THI3_YEAST
ID THI3_YEAST Reviewed; 609 AA.
AC Q07471; D6VRR9; P89098;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Thiamine metabolism regulatory protein THI3;
DE EC=4.1.1.72 {ECO:0000269|PubMed:10753893, ECO:0000269|PubMed:9341119};
DE AltName: Full=Keto isocaproate decarboxylase 1;
DE AltName: Full=Thiamine pyrophosphate-dependent 2-oxo-acid decarboxylase;
DE Short=2ODC;
GN Name=THI3; Synonyms=KID1; OrderedLocusNames=YDL080C;
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].
RC STRAIN=S288c / GRF88;
RA Nishimura H., Nosaka K., Kaneko Y., Watanabe K., Iwashima A.;
RT "Sequencing and expression of THI3 gene coding a positive regulatory factor
RT with thiamin pyrophosphate-binding motif for thiamin metabolism in
RT Saccharomyces cerevisiae.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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, AND REGULATION OF THIAMINE METABOLISM.
RX PubMed=1624458; DOI=10.1128/jb.174.14.4701-4706.1992;
RA Nishimura H., Kawasaki Y., Kaneko Y., Nosaka K., Iwashima A.;
RT "A positive regulatory gene, THI3, is required for thiamine metabolism in
RT Saccharomyces cerevisiae.";
RL J. Bacteriol. 174:4701-4706(1992).
RN [5]
RP ROLE IN LEUCINE 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 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 [7]
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 [8]
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 [9]
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 [10]
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 [11]
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 [12]
RP LACK OF DECARBOXYLATION ACTIVITY.
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).
CC -!- FUNCTION: One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6,
CC ARO10, and THI3) involved in amino acid catabolism. The enzyme
CC catalyzes the decarboxylation of amino acids, which, in a first step,
CC have been transaminated to the corresponding 2-oxo acids (alpha-keto-
CC acids). In a third step, the resulting aldehydes are reduced to
CC alcohols, collectively referred to as fusel oils or alcohols. Its
CC preferred substrates are the transaminated amino acids derived from
CC leucine (4-methyl-2-oxopentanoate, also alpha-keto-isocaproate) and
CC isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-
CC methylvalerate), whereas transaminated valine, transaminated aromatic
CC amino acids, and pyruvate are no substrates. In analogy to the pyruvate
CC decarboxylases the enzyme may in a side-reaction catalyze condensation
CC (or carboligation) reactions leading to the formation of 2-hydroxy
CC ketone, collectively called acyloins. The enzyme is also positively
CC regulating the thiamine metabolism by a molecular mechanism that may
CC involve thiamine concentration sensing and signal transmission.
CC {ECO:0000269|PubMed:10753893, ECO:0000269|PubMed:12499363,
CC ECO:0000269|PubMed:12902239, ECO:0000269|PubMed:1624458,
CC ECO:0000269|PubMed:9341119, ECO:0000269|PubMed:9748245}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-methyl-2-oxopentanoate + H(+) = 3-methylbutanal + CO2;
CC Xref=Rhea:RHEA:54360, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16638, ChEBI:CHEBI:17865; EC=4.1.1.72;
CC Evidence={ECO:0000269|PubMed:9341119};
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 1 Mg(2+) per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250};
CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC -!- PATHWAY: Amino-acid degradation; Ehrlich pathway.
CC -!- INTERACTION:
CC Q07471; P32896: PDC2; NbExp=3; IntAct=EBI-19209, EBI-13004;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- BIOTECHNOLOGY: Fusel oils are important flavor and aroma compounds in
CC yeast-fermented products contributing to the quality of beverages and
CC food. In low concentration they are generally desirable, whereas high
CC concentrations may spoil the product. By adjusting growth conditions
CC and substrate their production is sought to be influenced.
CC -!- MISCELLANEOUS: Present with 2140 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}.
CC -!- CAUTION: While genetic evidence suggests this enzyme is involved in
CC leucine and isoleucine catabolism (PubMed:9341119, PubMed:10753893), no
CC decarboxylase enzymatic activity could be detected in cell extracts of
CC S.cerevisiae strains expressing the individual gene (PubMed:22904058).
CC {ECO:0000305|PubMed:10753893, ECO:0000305|PubMed:22904058,
CC ECO:0000305|PubMed:9341119}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA04886.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D21880; BAA04886.1; ALT_INIT; Genomic_DNA.
DR EMBL; Z74128; CAA98646.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11779.1; -; Genomic_DNA.
DR PIR; S67616; S67616.
DR RefSeq; NP_010203.1; NM_001180139.1.
DR AlphaFoldDB; Q07471; -.
DR SMR; Q07471; -.
DR BioGRID; 31981; 111.
DR DIP; DIP-6304N; -.
DR IntAct; Q07471; 15.
DR MINT; Q07471; -.
DR STRING; 4932.YDL080C; -.
DR iPTMnet; Q07471; -.
DR MaxQB; Q07471; -.
DR PaxDb; Q07471; -.
DR PRIDE; Q07471; -.
DR EnsemblFungi; YDL080C_mRNA; YDL080C; YDL080C.
DR GeneID; 851479; -.
DR KEGG; sce:YDL080C; -.
DR SGD; S000002238; THI3.
DR VEuPathDB; FungiDB:YDL080C; -.
DR eggNOG; KOG1184; Eukaryota.
DR GeneTree; ENSGT00940000176336; -.
DR HOGENOM; CLU_013748_0_2_1; -.
DR InParanoid; Q07471; -.
DR OMA; LRQEWVW; -.
DR BioCyc; MetaCyc:MON3O-409; -.
DR BioCyc; YEAST:MON3O-409; -.
DR BRENDA; 4.1.1.72; 984.
DR UniPathway; UPA00866; -.
DR PRO; PR:Q07471; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q07471; protein.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:SGD.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0000955; P:amino acid catabolic process via Ehrlich pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0090180; P:positive regulation of thiamine biosynthetic process; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP: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; 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.
PE 1: Evidence at protein level;
KW Branched-chain amino acid catabolism; Decarboxylase; Lyase; Magnesium;
KW Metal-binding; Nucleus; Reference proteome; Thiamine pyrophosphate.
FT CHAIN 1..609
FT /note="Thiamine metabolism regulatory protein THI3"
FT /id="PRO_0000090836"
FT REGION 578..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 609 AA; 68366 MW; 8EC37CC5B2BFA1AD CRC64;
MNSSYTQRYA LPKCIAISDY LFHRLNQLNI HTIFGLSGEF SMPLLDKLYN IPNLRWAGNS
NELNAAYAAD GYSRLKGLGC LITTFGVGEL SAINGVAGSY AEHVGILHIV GMPPTSAQTK
QLLLHHTLGN GDFTVFHRIA SDVACYTTLI IDSELCADEV DKCIKKAWIE QRPVYMGMPV
NQVNLPIESA RLNTPLDLQL HKNDPDVEKE VISRILSFIY KSQNPAIIVD ACTSRQNLIE
ETKELCNRLK FPVFVTPMGK GTVNETDPQF GGVFTGSISA PEVREVVDFA DFIIVIGCML
SEFSTSTFHF QYKTKNCALL YSTSVKLKNA TYPDLSIKLL LQKILANLDE SKLSYQPSEQ
PSMMVPRPYP AGNVLLRQEW VWNEISHWFQ PGDIIITETG ASAFGVNQTR FPVNTLGISQ
ALWGSVGYTM GACLGAEFAV QEINKDKFPA TKHRVILFMG DGAFQLTVQE LSTIVKWGLT
PYIFVMNNQG YSVDRFLHHR SDASYYDIQP WNYLGLLRVF GCTNYETKKI ITVGEFRSMI
SDPNFATNDK IRMIEIMLPP RDVPQALLDR WVVEKEQSKQ VQEENENSSA VNTPTPEFQP
LLKKNQVGY
