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Database: UniProt
Entry: PDC1_YEAST
LinkDB: PDC1_YEAST
Original site: PDC1_YEAST 
ID   PDC1_YEAST              Reviewed;         563 AA.
AC   P06169; D6VY46; O00042; Q07991; Q12682; Q12686; Q12687;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 7.
DT   24-JAN-2024, entry version 235.
DE   RecName: Full=Pyruvate decarboxylase isozyme 1 {ECO:0000303|PubMed:3537965};
DE            EC=4.1.1.- {ECO:0000269|PubMed:23642236, ECO:0000269|PubMed:4687392};
DE            EC=4.1.1.43 {ECO:0000269|PubMed:12499363};
DE            EC=4.1.1.72 {ECO:0000269|PubMed:10753893, ECO:0000269|PubMed:9748245};
DE            EC=4.1.1.74 {ECO:0000269|PubMed:12499363};
DE   AltName: Full=Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase;
DE            Short=2ODC;
GN   Name=PDC1 {ECO:0000303|PubMed:3537965}; OrderedLocusNames=YLR044C;
GN   ORFNames=L2104;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3537965; DOI=10.1093/nar/14.22.8963;
RA   Kellermann E., Seeboth P.G., Hollenberg C.P.;
RT   "Analysis of the primary structure and promoter function of a pyruvate
RT   decarboxylase gene (PDC1) from Saccharomyces cerevisiae.";
RL   Nucleic Acids Res. 14:8963-8977(1986).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=2185016; DOI=10.1111/j.1432-1033.1990.tb15442.x;
RA   Hohmann S., Cederberg H.;
RT   "Autoregulation may control the expression of yeast pyruvate decarboxylase
RT   structural genes PDC1 and PDC5.";
RL   Eur. J. Biochem. 188:615-621(1990).
RN   [3]
RP   SEQUENCE REVISION.
RA   Hohmann S.;
RL   Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(1997).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (MUTANTS PDC1-8 AND PDC1-803).
RA   Eberhardt I., Cederberg H., Hohmann S.;
RL   Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   PROTEIN SEQUENCE OF 37-52.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7895733; DOI=10.1002/elps.11501501210;
RA   Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
RA   Volpe T., Warner J.R., McLaughlin C.S.;
RT   "Protein identifications for a Saccharomyces cerevisiae protein database.";
RL   Electrophoresis 15:1466-1486(1994).
RN   [8]
RP   PROTEIN SEQUENCE OF 47-57; 260-269; 344-355; 486-497 AND 507-512.
RC   STRAIN=ATCC 38531 / Y41;
RX   PubMed=7737086; DOI=10.1002/elps.1150160124;
RA   Norbeck J., Blomberg A.;
RT   "Gene linkage of two-dimensional polyacrylamide gel electrophoresis
RT   resolved proteins from isogene families in Saccharomyces cerevisiae by
RT   microsequencing of in-gel trypsin generated peptides.";
RL   Electrophoresis 16:149-156(1995).
RN   [9]
RP   FUNCTION, AND ENZYME ACTIVITY.
RX   PubMed=4687392; DOI=10.1111/j.1432-1033.1973.tb02582.x;
RA   Lehmann H., Fischer G., Hubner G., Kohnert K.D., Schellenberger A.;
RT   "The influence of steric and electronic parameters on the substrate
RT   behavior of 2-oxo acids to yeast pyruvate decarboxylase.";
RL   Eur. J. Biochem. 32:83-87(1973).
RN   [10]
RP   MUTAGENESIS OF ASP-291.
RX   PubMed=7050079; DOI=10.1128/jb.151.3.1146-1152.1982;
RA   Schmitt H.D., Zimmermann F.K.;
RT   "Genetic analysis of the pyruvate decarboxylase reaction in yeast
RT   glycolysis.";
RL   J. Bacteriol. 151:1146-1152(1982).
RN   [11]
RP   FUNCTION.
RX   PubMed=6383467; DOI=10.1021/bi00311a002;
RA   Chen G.C., Jordan F.;
RT   "Brewers' yeast pyruvate decarboxylase produces acetoin from acetaldehyde:
RT   a novel tool to study the mechanism of steps subsequent to carbon dioxide
RT   loss.";
RL   Biochemistry 23:3576-3582(1984).
RN   [12]
RP   FUNCTION, AND ETHANOL REPRESSION OF EXPRESSION.
RX   PubMed=8866484; DOI=10.1111/j.1365-2958.1996.tb02570.x;
RA   Liesen T., Hollenberg C.P., Heinisch J.J.;
RT   "ERA, a novel cis-acting element required for autoregulation and ethanol
RT   repression of PDC1 transcription in Saccharomyces cerevisiae.";
RL   Mol. Microbiol. 21:621-632(1996).
RN   [13]
RP   ACETYLATION AT SER-2.
RX   PubMed=9298649; DOI=10.1002/elps.1150180810;
RA   Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,
RA   Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R.,
RA   Payne W.E.;
RT   "Proteome studies of Saccharomyces cerevisiae: identification and
RT   characterization of abundant proteins.";
RL   Electrophoresis 18:1347-1360(1997).
RN   [14]
RP   ROLE IN AMINO ACID CATABOLISM.
RX   PubMed=9341119; DOI=10.1074/jbc.272.43.26871;
RA   Dickinson J.R., Lanterman M.M., Danner D.J., Pearson B.M., Sanz P.,
RA   Harrison S.J., Hewlins M.J.;
RT   "A 13C nuclear magnetic resonance investigation of the metabolism of
RT   leucine to isoamyl alcohol in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 272:26871-26878(1997).
RN   [15]
RP   ROLE IN VALINE CATABOLISM.
RX   PubMed=9748245; DOI=10.1074/jbc.273.40.25751;
RA   Dickinson J.R., Harrison S.J., Hewlins M.J.;
RT   "An investigation of the metabolism of valine to isobutyl alcohol in
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 273:25751-25756(1998).
RN   [16]
RP   FUNCTION, AND CYTOSOLIC ACETYL-COA PRODUCTION.
RX   PubMed=10234824; DOI=10.1111/j.1574-6968.1999.tb13551.x;
RA   Flikweert M.T., de Swaaf M., van Dijken J.P., Pronk J.T.;
RT   "Growth requirements of pyruvate-decarboxylase-negative Saccharomyces
RT   cerevisiae.";
RL   FEMS Microbiol. Lett. 174:73-79(1999).
RN   [17]
RP   FUNCTION, AND AUTOREGULATION OF PDC1 AND PDC5 EXPRESSION.
RX   PubMed=10231381; DOI=10.1046/j.1432-1327.1999.00370.x;
RA   Eberhardt I., Cederberg H., Li H., Konig S., Jordan F., Hohmann S.;
RT   "Autoregulation of yeast pyruvate decarboxylase gene expression requires
RT   the enzyme but not its catalytic activity.";
RL   Eur. J. Biochem. 262:191-201(1999).
RN   [18]
RP   ACETYLATION AT SER-2.
RX   PubMed=10545125; DOI=10.1093/emboj/18.21.6155;
RA   Polevoda B., Norbeck J., Takakura H., Blomberg A., Sherman F.;
RT   "Identification and specificities of N-terminal acetyltransferases from
RT   Saccharomyces cerevisiae.";
RL   EMBO J. 18:6155-6168(1999).
RN   [19]
RP   ROLE IN ISOLEUCINE CATABOLISM.
RX   PubMed=10753893; DOI=10.1074/jbc.275.15.10937;
RA   Dickinson J.R., Harrison S.J., Dickinson J.A., Hewlins M.J.;
RT   "An investigation of the metabolism of isoleucine to active Amyl alcohol in
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 275:10937-10942(2000).
RN   [20]
RP   FUNCTION, AND GENERATION OF ACYLOINS.
RX   PubMed=11141278; DOI=10.1021/jf000535b;
RA   Neuser F., Zorn H., Berger R.G.;
RT   "Generation of odorous acyloins by yeast pyruvate decarboxylases and their
RT   occurrence in sherry and soy sauce.";
RL   J. Agric. Food Chem. 48:6191-6195(2000).
RN   [21]
RP   ROLE IN PHENYLALANINE; TRYPTOPHAN AND LEUCINE CATABOLISM.
RX   PubMed=12499363; DOI=10.1074/jbc.m211914200;
RA   Dickinson J.R., Salgado L.E., Hewlins M.J.;
RT   "The catabolism of amino acids to long chain and complex alcohols in
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 278:8028-8034(2003).
RN   [22]
RP   FUNCTION, AND AROMATIC AMINO ACIDS AS NITROGEN SOURCE.
RX   PubMed=12902239; DOI=10.1128/aem.69.8.4534-4541.2003;
RA   Vuralhan Z., Morais M.A., Tai S.L., Piper M.D., Pronk J.T.;
RT   "Identification and characterization of phenylpyruvate decarboxylase genes
RT   in Saccharomyces cerevisiae.";
RL   Appl. Environ. Microbiol. 69:4534-4541(2003).
RN   [23]
RP   REVIEW, AND BIOTECHNOLOGICAL RELEVANCE.
RX   PubMed=9655924; DOI=10.1016/s0167-4838(98)00076-4;
RA   Iding H., Siegert P., Mesch K., Pohl M.;
RT   "Application of alpha-keto acid decarboxylases in biotransformations.";
RL   Biochim. Biophys. Acta 1385:307-322(1998).
RN   [24]
RP   REVIEW.
RX   PubMed=9655908; DOI=10.1016/s0167-4838(98)00069-7;
RA   Hohmann S., Meacock P.A.;
RT   "Thiamin metabolism and thiamin diphosphate-dependent enzymes in the yeast
RT   Saccharomyces cerevisiae: genetic regulation.";
RL   Biochim. Biophys. Acta 1385:201-219(1998).
RN   [25]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [26]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [27]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND THR-353, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [28]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223; THR-266 AND SER-526, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [29]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223; THR-336; THR-353 AND
RP   THR-522, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [30]
RP   CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=22904058; DOI=10.1128/aem.01675-12;
RA   Romagnoli G., Luttik M.A., Koetter P., Pronk J.T., Daran J.M.;
RT   "Substrate specificity of thiamine pyrophosphate-dependent 2-oxo-acid
RT   decarboxylases in Saccharomyces cerevisiae.";
RL   Appl. Environ. Microbiol. 78:7538-7548(2012).
RN   [31]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-212; LYS-233; LYS-269;
RP   LYS-332; LYS-484; LYS-505 AND LYS-520, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
RN   [32]
RP   FUNCTION IN BUTANOL PRODUCTION.
RX   PubMed=23642236; DOI=10.1186/1754-6834-6-68;
RA   Branduardi P., Longo V., Berterame N.M., Rossi G., Porro D.;
RT   "A novel pathway to produce butanol and isobutanol in Saccharomyces
RT   cerevisiae.";
RL   Biotechnol. Biofuels 6:68-68(2013).
RN   [33]
RP   METHYLATION AT ARG-161.
RX   PubMed=26046779; DOI=10.1002/pmic.201500032;
RA   Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O.,
RA   Pears C., Schofield C.J., Kessler B.M.;
RT   "Expanding the yeast protein arginine methylome.";
RL   Proteomics 15:3232-3243(2015).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-556 IN COMPLEX WITH THIAMINE
RP   PYROPHOSPHATE.
RX   PubMed=8512926; DOI=10.1021/bi00075a008;
RA   Dyda F., Furey W.F. Jr., Swaminathan S., Sax M., Farrenkopf B., Jordan F.;
RT   "Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate
RT   decarboxylase at 2.4-A resolution.";
RL   Biochemistry 32:6165-6170(1993).
RN   [35]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-556 IN COMPLEX WITH THIAMINE
RP   PYROPHOSPHATE.
RX   PubMed=8604141; DOI=10.1006/jmbi.1996.0111;
RA   Arjunan P., Umland T., Dyda F., Swaminathan S., Furey W.F. Jr., Sax M.,
RA   Farrenkopf B., Gao Y., Zhang D., Jordan F.;
RT   "Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate
RT   decarboxylase from the yeast Saccharomyces cerevisiae at 2.3-A
RT   resolution.";
RL   J. Mol. Biol. 256:590-600(1996).
RN   [36] {ECO:0007744|PDB:1QPB}
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-556 IN COMPLEX WITH THIAMINE
RP   PYROPHOSPHATE AND SUBSTRATE ANALOG PYRUVAMIDE, SUBSTRATE ACTIVATION, AND
RP   COFACTOR.
RX   PubMed=10651824; DOI=10.1046/j.1432-1327.2000.01070.x;
RA   Lu G., Dobritzsch D., Baumann S., Schneider G., Koenig S.;
RT   "The structural basis of substrate activation in yeast pyruvate
RT   decarboxylase. A crystallographic and kinetic study.";
RL   Eur. J. Biochem. 267:861-868(2000).
CC   -!- FUNCTION: Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6)
CC       implicated in the nonoxidative conversion of pyruvate to acetaldehyde
CC       and carbon dioxide during alcoholic fermentation. Most of the produced
CC       acetaldehyde is subsequently reduced to ethanol, but some is required
CC       for cytosolic acetyl-CoA production for biosynthetic pathways. The
CC       enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6,
CC       ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-
CC       ketoacids) than pyruvate, which seem mainly involved in amino acid
CC       catabolism. Here the enzyme catalyzes the decarboxylation of amino
CC       acids, which, in a first step, have been transaminated to the
CC       corresponding 2-oxo acids. In a third step, the resulting aldehydes are
CC       reduced to alcohols, collectively referred to as fusel oils or
CC       alcohols. Its preferred substrates are the transaminated amino acids
CC       derived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate),
CC       valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate),
CC       isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-
CC       methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-
CC       (indol-3-yl)pyruvate), whereas transaminated leucine is no substrate.
CC       In a side-reaction the carbanionic intermediate (or active aldehyde)
CC       generated by decarboxylation or by activation of an aldehyde can react
CC       with an aldehyde via condensation (or carboligation) yielding a 2-
CC       hydroxy ketone, collectively called acyloins.
CC       {ECO:0000269|PubMed:10231381, ECO:0000269|PubMed:10234824,
CC       ECO:0000269|PubMed:10753893, ECO:0000269|PubMed:11141278,
CC       ECO:0000269|PubMed:12499363, ECO:0000269|PubMed:12902239,
CC       ECO:0000269|PubMed:22904058, ECO:0000269|PubMed:4687392,
CC       ECO:0000269|PubMed:8866484, ECO:0000269|PubMed:9341119,
CC       ECO:0000269|PubMed:9748245}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + pyruvate = acetaldehyde + CO2; Xref=Rhea:RHEA:45484,
CC         ChEBI:CHEBI:15343, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526; Evidence={ECO:0000269|PubMed:4687392};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-methyl-2-oxobutanoate + H(+) = 2-methylpropanal + CO2;
CC         Xref=Rhea:RHEA:54356, ChEBI:CHEBI:11851, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:48943; EC=4.1.1.72;
CC         Evidence={ECO:0000269|PubMed:9748245};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-3-methyl-2-oxopentanoate + H(+) = 2-methylbutanal + CO2;
CC         Xref=Rhea:RHEA:21108, ChEBI:CHEBI:15378, ChEBI:CHEBI:16182,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:35146; EC=4.1.1.72;
CC         Evidence={ECO:0000269|PubMed:10753893};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + indole-3-pyruvate = CO2 + indole-3-acetaldehyde;
CC         Xref=Rhea:RHEA:18017, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17640, ChEBI:CHEBI:18086; EC=4.1.1.74;
CC         Evidence={ECO:0000269|PubMed:12499363};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-phenylpyruvate + H(+) = 2-phenylacetaldehyde + CO2;
CC         Xref=Rhea:RHEA:14185, ChEBI:CHEBI:15378, ChEBI:CHEBI:16424,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:18005; EC=4.1.1.43;
CC         Evidence={ECO:0000269|PubMed:12499363};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxobutanoate + H(+) = CO2 + propanal; Xref=Rhea:RHEA:55072,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:16763,
CC         ChEBI:CHEBI:17153; Evidence={ECO:0000269|PubMed:22904058};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxopentanoate + H(+) = butanal + CO2; Xref=Rhea:RHEA:50312,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15743, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:28644; Evidence={ECO:0000269|PubMed:22904058,
CC         ECO:0000269|PubMed:23642236};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 acetaldehyde = acetoin; Xref=Rhea:RHEA:54364,
CC         ChEBI:CHEBI:15343, ChEBI:CHEBI:15688;
CC         Evidence={ECO:0000269|PubMed:11141278, ECO:0000305|PubMed:6383467};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetaldehyde + H(+) + pyruvate = acetoin + CO2;
CC         Xref=Rhea:RHEA:54368, ChEBI:CHEBI:15343, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15688, ChEBI:CHEBI:16526;
CC         Evidence={ECO:0000269|PubMed:11141278, ECO:0000305|PubMed:6383467};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:10651824};
CC       Note=Binds 1 Mg(2+) per subunit. {ECO:0000269|PubMed:10651824};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000269|PubMed:10651824};
CC       Note=Binds 1 thiamine pyrophosphate per subunit.
CC       {ECO:0000269|PubMed:10651824};
CC   -!- ACTIVITY REGULATION: Allosterically activated by its substrate,
CC       pyruvate. {ECO:0000269|PubMed:10651824}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.8 mM for pyruvate {ECO:0000269|PubMed:22904058};
CC         KM=1.0 mM for 2-oxobutanoate {ECO:0000269|PubMed:22904058};
CC         KM=1.5 mM for 2-oxopentanoate {ECO:0000269|PubMed:22904058};
CC         Vmax=1.5 umol/min/mg enzyme for pyruvate
CC         {ECO:0000269|PubMed:22904058};
CC         Vmax=0.5 umol/min/mg enzyme for 2-oxobutanoate
CC         {ECO:0000269|PubMed:22904058};
CC         Vmax=0.4 umol/min/mg enzyme for 2-oxopentanoate
CC         {ECO:0000269|PubMed:22904058};
CC         Vmax=38 umol/min/mg enzyme for 3-methyl-2-oxobutanoate
CC         {ECO:0000269|PubMed:22904058};
CC         Vmax=15 umol/min/mg enzyme for 4-methyl-2-oxopentanoate
CC         {ECO:0000269|PubMed:22904058};
CC         Vmax=9 umol/min/mg enzyme for 3-methyl-2-oxopentanoate
CC         {ECO:0000269|PubMed:22904058};
CC         Vmax=41 umol/min/mg enzyme for 4-methylthio-2-oxobutanoate
CC         {ECO:0000269|PubMed:22904058};
CC   -!- PATHWAY: Fermentation; ethanol fermentation.
CC   -!- PATHWAY: Amino-acid degradation; Ehrlich pathway.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10651824,
CC       ECO:0000269|PubMed:8512926, ECO:0000269|PubMed:8604141}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: Protein expression is strongly induced by high
CC       concentrations of fermentable carbon sources and under anaerobic growth
CC       conditions and is repressed by ethanol. Protein expression level is
CC       also autoregulated through an unknown mechanism.
CC   -!- PTM: Cleavage of N-terminal methionine and N-terminal acetylation by
CC       NAT1/ARD1. {ECO:0000269|PubMed:10545125, ECO:0000269|PubMed:9298649}.
CC   -!- BIOTECHNOLOGY: Fusel oils and acyloins are important flavor and aroma
CC       compounds in yeast-fermented products contributing to the quality of
CC       beverages and food, e.g. fusel oils in whiskey, contrary to common
CC       believe, seem to alleviate hangover. In general they are desirable at
CC       low concentrations, whereas high concentrations may spoil the product.
CC       By adjusting growth conditions and substrate their production is sought
CC       to be influenced. Due to their broad substrate tolerance pyruvate
CC       decarboxylases are important biocatalysts for chemoenzymatic syntheses,
CC       both by fermentation and in vitro, e.g. in the production of ephedrine,
CC       vitamin E, or phenylethanol (rose flavor).
CC       {ECO:0000269|PubMed:9655924}.
CC   -!- MISCELLANEOUS: Present with 8966 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR   EMBL; X04675; CAA28380.1; -; Genomic_DNA.
DR   EMBL; X77316; CAA54522.1; -; Genomic_DNA.
DR   EMBL; X94607; CAA64291.1; -; Genomic_DNA.
DR   EMBL; Z73216; CAA97573.1; -; Genomic_DNA.
DR   EMBL; Z73217; CAA97575.1; -; Genomic_DNA.
DR   EMBL; X77312; CAA54518.1; -; Genomic_DNA.
DR   EMBL; X77315; CAA54521.1; -; Genomic_DNA.
DR   EMBL; BK006945; DAA09362.1; -; Genomic_DNA.
DR   PIR; S64871; DCBYP.
DR   RefSeq; NP_013145.1; NM_001181931.1.
DR   PDB; 1PVD; X-ray; 2.30 A; A/B=2-556.
DR   PDB; 1PYD; X-ray; 2.40 A; A/B=1-556.
DR   PDB; 1QPB; X-ray; 2.40 A; A/B=1-563.
DR   PDB; 2VK1; X-ray; 1.71 A; A/B/C/D=1-563.
DR   PDB; 2VK8; X-ray; 1.42 A; A/B/C/D=1-563.
DR   PDB; 2W93; X-ray; 1.60 A; A/B/C/D=1-563.
DR   PDBsum; 1PVD; -.
DR   PDBsum; 1PYD; -.
DR   PDBsum; 1QPB; -.
DR   PDBsum; 2VK1; -.
DR   PDBsum; 2VK8; -.
DR   PDBsum; 2W93; -.
DR   AlphaFoldDB; P06169; -.
DR   SMR; P06169; -.
DR   BioGRID; 31319; 223.
DR   DIP; DIP-6773N; -.
DR   IntAct; P06169; 134.
DR   MINT; P06169; -.
DR   STRING; 4932.YLR044C; -.
DR   CarbonylDB; P06169; -.
DR   iPTMnet; P06169; -.
DR   COMPLUYEAST-2DPAGE; P06169; -.
DR   SWISS-2DPAGE; P06169; -.
DR   MaxQB; P06169; -.
DR   PaxDb; 4932-YLR044C; -.
DR   PeptideAtlas; P06169; -.
DR   TopDownProteomics; P06169; -.
DR   EnsemblFungi; YLR044C_mRNA; YLR044C; YLR044C.
DR   GeneID; 850733; -.
DR   KEGG; sce:YLR044C; -.
DR   AGR; SGD:S000004034; -.
DR   SGD; S000004034; PDC1.
DR   VEuPathDB; FungiDB:YLR044C; -.
DR   eggNOG; KOG1184; Eukaryota.
DR   GeneTree; ENSGT00940000176336; -.
DR   HOGENOM; CLU_013748_0_2_1; -.
DR   InParanoid; P06169; -.
DR   OMA; EQRYNDI; -.
DR   OrthoDB; 1000728at2759; -.
DR   BioCyc; MetaCyc:MONOMER3O-117; -.
DR   BioCyc; YEAST:MONOMER3O-117; -.
DR   BRENDA; 4.1.1.1; 984.
DR   SABIO-RK; P06169; -.
DR   UniPathway; UPA00206; -.
DR   UniPathway; UPA00866; -.
DR   BioGRID-ORCS; 850733; 1 hit in 10 CRISPR screens.
DR   EvolutionaryTrace; P06169; -.
DR   PRO; PR:P06169; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P06169; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0047433; F:branched-chain-2-oxoacid decarboxylase activity; IMP:SGD.
DR   GO; GO:0047434; F:indolepyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0050177; F:phenylpyruvate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004737; F:pyruvate decarboxylase activity; IDA:SGD.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0000949; P:aromatic amino acid family catabolic process to alcohol via Ehrlich pathway; IGI:SGD.
DR   GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0019655; P:glycolytic fermentation to ethanol; IDA:SGD.
DR   GO; GO:0006559; P:L-phenylalanine catabolic process; IGI:SGD.
DR   GO; GO:0006090; P:pyruvate metabolic process; IDA:SGD.
DR   GO; GO:0006569; P:tryptophan catabolic process; IGI:SGD.
DR   CDD; cd02005; TPP_PDC_IPDC; 1.
DR   CDD; cd07038; TPP_PYR_PDC_IPDC_like; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR   InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR   InterPro; IPR012110; PDC/IPDC-like.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR   InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   InterPro; IPR047214; TPP_PDC_IPDC.
DR   InterPro; IPR047213; TPP_PYR_PDC_IPDC-like.
DR   PANTHER; PTHR43452; PYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43452:SF30; PYRUVATE DECARBOXYLASE ISOZYME 1-RELATED; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   Pfam; PF00205; TPP_enzyme_M; 1.
DR   Pfam; PF02776; TPP_enzyme_N; 1.
DR   PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Allosteric enzyme;
KW   Branched-chain amino acid catabolism; Cytoplasm; Decarboxylase;
KW   Direct protein sequencing; Isopeptide bond; Lyase; Magnesium;
KW   Metal-binding; Methylation; Nucleus; Phenylalanine catabolism;
KW   Phosphoprotein; Reference proteome; Thiamine pyrophosphate;
KW   Tryptophan catabolism; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:10545125,
FT                   ECO:0000269|PubMed:9298649"
FT   CHAIN           2..563
FT                   /note="Pyruvate decarboxylase isozyme 1"
FT                   /id="PRO_0000090770"
FT   BINDING         28
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate; ligand shared between two
FT                   neighboring subunits"
FT                   /evidence="ECO:0000305|PubMed:10651824"
FT   BINDING         115
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate; ligand shared between two
FT                   neighboring subunits"
FT                   /evidence="ECO:0000305|PubMed:10651824,
FT                   ECO:0007744|PDB:1QPB"
FT   BINDING         157
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="2"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000305|PubMed:10651824"
FT   BINDING         224
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="2"
FT                   /ligand_note="allosteric activator"
FT                   /evidence="ECO:0000305|PubMed:10651824,
FT                   ECO:0007744|PDB:1QPB"
FT   BINDING         390
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000269|PubMed:10651824,
FT                   ECO:0007744|PDB:1QPB"
FT   BINDING         413..415
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000269|PubMed:10651824,
FT                   ECO:0007744|PDB:1QPB"
FT   BINDING         444
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:10651824,
FT                   ECO:0007744|PDB:1QPB"
FT   BINDING         445..446
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000269|PubMed:10651824,
FT                   ECO:0007744|PDB:1QPB"
FT   BINDING         471..476
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000269|PubMed:10651824,
FT                   ECO:0007744|PDB:1QPB"
FT   BINDING         471
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:10651824,
FT                   ECO:0007744|PDB:1QPB"
FT   BINDING         473
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000269|PubMed:10651824,
FT                   ECO:0007744|PDB:1QPB"
FT   BINDING         477
FT                   /ligand="pyruvate"
FT                   /ligand_id="ChEBI:CHEBI:15361"
FT                   /ligand_label="1"
FT                   /ligand_note="substrate; ligand shared between two
FT                   neighboring subunits"
FT                   /evidence="ECO:0000305|PubMed:10651824"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:10545125,
FT                   ECO:0000269|PubMed:9298649"
FT   MOD_RES         161
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000269|PubMed:26046779"
FT   MOD_RES         223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT   MOD_RES         266
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         336
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         353
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17330950,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         522
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         526
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   CROSSLNK        212
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        233
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        269
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        332
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        484
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        505
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   CROSSLNK        520
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   MUTAGEN         291
FT                   /note="D->N: In PDC1-8; reduces catalytic activity to 10%
FT                   but retains autoregulatory activity."
FT                   /evidence="ECO:0000269|PubMed:7050079"
FT   CONFLICT        55
FT                   /note="A -> R (in Ref. 1; CAA54522)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="A -> S (in Ref. 1; CAA28380/CAA54522/CAA54518/
FT                   CAA54521)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        115
FT                   /note="Missing (in Ref. 1; CAA28380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        143
FT                   /note="A -> C (in Ref. 1; CAA54522/CAA54518/CAA54521)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        145..146
FT                   /note="AP -> PQ (in Ref. 1; CAA28380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        206
FT                   /note="A -> V (in Ref. 1; CAA28380)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        208
FT                   /note="V -> A (in Ref. 1; CAA54522)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        253
FT                   /note="D -> S (in Ref. 1; CAA28380/CAA54522/CAA54518/
FT                   CAA54521)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        336
FT                   /note="T -> N (in Ref. 1; CAA28380/CAA54522/CAA54518/
FT                   CAA54521)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        538
FT                   /note="I -> V (in Ref. 1; CAA28380/CAA54522/CAA54518/
FT                   CAA54521)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        545..563
FT                   /note="APQNLVEQAKLTAATNAKQ -> CSTKLG (in Ref. 1; CAA28380)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..5
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           6..16
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          21..24
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           28..30
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           31..35
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           36..39
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           51..65
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           76..91
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          95..101
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           104..108
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          109..111
FT                   /evidence="ECO:0007829|PDB:1QPB"
FT   STRAND          114..116
FT                   /evidence="ECO:0007829|PDB:1QPB"
FT   STRAND          118..120
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           124..130
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          134..138
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   TURN            142..144
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           145..159
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          163..168
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           171..173
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           178..182
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           194..210
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          212..218
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           220..224
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           228..238
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          242..244
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   TURN            246..250
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          259..262
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           265..267
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           270..277
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          280..286
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   TURN            291..297
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          306..309
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          311..316
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          319..322
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           326..340
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   TURN            341..343
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           367..374
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   TURN            375..377
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          383..386
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           390..394
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           395..397
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          405..407
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   TURN            410..412
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           417..432
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          438..443
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           444..450
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           451..453
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           454..459
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          465..473
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           475..480
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           486..488
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           495..497
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           498..501
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          505..512
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           515..522
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   TURN            525..528
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   STRAND          531..539
FT                   /evidence="ECO:0007829|PDB:2VK8"
FT   HELIX           547..561
FT                   /evidence="ECO:0007829|PDB:2VK8"
SQ   SEQUENCE   563 AA;  61495 MW;  799F85C3AC3FCAB6 CRC64;
     MSEITLGKYL FERLKQVNVN TVFGLPGDFN LSLLDKIYEV EGMRWAGNAN ELNAAYAADG
     YARIKGMSCI ITTFGVGELS ALNGIAGSYA EHVGVLHVVG VPSISAQAKQ LLLHHTLGNG
     DFTVFHRMSA NISETTAMIT DIATAPAEID RCIRTTYVTQ RPVYLGLPAN LVDLNVPAKL
     LQTPIDMSLK PNDAESEKEV IDTILALVKD AKNPVILADA CCSRHDVKAE TKKLIDLTQF
     PAFVTPMGKG SIDEQHPRYG GVYVGTLSKP EVKEAVESAD LILSVGALLS DFNTGSFSYS
     YKTKNIVEFH SDHMKIRNAT FPGVQMKFVL QKLLTTIADA AKGYKPVAVP ARTPANAAVP
     ASTPLKQEWM WNQLGNFLQE GDVVIAETGT SAFGINQTTF PNNTYGISQV LWGSIGFTTG
     ATLGAAFAAE EIDPKKRVIL FIGDGSLQLT VQEISTMIRW GLKPYLFVLN NDGYTIEKLI
     HGPKAQYNEI QGWDHLSLLP TFGAKDYETH RVATTGEWDK LTQDKSFNDN SKIRMIEIML
     PVFDAPQNLV EQAKLTAATN AKQ
//
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