CAA54522.1 .
    X94607 Genomic DNA. Translation: CAA64291.1 .
    Z73216 Genomic DNA. Translation: CAA97573.1 .
    Z73217 Genomic DNA. Translation: CAA97575.1 .
    X77312 Genomic DNA. Translation: CAA54518.1 .
    X77315 Genomic DNA. Translation: CAA54521.1 .
    BK006945 Genomic DNA. Translation: DAA09362.1 .
    PIRi S64871. DCBYP.
    RefSeqi NP_013145.1. NM_001181931.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PVD X-ray 2.30 A/B 2-556 [» ]
    1PYD X-ray 2.40 A/B 1-556 [» ]
    1QPB X-ray 2.40 A/B 1-563 [» ]
    2VK1 X-ray 1.71 A/B/C/D 1-563 [» ]
    2VK8 X-ray 1.42 A/B/C/D 1-563 [» ]
    2W93 X-ray 1.60 A/B/C/D 1-563 [» ]
    ProteinModelPortali P06169.
    SMRi P06169. Positions 2-563.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31319. 121 interactions.
    DIPi DIP-6773N.
    IntActi P06169. 79 interactions.
    MINTi MINT-667063.

    2D gel databases

    COMPLUYEAST-2DPAGE P06169.
    SWISS-2DPAGE P06169.

    Proteomic databases

    MaxQBi P06169.
    PaxDbi P06169.
    PeptideAtlasi P06169.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR044C ; YLR044C ; YLR044C .
    GeneIDi 850733.
    KEGGi sce:YLR044C.

    Organism-specific databases

    SGDi S000004034. PDC1.

    Phylogenomic databases

    eggNOGi COG3961.
    GeneTreei ENSGT00550000075465.
    KOi K01568.
    OMAi LADACCS.
    OrthoDBi EOG779P6S.

    Enzyme and pathway databases

    UniPathwayi UPA00206 .
    UPA00866 .
    BioCyci MetaCyc:MONOMER3O-117.
    YEAST:MONOMER3O-117.
    BRENDAi 4.1.1.1. 984.
    SABIO-RK P06169.

    Miscellaneous databases

    EvolutionaryTracei P06169.
    NextBioi 966831.

    Gene expression databases

    Genevestigatori P06169.

    Family and domain databases

    Gene3Di 3.40.50.1220. 1 hit.
    3.40.50.970. 2 hits.
    InterProi IPR029035. DHS-like_NAD/FAD-binding_dom.
    IPR029061. THDP-binding.
    IPR012000. Thiamin_PyroP_enz_cen_dom.
    IPR012001. Thiamin_PyroP_enz_TPP-bd_dom.
    IPR000399. TPP-bd_CS.
    IPR012110. TPP_enzyme.
    IPR011766. TPP_enzyme-bd_C.
    [Graphical view ]
    PANTHERi PTHR18968:SF4. PTHR18968:SF4. 1 hit.
    Pfami PF02775. TPP_enzyme_C. 1 hit.
    PF00205. TPP_enzyme_M. 1 hit.
    PF02776. TPP_enzyme_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036565. Pyruvt_ip_decrb. 1 hit.
    SUPFAMi SSF52467. SSF52467. 1 hit.
    SSF52518. SSF52518. 2 hits.
    PROSITEi PS00187. TPP_ENZYMES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Analysis of the primary structure and promoter function of a pyruvate decarboxylase gene (PDC1) from Saccharomyces cerevisiae."
      Kellermann E., Seeboth P.G., Hollenberg C.P.
      Nucleic Acids Res. 14:8963-8977(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Autoregulation may control the expression of yeast pyruvate decarboxylase structural genes PDC1 and PDC5."
      Hohmann S., Cederberg H.
      Eur. J. Biochem. 188:615-621(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. Hohmann S.
      Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Eberhardt I., Cederberg H., Hohmann S.
      Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (MUTANTS PDC1-8 AND PDC1-803).
    7. Cited for: PROTEIN SEQUENCE OF 37-52.
      Strain: ATCC 204508 / S288c.
    8. "Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides."
      Norbeck J., Blomberg A.
      Electrophoresis 16:149-156(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 47-57; 260-269; 344-355; 486-497 AND 507-512.
      Strain: ATCC 38531 / Y41.
    9. "The influence of steric and electronic parameters on the substrate behavior of 2-oxo acids to yeast pyruvate decarboxylase."
      Lehmann H., Fischer G., Hubner G., Kohnert K.D., Schellenberger A.
      Eur. J. Biochem. 32:83-87(1973) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY.
    10. "Genetic analysis of the pyruvate decarboxylase reaction in yeast glycolysis."
      Schmitt H.D., Zimmermann F.K.
      J. Bacteriol. 151:1146-1152(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-291.
    11. "ERA, a novel cis-acting element required for autoregulation and ethanol repression of PDC1 transcription in Saccharomyces cerevisiae."
      Liesen T., Hollenberg C.P., Heinisch J.J.
      Mol. Microbiol. 21:621-632(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ETHANOL REPRESSION OF EXPRESSION.
    12. "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
      Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
      Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT SER-2.
    13. "A 13C nuclear magnetic resonance investigation of the metabolism of leucine to isoamyl alcohol in Saccharomyces cerevisiae."
      Dickinson J.R., Lanterman M.M., Danner D.J., Pearson B.M., Sanz P., Harrison S.J., Hewlins M.J.
      J. Biol. Chem. 272:26871-26878(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN AMINO ACID CATABOLISM.
    14. "An investigation of the metabolism of valine to isobutyl alcohol in Saccharomyces cerevisiae."
      Dickinson J.R., Harrison S.J., Hewlins M.J.
      J. Biol. Chem. 273:25751-25756(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN VALINE CATABOLISM.
    15. "Growth requirements of pyruvate-decarboxylase-negative Saccharomyces cerevisiae."
      Flikweert M.T., de Swaaf M., van Dijken J.P., Pronk J.T.
      FEMS Microbiol. Lett. 174:73-79(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CYTOSOLIC ACETYL-COA PRODUCTION.
    16. "Autoregulation of yeast pyruvate decarboxylase gene expression requires the enzyme but not its catalytic activity."
      Eberhardt I., Cederberg H., Li H., Konig S., Jordan F., Hohmann S.
      Eur. J. Biochem. 262:191-201(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOREGULATION OF PDC1 AND PDC5 EXPRESSION.
    17. "Identification and specificities of N-terminal acetyltransferases from Saccharomyces cerevisiae."
      Polevoda B., Norbeck J., Takakura H., Blomberg A., Sherman F.
      EMBO J. 18:6155-6168(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT SER-2.
    18. "An investigation of the metabolism of isoleucine to active Amyl alcohol in Saccharomyces cerevisiae."
      Dickinson J.R., Harrison S.J., Dickinson J.A., Hewlins M.J.
      J. Biol. Chem. 275:10937-10942(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN ISOLEUCINE CATABOLISM.
    19. "Generation of odorous acyloins by yeast pyruvate decarboxylases and their occurrence in sherry and soy sauce."
      Neuser F., Zorn H., Berger R.G.
      J. Agric. Food Chem. 48:6191-6195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, GENERATION OF ACYLOINS.
    20. "The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae."
      Dickinson J.R., Salgado L.E., Hewlins M.J.
      J. Biol. Chem. 278:8028-8034(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ROLE IN PHENYLALANINE; TRYPTOPHAN AND LEUCINE CATABOLISM.
    21. "Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae."
      Vuralhan Z., Morais M.A., Tai S.L., Piper M.D., Pronk J.T.
      Appl. Environ. Microbiol. 69:4534-4541(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AROMATIC AMINO ACIDS AS NITROGEN SOURCE.
    22. "Application of alpha-keto acid decarboxylases in biotransformations."
      Iding H., Siegert P., Mesch K., Pohl M.
      Biochim. Biophys. Acta 1385:307-322(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW, BIOTECHNOLOGICAL RELEVANCE.
    23. "Thiamin metabolism and thiamin diphosphate-dependent enzymes in the yeast Saccharomyces cerevisiae: genetic regulation."
      Hohmann S., Meacock P.A.
      Biochim. Biophys. Acta 1385:201-219(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    24. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    25. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    26. "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-223 AND THR-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    27. "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-223; THR-266 AND SER-526, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    28. "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-223; THR-336; THR-353 AND THR-522, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
      Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
      Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. "Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-A resolution."
      Dyda F., Furey W.F. Jr., Swaminathan S., Sax M., Farrenkopf B., Jordan F.
      Biochemistry 32:6165-6170(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-556 IN COMPLEX WITH THIAMINE PYROPHOSPHATE.
    31. "Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3-A resolution."
      Arjunan P., Umland T., Dyda F., Swaminathan S., Furey W.F. Jr., Sax M., Farrenkopf B., Gao Y., Zhang D., Jordan F.
      J. Mol. Biol. 256:590-600(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-556 IN COMPLEX WITH THIAMINE PYROPHOSPHATE.
    32. "The structural basis of substrate activation in yeast pyruvate decarboxylase. A crystallographic and kinetic study."
      Lu G., Dobritzsch D., Baumann S., Schneider G., Koenig S.
      Eur. J. Biochem. 267:861-868(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-556 IN COMPLEX WITH THIAMINE PYROPHOSPHATE AND SUBSTRATE ANALOG, SUBSTRATE ACTIVATION.

    Entry informationi

    Entry nameiPDC1_YEAST
    AccessioniPrimary (citable) accession number: P06169
    Secondary accession number(s): D6VY46
    , O00042, Q07991, Q12682, Q12686, Q12687
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 167 of the entry and version 7 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 8966 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3