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Pyruvate decarboxylase isozyme 1 (EC 4.1.1.-) (EC 4.1.1.1) (EC 4.1.1.43) (EC 4.1.1.74)

 PDC1_YEAST              Reviewed;         563 AA.
P06169; D6VY46; O00042; Q07991; Q12682; Q12686; Q12687;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 7.
05-JUL-2017, entry version 194.
RecName: Full=Pyruvate decarboxylase isozyme 1;
EC=4.1.1.- {ECO:0000305|PubMed:4687392};
EC=4.1.1.1 {ECO:0000269|PubMed:4687392};
EC=4.1.1.43 {ECO:0000269|PubMed:12499363};
EC=4.1.1.74 {ECO:0000269|PubMed:12499363};
Name=PDC1; OrderedLocusNames=YLR044C; ORFNames=L2104;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3537965; DOI=10.1093/nar/14.22.8963;
Kellermann E., Seeboth P.G., Hollenberg C.P.;
"Analysis of the primary structure and promoter function of a pyruvate
decarboxylase gene (PDC1) from Saccharomyces cerevisiae.";
Nucleic Acids Res. 14:8963-8977(1986).
[2]
SEQUENCE REVISION.
PubMed=2185016; DOI=10.1111/j.1432-1033.1990.tb15442.x;
Hohmann S., Cederberg H.;
"Autoregulation may control the expression of yeast pyruvate
decarboxylase structural genes PDC1 and PDC5.";
Eur. J. Biochem. 188:615-621(1990).
[3]
SEQUENCE REVISION.
Hohmann S.;
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
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.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[5]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (MUTANTS PDC1-8 AND PDC1-803).
Eberhardt I., Cederberg H., Hohmann S.;
Submitted (FEB-1994) to the EMBL/GenBank/DDBJ databases.
[7]
PROTEIN SEQUENCE OF 37-52.
STRAIN=ATCC 204508 / S288c;
PubMed=7895733; DOI=10.1002/elps.11501501210;
Garrels J.I., Futcher B., Kobayashi R., Latter G.I., Schwender B.,
Volpe T., Warner J.R., McLaughlin C.S.;
"Protein identifications for a Saccharomyces cerevisiae protein
database.";
Electrophoresis 15:1466-1486(1994).
[8]
PROTEIN SEQUENCE OF 47-57; 260-269; 344-355; 486-497 AND 507-512.
STRAIN=ATCC 38531 / Y41;
PubMed=7737086; DOI=10.1002/elps.1150160124;
Norbeck J., Blomberg A.;
"Gene linkage of two-dimensional polyacrylamide gel electrophoresis
resolved proteins from isogene families in Saccharomyces cerevisiae by
microsequencing of in-gel trypsin generated peptides.";
Electrophoresis 16:149-156(1995).
[9]
FUNCTION, AND ENZYME ACTIVITY.
PubMed=4687392; DOI=10.1111/j.1432-1033.1973.tb02582.x;
Lehmann H., Fischer G., Hubner G., Kohnert K.D., Schellenberger A.;
"The influence of steric and electronic parameters on the substrate
behavior of 2-oxo acids to yeast pyruvate decarboxylase.";
Eur. J. Biochem. 32:83-87(1973).
[10]
MUTAGENESIS OF ASP-291.
PubMed=7050079;
Schmitt H.D., Zimmermann F.K.;
"Genetic analysis of the pyruvate decarboxylase reaction in yeast
glycolysis.";
J. Bacteriol. 151:1146-1152(1982).
[11]
FUNCTION, AND ETHANOL REPRESSION OF EXPRESSION.
PubMed=8866484; DOI=10.1111/j.1365-2958.1996.tb02570.x;
Liesen T., Hollenberg C.P., Heinisch J.J.;
"ERA, a novel cis-acting element required for autoregulation and
ethanol repression of PDC1 transcription in Saccharomyces
cerevisiae.";
Mol. Microbiol. 21:621-632(1996).
[12]
ACETYLATION AT SER-2.
PubMed=9298649; DOI=10.1002/elps.1150180810;
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.;
"Proteome studies of Saccharomyces cerevisiae: identification and
characterization of abundant proteins.";
Electrophoresis 18:1347-1360(1997).
[13]
ROLE IN AMINO ACID CATABOLISM.
PubMed=9341119; DOI=10.1074/jbc.272.43.26871;
Dickinson J.R., Lanterman M.M., Danner D.J., Pearson B.M., Sanz P.,
Harrison S.J., Hewlins M.J.;
"A 13C nuclear magnetic resonance investigation of the metabolism of
leucine to isoamyl alcohol in Saccharomyces cerevisiae.";
J. Biol. Chem. 272:26871-26878(1997).
[14]
ROLE IN VALINE CATABOLISM.
PubMed=9748245; DOI=10.1074/jbc.273.40.25751;
Dickinson J.R., Harrison S.J., Hewlins M.J.;
"An investigation of the metabolism of valine to isobutyl alcohol in
Saccharomyces cerevisiae.";
J. Biol. Chem. 273:25751-25756(1998).
[15]
FUNCTION, AND CYTOSOLIC ACETYL-COA PRODUCTION.
PubMed=10234824; DOI=10.1111/j.1574-6968.1999.tb13551.x;
Flikweert M.T., de Swaaf M., van Dijken J.P., Pronk J.T.;
"Growth requirements of pyruvate-decarboxylase-negative Saccharomyces
cerevisiae.";
FEMS Microbiol. Lett. 174:73-79(1999).
[16]
FUNCTION, AND AUTOREGULATION OF PDC1 AND PDC5 EXPRESSION.
PubMed=10231381; DOI=10.1046/j.1432-1327.1999.00370.x;
Eberhardt I., Cederberg H., Li H., Konig S., Jordan F., Hohmann S.;
"Autoregulation of yeast pyruvate decarboxylase gene expression
requires the enzyme but not its catalytic activity.";
Eur. J. Biochem. 262:191-201(1999).
[17]
ACETYLATION AT SER-2.
PubMed=10545125; DOI=10.1093/emboj/18.21.6155;
Polevoda B., Norbeck J., Takakura H., Blomberg A., Sherman F.;
"Identification and specificities of N-terminal acetyltransferases
from Saccharomyces cerevisiae.";
EMBO J. 18:6155-6168(1999).
[18]
ROLE IN ISOLEUCINE CATABOLISM.
PubMed=10753893; DOI=10.1074/jbc.275.15.10937;
Dickinson J.R., Harrison S.J., Dickinson J.A., Hewlins M.J.;
"An investigation of the metabolism of isoleucine to active Amyl
alcohol in Saccharomyces cerevisiae.";
J. Biol. Chem. 275:10937-10942(2000).
[19]
FUNCTION, AND GENERATION OF ACYLOINS.
PubMed=11141278; DOI=10.1021/jf000535b;
Neuser F., Zorn H., Berger R.G.;
"Generation of odorous acyloins by yeast pyruvate decarboxylases and
their occurrence in sherry and soy sauce.";
J. Agric. Food Chem. 48:6191-6195(2000).
[20]
ROLE IN PHENYLALANINE; TRYPTOPHAN AND LEUCINE CATABOLISM.
PubMed=12499363; DOI=10.1074/jbc.M211914200;
Dickinson J.R., Salgado L.E., Hewlins M.J.;
"The catabolism of amino acids to long chain and complex alcohols in
Saccharomyces cerevisiae.";
J. Biol. Chem. 278:8028-8034(2003).
[21]
FUNCTION, AND AROMATIC AMINO ACIDS AS NITROGEN SOURCE.
PubMed=12902239; DOI=10.1128/AEM.69.8.4534-4541.2003;
Vuralhan Z., Morais M.A., Tai S.L., Piper M.D., Pronk J.T.;
"Identification and characterization of phenylpyruvate decarboxylase
genes in Saccharomyces cerevisiae.";
Appl. Environ. Microbiol. 69:4534-4541(2003).
[22]
REVIEW, AND BIOTECHNOLOGICAL RELEVANCE.
PubMed=9655924; DOI=10.1016/S0167-4838(98)00076-4;
Iding H., Siegert P., Mesch K., Pohl M.;
"Application of alpha-keto acid decarboxylases in
biotransformations.";
Biochim. Biophys. Acta 1385:307-322(1998).
[23]
REVIEW.
PubMed=9655908; DOI=10.1016/S0167-4838(98)00069-7;
Hohmann S., Meacock P.A.;
"Thiamin metabolism and thiamin diphosphate-dependent enzymes in the
yeast Saccharomyces cerevisiae: genetic regulation.";
Biochim. Biophys. Acta 1385:201-219(1998).
[24]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[25]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223 AND THR-353, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223; THR-266 AND
SER-526, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223; THR-336; THR-353
AND THR-522, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[29]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-212; LYS-233; LYS-269;
LYS-332; LYS-484; LYS-505 AND LYS-520, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[30]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-556 IN COMPLEX WITH
THIAMINE PYROPHOSPHATE.
PubMed=8512926; DOI=10.1021/bi00075a008;
Dyda F., Furey W.F. Jr., Swaminathan S., Sax M., Farrenkopf B.,
Jordan F.;
"Catalytic centers in the thiamin diphosphate dependent enzyme
pyruvate decarboxylase at 2.4-A resolution.";
Biochemistry 32:6165-6170(1993).
[31]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-556 IN COMPLEX WITH
THIAMINE PYROPHOSPHATE.
PubMed=8604141; DOI=10.1006/jmbi.1996.0111;
Arjunan P., Umland T., Dyda F., Swaminathan S., Furey W.F. Jr.,
Sax M., Farrenkopf B., Gao Y., Zhang D., Jordan F.;
"Crystal structure of the thiamin diphosphate-dependent enzyme
pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3-
A resolution.";
J. Mol. Biol. 256:590-600(1996).
[32]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-556 IN COMPLEX WITH
THIAMINE PYROPHOSPHATE AND SUBSTRATE ANALOG, AND SUBSTRATE ACTIVATION.
PubMed=10651824; DOI=10.1046/j.1432-1327.2000.01070.x;
Lu G., Dobritzsch D., Baumann S., Schneider G., Koenig S.;
"The structural basis of substrate activation in yeast pyruvate
decarboxylase. A crystallographic and kinetic study.";
Eur. J. Biochem. 267:861-868(2000).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:10231381, ECO:0000269|PubMed:10234824,
ECO:0000269|PubMed:10753893, ECO:0000269|PubMed:11141278,
ECO:0000269|PubMed:12499363, ECO:0000269|PubMed:12902239,
ECO:0000269|PubMed:4687392, ECO:0000269|PubMed:8866484,
ECO:0000269|PubMed:9341119, ECO:0000269|PubMed:9748245}.
-!- CATALYTIC ACTIVITY: A 2-oxo acid = an aldehyde + CO(2).
{ECO:0000269|PubMed:4687392}.
-!- CATALYTIC ACTIVITY: Pyruvate = Acetaldehyde + CO(2).
{ECO:0000269|PubMed:4687392}.
-!- CATALYTIC ACTIVITY: Phenylpyruvate = phenylacetaldehyde + CO(2).
{ECO:0000269|PubMed:12499363}.
-!- CATALYTIC ACTIVITY: 3-(indol-3-yl)pyruvate = 2-(indol-3-
yl)acetaldehyde + CO(2). {ECO:0000269|PubMed:12499363}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 1 Mg(2+) per subunit.;
-!- COFACTOR:
Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
Note=Binds 1 thiamine pyrophosphate per subunit.;
-!- ENZYME REGULATION: Allosterically activated by substrate.
-!- PATHWAY: Fermentation; ethanol fermentation.
-!- PATHWAY: Amino-acid degradation; Ehrlich pathway.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10651824,
ECO:0000269|PubMed:8512926, ECO:0000269|PubMed:8604141}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
Nucleus {ECO:0000269|PubMed:14562095}.
-!- INDUCTION: 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.
-!- PTM: Cleavage of N-terminal methionine and N-terminal acetylation
by NAT1/ARD1. {ECO:0000269|PubMed:10545125,
ECO:0000269|PubMed:9298649}.
-!- BIOTECHNOLOGY: 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). {ECO:0000269|PubMed:9655924}.
-!- MISCELLANEOUS: Present with 8966 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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EMBL; X04675; CAA28380.1; -; Genomic_DNA.
EMBL; X77316; CAA54522.1; -; Genomic_DNA.
EMBL; X94607; CAA64291.1; -; Genomic_DNA.
EMBL; Z73216; CAA97573.1; -; Genomic_DNA.
EMBL; Z73217; CAA97575.1; -; Genomic_DNA.
EMBL; X77312; CAA54518.1; -; Genomic_DNA.
EMBL; X77315; CAA54521.1; -; Genomic_DNA.
EMBL; BK006945; DAA09362.1; -; Genomic_DNA.
PIR; S64871; DCBYP.
RefSeq; NP_013145.1; NM_001181931.1.
PDB; 1PVD; X-ray; 2.30 A; A/B=2-556.
PDB; 1PYD; X-ray; 2.40 A; A/B=1-556.
PDB; 1QPB; X-ray; 2.40 A; A/B=1-563.
PDB; 2VK1; X-ray; 1.71 A; A/B/C/D=1-563.
PDB; 2VK8; X-ray; 1.42 A; A/B/C/D=1-563.
PDB; 2W93; X-ray; 1.60 A; A/B/C/D=1-563.
PDBsum; 1PVD; -.
PDBsum; 1PYD; -.
PDBsum; 1QPB; -.
PDBsum; 2VK1; -.
PDBsum; 2VK8; -.
PDBsum; 2W93; -.
ProteinModelPortal; P06169; -.
SMR; P06169; -.
BioGrid; 31319; 165.
DIP; DIP-6773N; -.
IntAct; P06169; 79.
MINT; MINT-667063; -.
STRING; 4932.YLR044C; -.
iPTMnet; P06169; -.
COMPLUYEAST-2DPAGE; P06169; -.
SWISS-2DPAGE; P06169; -.
MaxQB; P06169; -.
PRIDE; P06169; -.
TopDownProteomics; P06169; -.
EnsemblFungi; YLR044C; YLR044C; YLR044C.
GeneID; 850733; -.
KEGG; sce:YLR044C; -.
EuPathDB; FungiDB:YLR044C; -.
SGD; S000004034; PDC1.
GeneTree; ENSGT00550000075465; -.
InParanoid; P06169; -.
KO; K01568; -.
OMA; EWIGNCN; -.
OrthoDB; EOG092C29BL; -.
BioCyc; MetaCyc:MONOMER3O-117; -.
BioCyc; YEAST:MONOMER3O-117; -.
BRENDA; 4.1.1.1; 984.
SABIO-RK; P06169; -.
UniPathway; UPA00206; -.
UniPathway; UPA00866; -.
EvolutionaryTrace; P06169; -.
PRO; PR:P06169; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0005829; C:cytosol; IDA:SGD.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0047433; F:branched-chain-2-oxoacid decarboxylase activity; IMP:SGD.
GO; GO:0047434; F:indolepyruvate decarboxylase activity; IEA:UniProtKB-EC.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0050177; F:phenylpyruvate decarboxylase activity; IEA:UniProtKB-EC.
GO; GO:0004737; F:pyruvate decarboxylase activity; IDA:SGD.
GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
GO; GO:0000949; P:aromatic amino acid family catabolic process to alcohol via Ehrlich pathway; IGI:SGD.
GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:UniProtKB-KW.
GO; GO:0019655; P:glycolytic fermentation to ethanol; IDA:SGD.
GO; GO:0006559; P:L-phenylalanine catabolic process; IGI:SGD.
GO; GO:0006090; P:pyruvate metabolic process; IDA:SGD.
GO; GO:0006569; P:tryptophan catabolic process; IGI:SGD.
Gene3D; 3.40.50.1220; -; 1.
InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
InterPro; IPR029061; THDP-binding.
InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
InterPro; IPR000399; TPP-bd_CS.
InterPro; IPR012110; TPP_enzyme.
InterPro; IPR011766; TPP_enzyme-bd_C.
Pfam; PF02775; TPP_enzyme_C; 1.
Pfam; PF00205; TPP_enzyme_M; 1.
Pfam; PF02776; TPP_enzyme_N; 1.
PIRSF; PIRSF036565; Pyruvt_ip_decrb; 1.
SUPFAM; SSF52467; SSF52467; 1.
SUPFAM; SSF52518; SSF52518; 2.
PROSITE; PS00187; TPP_ENZYMES; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme;
Branched-chain amino acid catabolism; Complete proteome; Cytoplasm;
Decarboxylase; Direct protein sequencing; Isopeptide bond; Lyase;
Magnesium; Metal-binding; Nucleus; Phenylalanine catabolism;
Phosphoprotein; Reference proteome; Thiamine pyrophosphate;
Tryptophan catabolism; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:10545125,
ECO:0000269|PubMed:9298649}.
CHAIN 2 563 Pyruvate decarboxylase isozyme 1.
/FTId=PRO_0000090770.
REGION 390 476 Thiamine pyrophosphate binding.
METAL 444 444 Magnesium.
METAL 471 471 Magnesium.
METAL 473 473 Magnesium; via carbonyl oxygen.
BINDING 28 28 Substrate.
BINDING 115 115 Substrate.
BINDING 157 157 Substrate; allosteric site.
BINDING 477 477 Substrate.
MOD_RES 2 2 N-acetylserine.
{ECO:0000269|PubMed:10545125,
ECO:0000269|PubMed:9298649}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 266 266 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 336 336 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 353 353 Phosphothreonine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 522 522 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 526 526 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
CROSSLNK 212 212 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 233 233 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 269 269 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 332 332 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 484 484 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 505 505 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 520 520 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
MUTAGEN 291 291 D->N: In PDC1-8; reduces catalytic
activity to 10% but retains
autoregulatory activity.
{ECO:0000269|PubMed:7050079}.
CONFLICT 55 55 A -> R (in Ref. 1; CAA54522).
{ECO:0000305}.
CONFLICT 106 106 A -> S (in Ref. 1; CAA28380/CAA54522/
CAA54518/CAA54521). {ECO:0000305}.
CONFLICT 115 115 Missing (in Ref. 1; CAA28380).
{ECO:0000305}.
CONFLICT 143 143 A -> C (in Ref. 1; CAA54522/CAA54518/
CAA54521). {ECO:0000305}.
CONFLICT 145 146 AP -> PQ (in Ref. 1; CAA28380).
{ECO:0000305}.
CONFLICT 206 206 A -> V (in Ref. 1; CAA28380).
{ECO:0000305}.
CONFLICT 208 208 V -> A (in Ref. 1; CAA54522).
{ECO:0000305}.
CONFLICT 253 253 D -> S (in Ref. 1; CAA28380/CAA54522/
CAA54518/CAA54521). {ECO:0000305}.
CONFLICT 336 336 T -> N (in Ref. 1; CAA28380/CAA54522/
CAA54518/CAA54521). {ECO:0000305}.
CONFLICT 538 538 I -> V (in Ref. 1; CAA28380/CAA54522/
CAA54518/CAA54521). {ECO:0000305}.
CONFLICT 545 563 APQNLVEQAKLTAATNAKQ -> CSTKLG (in Ref. 1;
CAA28380). {ECO:0000305}.
STRAND 3 5 {ECO:0000244|PDB:2VK8}.
HELIX 6 16 {ECO:0000244|PDB:2VK8}.
STRAND 21 24 {ECO:0000244|PDB:2VK8}.
HELIX 28 30 {ECO:0000244|PDB:2VK8}.
HELIX 31 35 {ECO:0000244|PDB:2VK8}.
HELIX 36 39 {ECO:0000244|PDB:2VK8}.
HELIX 51 65 {ECO:0000244|PDB:2VK8}.
STRAND 68 73 {ECO:0000244|PDB:2VK8}.
HELIX 76 91 {ECO:0000244|PDB:2VK8}.
STRAND 95 101 {ECO:0000244|PDB:2VK8}.
HELIX 104 108 {ECO:0000244|PDB:2VK8}.
STRAND 109 111 {ECO:0000244|PDB:1QPB}.
STRAND 114 116 {ECO:0000244|PDB:1QPB}.
STRAND 118 120 {ECO:0000244|PDB:2VK8}.
HELIX 124 130 {ECO:0000244|PDB:2VK8}.
STRAND 134 138 {ECO:0000244|PDB:2VK8}.
TURN 142 144 {ECO:0000244|PDB:2VK8}.
HELIX 145 159 {ECO:0000244|PDB:2VK8}.
STRAND 163 168 {ECO:0000244|PDB:2VK8}.
HELIX 171 173 {ECO:0000244|PDB:2VK8}.
STRAND 174 177 {ECO:0000244|PDB:2VK8}.
HELIX 178 182 {ECO:0000244|PDB:2VK8}.
HELIX 194 210 {ECO:0000244|PDB:2VK8}.
STRAND 212 218 {ECO:0000244|PDB:2VK8}.
HELIX 220 224 {ECO:0000244|PDB:2VK8}.
HELIX 228 238 {ECO:0000244|PDB:2VK8}.
STRAND 242 244 {ECO:0000244|PDB:2VK8}.
TURN 246 250 {ECO:0000244|PDB:2VK8}.
STRAND 259 262 {ECO:0000244|PDB:2VK8}.
HELIX 265 267 {ECO:0000244|PDB:2VK8}.
HELIX 270 277 {ECO:0000244|PDB:2VK8}.
STRAND 280 286 {ECO:0000244|PDB:2VK8}.
TURN 291 297 {ECO:0000244|PDB:2VK8}.
STRAND 306 309 {ECO:0000244|PDB:2VK8}.
STRAND 311 316 {ECO:0000244|PDB:2VK8}.
STRAND 319 322 {ECO:0000244|PDB:2VK8}.
HELIX 326 340 {ECO:0000244|PDB:2VK8}.
TURN 341 343 {ECO:0000244|PDB:2VK8}.
HELIX 367 374 {ECO:0000244|PDB:2VK8}.
TURN 375 377 {ECO:0000244|PDB:2VK8}.
STRAND 383 386 {ECO:0000244|PDB:2VK8}.
HELIX 390 394 {ECO:0000244|PDB:2VK8}.
HELIX 395 397 {ECO:0000244|PDB:2VK8}.
STRAND 405 407 {ECO:0000244|PDB:2VK8}.
TURN 410 412 {ECO:0000244|PDB:2VK8}.
HELIX 417 432 {ECO:0000244|PDB:2VK8}.
STRAND 438 443 {ECO:0000244|PDB:2VK8}.
HELIX 444 450 {ECO:0000244|PDB:2VK8}.
HELIX 451 453 {ECO:0000244|PDB:2VK8}.
HELIX 454 459 {ECO:0000244|PDB:2VK8}.
STRAND 465 473 {ECO:0000244|PDB:2VK8}.
HELIX 475 480 {ECO:0000244|PDB:2VK8}.
HELIX 486 488 {ECO:0000244|PDB:2VK8}.
HELIX 495 497 {ECO:0000244|PDB:2VK8}.
HELIX 498 501 {ECO:0000244|PDB:2VK8}.
STRAND 505 512 {ECO:0000244|PDB:2VK8}.
HELIX 515 522 {ECO:0000244|PDB:2VK8}.
TURN 525 528 {ECO:0000244|PDB:2VK8}.
STRAND 531 539 {ECO:0000244|PDB:2VK8}.
HELIX 547 561 {ECO:0000244|PDB:2VK8}.
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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