Q07471 (THI3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thiamine metabolism regulatory protein THI3
EC=4.1.1.-

Alternative name(s):
Keto isocaproate decarboxylase KID1

Gene names

Name:	THI3
Synonyms:	KID1
Ordered Locus Names:	YDL080C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	609 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-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 leucine and isoleucine, whereas valine, aromatic amino acids, and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins. The enzyme is also positively regulating the thiamine metabolism by a molecular mechanism that may involve thiamine concentration sensing and signal transmission. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
Catalytic activity	A 2-oxo acid = an aldehyde + CO2.
Cofactor	Binds 1 magnesium per subunit By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity.
Pathway	Amino-acid degradation; Ehrlich pathway.
Subcellular location	Nucleus Ref.10.
Biotechnological use	Fusel oils are important flavor and aroma compounds in yeast-fermented products contributing to the quality of beverages and food. In low concentration they are generally desirable, whereas high concentrations may spoil the product. By adjusting growth conditions and substrate their production is sought to be influenced.
Miscellaneous	Present with 2140 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the TPP enzyme family.

Ontologies

Keywords
Biological process	Branched-chain amino acid catabolism
Cellular component	Nucleus
Ligand	Magnesium Metal-binding Thiamine pyrophosphate
Molecular function	Decarboxylase Lyase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	branched-chain amino acid catabolic process to alcohol via Ehrlich pathway Inferred from genetic interaction Ref.8. Source: SGD leucine catabolic process Inferred from genetic interaction Ref.8. Source: SGD positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 16194233. Source: SGD regulation of thiamine biosynthetic process Inferred from mutant phenotype PubMed 16194233. Source: SGD
Cellular_component	cytosol Inferred from direct assay PubMed 16850348. Source: SGD nucleus Inferred from direct assay Ref.10PubMed 16194233PubMed 16850348. Source: SGD
Molecular_function	carboxy-lyase activity Inferred from mutant phenotype Ref.7. Source: SGD magnesium ion binding Inferred from electronic annotation. Source: InterPro thiamine pyrophosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 609	609	Thiamine metabolism regulatory protein THI3		PRO_0000090836
Amino acid modifications
	Modified residue	134	1	Phosphothreonine Ref.12

Sequences

	Sequence		Length	Mass (Da)
	Q07471 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 8EC37CC5B2BFA1AD	FASTA	609	68,366
	10 20 30 40 50 60 MNSSYTQRYA LPKCIAISDY LFHRLNQLNI HTIFGLSGEF SMPLLDKLYN IPNLRWAGNS 70 80 90 100 110 120 NELNAAYAAD GYSRLKGLGC LITTFGVGEL SAINGVAGSY AEHVGILHIV GMPPTSAQTK 130 140 150 160 170 180 QLLLHHTLGN GDFTVFHRIA SDVACYTTLI IDSELCADEV DKCIKKAWIE QRPVYMGMPV 190 200 210 220 230 240 NQVNLPIESA RLNTPLDLQL HKNDPDVEKE VISRILSFIY KSQNPAIIVD ACTSRQNLIE 250 260 270 280 290 300 ETKELCNRLK FPVFVTPMGK GTVNETDPQF GGVFTGSISA PEVREVVDFA DFIIVIGCML 310 320 330 340 350 360 SEFSTSTFHF QYKTKNCALL YSTSVKLKNA TYPDLSIKLL LQKILANLDE SKLSYQPSEQ 370 380 390 400 410 420 PSMMVPRPYP AGNVLLRQEW VWNEISHWFQ PGDIIITETG ASAFGVNQTR FPVNTLGISQ 430 440 450 460 470 480 ALWGSVGYTM GACLGAEFAV QEINKDKFPA TKHRVILFMG DGAFQLTVQE LSTIVKWGLT 490 500 510 520 530 540 PYIFVMNNQG YSVDRFLHHR SDASYYDIQP WNYLGLLRVF GCTNYETKKI ITVGEFRSMI 550 560 570 580 590 600 SDPNFATNDK IRMIEIMLPP RDVPQALLDR WVVEKEQSKQ VQEENENSSA VNTPTPEFQP LLKKNQVGY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Nishimura H., Nosaka K., Kaneko Y., Watanabe K., Iwashima A. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 42-609. Strain: S288c / GRF88.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P. Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"A positive regulatory gene, THI3, is required for thiamine metabolism in Saccharomyces cerevisiae." Nishimura H., Kawasaki Y., Kaneko Y., Nosaka K., Iwashima A. J. Bacteriol. 174:4701-4706(1992) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, REGULATION OF THIAMINE METABOLISM.
[5]	"A 13C nuclear magnetic resonance investigation of the metabolism of leucine to isoamyl alcohol in Saccharomyces cerevisiae." Dickinson J.R., Lanterman M.M., Danner D.J., Pearson B.M., Sanz P., Harrison S.J., Hewlins M.J. J. Biol. Chem. 272:26871-26878(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN LEUCINE CATABOLISM.
[6]	"An investigation of the metabolism of valine to isobutyl alcohol in Saccharomyces cerevisiae." Dickinson J.R., Harrison S.J., Hewlins M.J. J. Biol. Chem. 273:25751-25756(1998) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN VALINE CATABOLISM.
[7]	"An investigation of the metabolism of isoleucine to active Amyl alcohol in Saccharomyces cerevisiae." Dickinson J.R., Harrison S.J., Dickinson J.A., Hewlins M.J. J. Biol. Chem. 275:10937-10942(2000) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN ISOLEUCINE CATABOLISM.
[8]	"The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae." Dickinson J.R., Salgado L.E., Hewlins M.J. J. Biol. Chem. 278:8028-8034(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE IN PHENYLALANINE; TRYPTOPHAN AND LEUCINE CATABOLISM.
[9]	"Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae." Vuralhan Z., Morais M.A., Tai S.L., Piper M.D., Pronk J.T. Appl. Environ. Microbiol. 69:4534-4541(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, AROMATIC AMINO ACIDS AS NITROGEN SOURCE.
[10]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[11]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-134, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D21880 Genomic DNA. Translation: BAA04886.1. Z74128 Genomic DNA. Translation: CAA98646.1. BK006938 Genomic DNA. Translation: DAA11779.1.
PIR	S67616.
RefSeq	NP_010203.1. NM_001180139.1.
3D structure databases
ProteinModelPortal	Q07471.
SMR	Q07471. Positions 15-570.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6304N.
IntAct	Q07471. 13 interactions.
MINT	MINT-633975.
Proteomic databases
PaxDb	Q07471.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YDL080C; YDL080C; YDL080C.
GeneID	851479.
KEGG	sce:YDL080C.
Organism-specific databases
CYGD	YDL080c.
SGD	S000002238. THI3.
Phylogenomic databases
eggNOG	COG3961.
GeneTree	ENSGT00550000075465.
HOGENOM	HOG000061334.
KO	K01568.
OMA	NEISHWF.
OrthoDB	EOG4KM2BH.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-11833.
UniPathway	UPA00866.
Gene expression databases
Genevestigator	Q07471.
GermOnline	YDL080C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR012000. Thiamin_PyroP_enz_cen_dom. IPR012001. Thiamin_PyroP_enz_TPP-bd_dom. IPR012110. TPP_enzyme. IPR011766. TPP_enzyme-bd_C. [Graphical view]
PANTHER	PTHR18968:SF4. PTHR18968:SF4. 1 hit.
Pfam	PF02775. TPP_enzyme_C. 1 hit. PF00205. TPP_enzyme_M. 1 hit. PF02776. TPP_enzyme_N. 1 hit. [Graphical view]
PIRSF	PIRSF036565. Pyruvt_ip_decrb. 1 hit.
ProtoNet	Search...
Other
NextBio	968789.

Entry information

Entry name

THI3_YEAST

Accession

Primary (citable) accession number: Q07471
Secondary accession number(s): D6VRR9, P89098

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program