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 04-NOV-2026, entry version 211. 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; DOI=10.1038/387s081; 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 non-oxidative 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=pyruvate + H(+) = 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=indole-3-pyruvate + H(+) = indole-3-acetaldehyde + CO2; 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(+) = propanal + CO2; 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 + pyruvate + H(+) = 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 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 83. DR DIP; DIP-3912N; -. DR FunCoup; P26263; 577. DR IntAct; P26263; 9. DR STRING; 4932.YGR087C; -. DR CarbonylDB; P26263; -. DR iPTMnet; P26263; -. DR PaxDb; 4932-YGR087C; -. DR PeptideAtlas; P26263; -. DR TopDownProteomics; P26263; -. DR EnsemblFungi; YGR087C_mRNA; YGR087C; YGR087C. DR GeneID; 852978; -. DR KEGG; sce:YGR087C; -. DR AGR; SGD:S000003319; -. DR SGD; S000003319; PDC6. DR VEuPathDB; FungiDB:YGR087C; -. DR eggNOG; KOG1184; Eukaryota. DR HOGENOM; CLU_013748_0_2_1; -. DR InParanoid; P26263; -. DR OMA; ACCVTAH; -. DR OrthoDB; 3970464at2759; -. DR BioCyc; MetaCyc:YGR087C-MONOMER; -. DR BioCyc; YEAST:YGR087C-MONOMER; -. DR BRENDA; 4.1.1.1; 984. DR SABIO-RK; P26263; -. DR UniPathway; UPA00206; -. DR UniPathway; UPA00866; -. DR BioGRID-ORCS; 852978; 1 hit in 10 CRISPR screens. 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:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0047433; F:branched-chain-2-oxoacid decarboxylase activity; EXP:UniProtKB. DR GO; GO:0047434; F:indolepyruvate decarboxylase activity; EXP:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0050177; F:phenylpyruvate decarboxylase activity; EXP:UniProtKB. DR GO; GO:0004737; F:pyruvate decarboxylase activity; IDA:SGD. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. 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:L-tryptophan catabolic process; IGI:SGD. DR CDD; cd02005; TPP_PDC_IPDC; 1. DR CDD; cd07038; TPP_PYR_PDC_IPDC_like; 1. DR FunFam; 3.40.50.1220:FF:000018; Pyruvate decarboxylase isozyme; 1. DR FunFam; 3.40.50.970:FF:000019; Pyruvate decarboxylase isozyme; 1. DR FunFam; 3.40.50.970:FF:000024; Pyruvate decarboxylase isozyme; 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 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 //