PDC5_YEAST
ID PDC5_YEAST Reviewed; 563 AA.
AC P16467; D6VYC9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Pyruvate decarboxylase isozyme 2;
DE EC=4.1.1.- {ECO:0000269|PubMed:2185016, 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=PDC5; OrderedLocusNames=YLR134W; ORFNames=L3133, L9606.7;
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=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 [2]
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 [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 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 [5]
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 [6]
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 [7]
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 [8]
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 [9]
RP FUNCTION, AND CONTROL OF PDC5 EXPRESSION BY PDC1.
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 [10]
RP FUNCTION, AND CONTROL OF PDC5 EXPRESSION BY THIAMINE.
RX PubMed=10338141; DOI=10.1016/s0014-5793(99)00449-4;
RA Muller E.H., Richards E.J., Norbeck J., Byrne K.L., Karlsson K.A.,
RA Pretorius G.H., Meacock P.A., Blomberg A., Hohmann S.;
RT "Thiamine repression and pyruvate decarboxylase autoregulation
RT independently control the expression of the Saccharomyces cerevisiae PDC5
RT gene.";
RL FEBS Lett. 449:245-250(1999).
RN [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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: Second most abundant of three pyruvate decarboxylases (PDC1,
CC PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to
CC acetaldehyde and carbon dioxide during alcoholic fermentation. Most of
CC the produced acetaldehyde is subsequently reduced to ethanol, but some
CC is required for cytosolic acetyl-CoA production for biosynthetic
CC pathways. The enzyme is also one of five 2-oxo acid decarboxylases
CC (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex
CC 2-oxo acids (alpha-keto-acids) than pyruvate, which seem mainly
CC involved in amino acid catabolism. Here the enzyme catalyzes the
CC decarboxylation of amino acids, which, in a first step, have been
CC transaminated to the corresponding 2-oxo acids. In a third step, the
CC resulting aldehydes are reduced to alcohols, collectively referred to
CC as fusel oils or alcohols. Its preferred substrates are the
CC transaminated amino acids derived from threonine (2-oxobutanoate),
CC norvaline (2-oxopentanoate), valine (3-methyl-2-oxobutanoate, also
CC alpha-keto-isovalerate), isoleucine ((3S)-3-methyl-2-oxopentanoate,
CC also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate),
CC and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine
CC is no substrate. In a side-reaction the carbanionic intermediate (or
CC active aldehyde) generated by decarboxylation or by activation of an
CC aldehyde can react with an aldehyde via condensation (or carboligation)
CC yielding a 2-hydroxy ketone, collectively called acyloins.
CC {ECO:0000269|PubMed:10231381, ECO:0000269|PubMed:10234824,
CC ECO:0000269|PubMed:10338141, ECO:0000269|PubMed:10753893,
CC ECO:0000269|PubMed:11141278, ECO:0000269|PubMed:12499363,
CC ECO:0000269|PubMed:12902239, ECO:0000269|PubMed:22904058,
CC ECO:0000269|PubMed:9341119, 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:2185016};
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 -!- ACTIVITY REGULATION: Allosterically activated by its substrate,
CC pyruvate. {ECO:0000250|UniProtKB:P06169}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.1 mM for pyruvate {ECO:0000269|PubMed:22904058};
CC KM=1.2 mM for 2-oxobutanoate {ECO:0000269|PubMed:22904058};
CC KM=1.5 mM for 2-oxopentanoate {ECO:0000269|PubMed:22904058};
CC KM=0.67 mM for phenylpyruvate {ECO:0000269|PubMed:22904058};
CC Vmax=1.3 umol/min/mg enzyme for pyruvate
CC {ECO:0000269|PubMed:22904058};
CC Vmax=0.4 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=68 umol/min/mg enzyme for phenylpyruvate
CC {ECO:0000269|PubMed:22904058};
CC Vmax=46 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=8 umol/min/mg enzyme for 3-methyl-2-oxopentanoate
CC {ECO:0000269|PubMed:22904058};
CC Vmax=54 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.
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, under anaerobic growth
CC conditions, and by thiamine limitation, but is repressed by the
CC presence of PDC1 (independent of its catalytic activity) and thiamine.
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 471316 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
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DR EMBL; X15668; CAA33709.1; -; Genomic_DNA.
DR EMBL; X91258; CAA62647.1; -; Genomic_DNA.
DR EMBL; Z73306; CAA97705.1; -; Genomic_DNA.
DR EMBL; U53881; AAB82395.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09445.1; -; Genomic_DNA.
DR PIR; S59324; S59324.
DR RefSeq; NP_013235.1; NM_001182021.1.
DR AlphaFoldDB; P16467; -.
DR SMR; P16467; -.
DR BioGRID; 31403; 56.
DR DIP; DIP-4603N; -.
DR IntAct; P16467; 12.
DR MINT; P16467; -.
DR STRING; 4932.YLR134W; -.
DR CarbonylDB; P16467; -.
DR iPTMnet; P16467; -.
DR MaxQB; P16467; -.
DR PaxDb; P16467; -.
DR PRIDE; P16467; -.
DR TopDownProteomics; P16467; -.
DR EnsemblFungi; YLR134W_mRNA; YLR134W; YLR134W.
DR GeneID; 850825; -.
DR KEGG; sce:YLR134W; -.
DR SGD; S000004124; PDC5.
DR VEuPathDB; FungiDB:YLR134W; -.
DR eggNOG; KOG1184; Eukaryota.
DR GeneTree; ENSGT00940000176336; -.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; P16467; -.
DR OMA; MIRCGQN; -.
DR BioCyc; MetaCyc:YLR134W-MON; -.
DR BioCyc; YEAST:YLR134W-MON; -.
DR BRENDA; 4.1.1.1; 984.
DR SABIO-RK; P16467; -.
DR UniPathway; UPA00206; -.
DR UniPathway; UPA00866; -.
DR PRO; PR:P16467; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P16467; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; 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: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 Allosteric enzyme; Branched-chain amino acid catabolism; Cytoplasm;
KW Decarboxylase; Lyase; Magnesium; Metal-binding; Nucleus;
KW Phenylalanine catabolism; Reference proteome; Thiamine pyrophosphate;
KW Tryptophan catabolism.
FT CHAIN 1..563
FT /note="Pyruvate decarboxylase isozyme 2"
FT /id="PRO_0000090771"
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:0000250|UniProtKB:P06169"
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:0000250|UniProtKB:P06169"
FT BINDING 157
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT BINDING 224
FT /ligand="pyruvate"
FT /ligand_id="ChEBI:CHEBI:15361"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
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_label="1"
FT /ligand_note="substrate; ligand shared between two
FT neighboring subunits"
FT /evidence="ECO:0000250|UniProtKB:P06169"
FT CONFLICT 35
FT /note="D -> N (in Ref. 1; CAA33709)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="A -> R (in Ref. 1; CAA33709)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="L -> F (in Ref. 1; CAA33709)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="A -> C (in Ref. 1; CAA33709)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="V -> A (in Ref. 1; CAA33709)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="H -> Q (in Ref. 1; CAA33709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 563 AA; 61912 MW; DCA06A73E18DD819 CRC64;
MSEITLGKYL FERLSQVNCN TVFGLPGDFN LSLLDKLYEV KGMRWAGNAN ELNAAYAADG
YARIKGMSCI ITTFGVGELS ALNGIAGSYA EHVGVLHVVG VPSISSQAKQ LLLHHTLGNG
DFTVFHRMSA NISETTAMIT DIANAPAEID RCIRTTYTTQ RPVYLGLPAN LVDLNVPAKL
LETPIDLSLK PNDAEAEAEV VRTVVELIKD AKNPVILADA CASRHDVKAE TKKLMDLTQF
PVYVTPMGKG AIDEQHPRYG GVYVGTLSRP EVKKAVESAD LILSIGALLS DFNTGSFSYS
YKTKNIVEFH SDHIKIRNAT FPGVQMKFAL QKLLDAIPEV VKDYKPVAVP ARVPITKSTP
ANTPMKQEWM WNHLGNFLRE GDIVIAETGT SAFGINQTTF PTDVYAIVQV LWGSIGFTVG
ALLGATMAAE ELDPKKRVIL FIGDGSLQLT VQEISTMIRW GLKPYIFVLN NNGYTIEKLI
HGPHAEYNEI QGWDHLALLP TFGARNYETH RVATTGEWEK LTQDKDFQDN SKIRMIEVML
PVFDAPQNLV KQAQLTAATN AKQ
