PDC6_YEAST
ID PDC6_YEAST Reviewed; 563 AA.
AC P26263; D6VUL9;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Pyruvate decarboxylase isozyme 3;
DE EC=4.1.1.- {ECO:0000269|PubMed:1744053, ECO:0000269|PubMed:23642236};
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=PDC6; OrderedLocusNames=YGR087C;
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], AND EXPRESSION LEVEL.
RX PubMed=1744053; DOI=10.1128/jb.173.24.7963-7969.1991;
RA Hohmann S.;
RT "Characterization of PDC6, a third structural gene for pyruvate
RT decarboxylase in Saccharomyces cerevisiae.";
RL J. Bacteriol. 173:7963-7969(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-159.
RA Hohmann S.;
RL Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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).
CC -!- FUNCTION: Minor 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 keto-acids) 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. The expression level of
CC this protein in the presence of fermentable carbon sources is so low
CC that it cannot compensate for the other two pyruvate decarboxylases to
CC sustain fermentation. {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: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:1744053};
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:0000250|UniProtKB:P06169};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000250|UniProtKB:P06169};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:P06169};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000250|UniProtKB:P06169};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.9 mM for pyruvate {ECO:0000269|PubMed:22904058};
CC KM=1.0 mM for 2-oxobutanoate {ECO:0000269|PubMed:22904058};
CC KM=1.6 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=31 umol/min/mg enzyme for 3-methyl-2-oxobutanoate
CC {ECO:0000269|PubMed:22904058};
CC Vmax=19 umol/min/mg enzyme for 4-methyl-2-oxopentanoate
CC {ECO:0000269|PubMed:22904058};
CC Vmax=10 umol/min/mg enzyme for 3-methyl-2-oxopentanoate
CC {ECO:0000269|PubMed:22904058};
CC Vmax=51 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:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- INDUCTION: Expression is very low in the presence of fermentable carbon
CC sources, but is induced, in contrast to PDC5, by ethanol.
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 1525 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; X55905; CAA39398.1; -; Genomic_DNA.
DR EMBL; Z72872; CAA97089.1; -; Genomic_DNA.
DR EMBL; Z72873; CAA97091.1; -; Genomic_DNA.
DR EMBL; X66843; CAA47319.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08180.1; -; Genomic_DNA.
DR PIR; S64382; S64382.
DR RefSeq; NP_011601.3; NM_001181216.3.
DR AlphaFoldDB; P26263; -.
DR SMR; P26263; -.
DR BioGRID; 33329; 77.
DR DIP; DIP-3912N; -.
DR IntAct; P26263; 7.
DR MINT; P26263; -.
DR STRING; 4932.YGR087C; -.
DR CarbonylDB; P26263; -.
DR iPTMnet; P26263; -.
DR MaxQB; P26263; -.
DR PaxDb; P26263; -.
DR PRIDE; P26263; -.
DR TopDownProteomics; P26263; -.
DR EnsemblFungi; YGR087C_mRNA; YGR087C; YGR087C.
DR GeneID; 852978; -.
DR KEGG; sce:YGR087C; -.
DR SGD; S000003319; PDC6.
DR VEuPathDB; FungiDB:YGR087C; -.
DR eggNOG; KOG1184; Eukaryota.
DR GeneTree; ENSGT00940000176336; -.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; P26263; -.
DR OMA; FHSDYVK; -.
DR BioCyc; MetaCyc:YGR087C-MON; -.
DR BioCyc; YEAST:YGR087C-MON; -.
DR BRENDA; 4.1.1.1; 984.
DR SABIO-RK; P26263; -.
DR UniPathway; UPA00206; -.
DR UniPathway; UPA00866; -.
DR PRO; PR:P26263; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P26263; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0047433; F:branched-chain-2-oxoacid decarboxylase activity; IEA:UniProtKB-EC.
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:0006067; P:ethanol metabolic process; IMP:SGD.
DR GO; GO:0006559; P:L-phenylalanine catabolic process; IGI: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 Acetylation; Branched-chain amino acid catabolism; Cytoplasm;
KW Decarboxylase; Isopeptide bond; Lyase; Magnesium; Metal-binding;
KW Phenylalanine catabolism; Phosphoprotein; Reference proteome;
KW Thiamine pyrophosphate; Tryptophan catabolism; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT CHAIN 2..563
FT /note="Pyruvate decarboxylase isozyme 3"
FT /id="PRO_0000090772"
FT BINDING 28
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 115
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 390
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 413..415
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 444
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 445..446
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 471..476
FT /ligand="thiamine diphosphate"
FT /ligand_id="ChEBI:CHEBI:58937"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 473
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 477
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT MOD_RES 266
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT MOD_RES 353
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT MOD_RES 522
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT CROSSLNK 212
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT CROSSLNK 233
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT CROSSLNK 269
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT CROSSLNK 505
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P06169"
SQ SEQUENCE 563 AA; 61580 MW; 83625F09371EBD0F CRC64;
MSEITLGKYL FERLKQVNVN TIFGLPGDFN LSLLDKIYEV DGLRWAGNAN ELNAAYAADG
YARIKGLSVL VTTFGVGELS ALNGIAGSYA EHVGVLHVVG VPSISAQAKQ LLLHHTLGNG
DFTVFHRMSA NISETTSMIT DIATAPSEID RLIRTTFITQ RPSYLGLPAN LVDLKVPGSL
LEKPIDLSLK PNDPEAEKEV IDTVLELIQN SKNPVILSDA CASRHNVKKE TQKLIDLTQF
PAFVTPLGKG SIDEQHPRYG GVYVGTLSKQ DVKQAVESAD LILSVGALLS DFNTGSFSYS
YKTKNVVEFH SDYVKVKNAT FLGVQMKFAL QNLLKVIPDV VKGYKSVPVP TKTPANKGVP
ASTPLKQEWL WNELSKFLQE GDVIISETGT SAFGINQTIF PKDAYGISQV LWGSIGFTTG
ATLGAAFAAE EIDPNKRVIL FIGDGSLQLT VQEISTMIRW GLKPYLFVLN NDGYTIEKLI
HGPHAEYNEI QTWDHLALLP AFGAKKYENH KIATTGEWDA LTTDSEFQKN SVIRLIELKL
PVFDAPESLI KQAQLTAATN AKQ
