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 03-AUG-2022, entry version 229.
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; 218.
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; P06169; -.
DR PRIDE; P06169; -.
DR TopDownProteomics; P06169; -.
DR EnsemblFungi; YLR044C_mRNA; YLR044C; YLR044C.
DR GeneID; 850733; -.
DR KEGG; sce:YLR044C; -.
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 BioCyc; MetaCyc:MON3O-117; -.
DR BioCyc; YEAST:MON3O-117; -.
DR BRENDA; 4.1.1.1; 984.
DR SABIO-RK; P06169; -.
DR UniPathway; UPA00206; -.
DR UniPathway; UPA00866; -.
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:0046809; C:replication compartment; IDA:SGD.
DR GO; GO:0047433; F:branched-chain-2-oxoacid decarboxylase activity; IMP:SGD.
DR GO; GO:0016831; F:carboxy-lyase activity; IBA:GO_Central.
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:0045069; P:regulation of viral genome replication; IMP:SGD.
DR GO; GO:0006569; P:tryptophan catabolic process; IGI:SGD.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
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; IPR012110; TPP_enzyme.
DR InterPro; IPR011766; TPP_enzyme-bd_C.
DR PANTHER; PTHR43452; PTHR43452; 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; SSF52467; 1.
DR SUPFAM; SSF52518; SSF52518; 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
