Canmetcon
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Identification
NameThiamine metabolism regulatory protein THI3
Synonyms
  • Keto isocaproate decarboxylase KID1
Gene NameTHI3
Enzyme Class
Biological Properties
General FunctionInvolved in magnesium ion binding
Specific FunctionOne 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
Cellular LocationNucleus
SMPDB Pathways
Leucine DegradationPW002490 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG PathwaysNot Available
SMPDB Reactions
Ketoleucine + hydron3-methylbutanal + Carbon dioxide
KEGG Reactions
hydron + (S)-3-methyl-2-oxovaleric acid2-Methylbutanal + Carbon dioxide
Ketoleucine + hydronCarbon dioxide + 3-methylbutanal
Metabolites
YMDB IDNameView
YMDB00168(S)-3-methyl-2-oxovaleric acidShow
YMDB00388KetoleucineShow
YMDB004852-MethylbutanalShow
YMDB004993-methylbutanalShow
YMDB00862hydronShow
YMDB00912Carbon dioxideShow
GO Classification
Component
Not Available
Function
vitamin binding
catalytic activity
magnesium ion binding
thiamin pyrophosphate binding
lyase activity
carbon-carbon lyase activity
carboxy-lyase activity
binding
ion binding
cation binding
metal ion binding
Process
Not Available
Gene Properties
Chromosome Locationchromosome 4
LocusYDL080C
Gene Sequence>1830 bp ATGAATTCTAGCTATACACAGAGATATGCACTGCCGAAGTGTATAGCAATATCAGATTAT CTTTTCCATCGGCTCAACCAGCTGAACATACATACCATATTTGGACTCTCCGGAGAATTT AGCATGCCGTTGCTGGATAAACTATACAACATTCCGAACTTACGATGGGCCGGTAATTCT AATGAGTTAAATGCTGCCTACGCAGCAGATGGATACTCACGACTAAAAGGCTTGGGATGT CTCATAACAACCTTTGGTGTAGGCGAATTATCGGCAATCAATGGCGTGGCCGGATCTTAC GCTGAACATGTAGGAATACTTCACATAGTGGGTATGCCGCCAACAAGTGCACAAACGAAA CAACTACTACTGCATCATACTCTGGGCAATGGTGATTTCACGGTATTTCATAGAATAGCC AGTGATGTAGCATGCTATACAACATTGATTATTGACTCTGAATTATGTGCCGACGAAGTC GATAAGTGCATCAAAAAGGCTTGGATAGAACAGAGGCCAGTATACATGGGCATGCCTGTC AACCAGGTAAATCTCCCGATTGAATCAGCAAGGCTTAATACACCTCTGGATTTACAATTG CATAAAAACGACCCAGACGTAGAGAAAGAAGTTATTTCTCGAATATTGAGTTTTATATAC AAAAGCCAGAATCCGGCAATCATCGTAGATGCATGTACTAGTCGACAGAATTTAATCGAG GAGACTAAAGAGCTTTGTAATAGGCTTAAATTTCCAGTTTTTGTTACACCTATGGGTAAG GGTACAGTAAACGAAACAGACCCGCAATTTGGGGGCGTATTCACGGGCTCGATATCAGCC CCAGAAGTAAGAGAAGTAGTTGATTTTGCCGATTTTATCATCGTCATTGGTTGCATGCTC TCCGAATTCAGCACGTCAACTTTCCACTTCCAATATAAAACTAAGAATTGTGCGCTACTA TATTCTACATCTGTGAAATTGAAAAATGCCACATATCCTGACTTGAGCATTAAATTACTA CTACAGAAAATATTAGCAAATCTTGATGAATCTAAACTGTCTTACCAACCAAGCGAACAA CCCAGTATGATGGTTCCAAGACCTTACCCAGCAGGAAATGTCCTCTTGAGACAAGAATGG GTCTGGAATGAAATATCCCATTGGTTCCAACCAGGTGACATAATCATAACAGAAACTGGT GCTTCTGCATTTGGAGTTAACCAGACCAGATTTCCGGTAAATACACTAGGTATTTCGCAA GCTCTTTGGGGATCTGTCGGATATACAATGGGGGCGTGTCTTGGGGCAGAATTTGCTGTT CAAGAGATAAACAAGGATAAATTCCCCGCAACTAAACATAGAGTTATTCTGTTTATGGGT GACGGTGCTTTCCAATTGACAGTTCAAGAATTATCCACAATTGTTAAGTGGGGATTGACA CCTTATATTTTTGTGATGAATAACCAAGGTTACTCTGTGGACAGGTTTTTGCATCACAGG TCAGATGCTAGTTATTACGATATCCAACCTTGGAACTACTTGGGATTATTGCGAGTATTT GGTTGCACGAACTACGAAACGAAAAAAATTATTACTGTTGGAGAATTCAGATCCATGATC AGTGACCCAAACTTTGCGACCAATGACAAAATTCGGATGATAGAGATTATGCTACCACCA AGGGATGTTCCACAGGCTCTGCTTGACAGGTGGGTGGTAGAAAAAGAACAGAGCAAACAA GTGCAAGAGGAGAACGAAAATTCTAGCGCAGTAAATACGCCAACTCCAGAATTCCAACCA CTTCTAAAAAAAAATCAAGTTGGATACTGA
Protein Properties
Pfam Domain Function
Protein Residues609
Protein Molecular Weight68365.79688
Protein Theoretical pI6.33
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Thiamine metabolism regulatory protein THI3 MNSSYTQRYALPKCIAISDYLFHRLNQLNIHTIFGLSGEFSMPLLDKLYNIPNLRWAGNS NELNAAYAADGYSRLKGLGCLITTFGVGELSAINGVAGSYAEHVGILHIVGMPPTSAQTK QLLLHHTLGNGDFTVFHRIASDVACYTTLIIDSELCADEVDKCIKKAWIEQRPVYMGMPV NQVNLPIESARLNTPLDLQLHKNDPDVEKEVISRILSFIYKSQNPAIIVDACTSRQNLIE ETKELCNRLKFPVFVTPMGKGTVNETDPQFGGVFTGSISAPEVREVVDFADFIIVIGCML SEFSTSTFHFQYKTKNCALLYSTSVKLKNATYPDLSIKLLLQKILANLDESKLSYQPSEQ PSMMVPRPYPAGNVLLRQEWVWNEISHWFQPGDIIITETGASAFGVNQTRFPVNTLGISQ ALWGSVGYTMGACLGAEFAVQEINKDKFPATKHRVILFMGDGAFQLTVQELSTIVKWGLT PYIFVMNNQGYSVDRFLHHRSDASYYDIQPWNYLGLLRVFGCTNYETKKIITVGEFRSMI SDPNFATNDKIRMIEIMLPPRDVPQALLDRWVVEKEQSKQVQEENENSSAVNTPTPEFQP LLKKNQVGY
References
External Links
ResourceLink
Saccharomyces Genome Database THI3
Uniprot IDQ07471
Uniprot NameTHI3_YEAST
GenBank Gene IDZ74128
Genebank Protein ID1431100
General Reference
  • Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, 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., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
  • Nishimura, H., Kawasaki, Y., Kaneko, Y., Nosaka, K., Iwashima, A. (1992). "A positive regulatory gene, THI3, is required for thiamine metabolism in Saccharomyces cerevisiae." J Bacteriol 174:4701-4706.1624458
  • Dickinson, J. R., Lanterman, M. M., Danner, D. J., Pearson, B. M., Sanz, P., Harrison, S. J., Hewlins, M. J. (1997). "A 13C nuclear magnetic resonance investigation of the metabolism of leucine to isoamyl alcohol in Saccharomyces cerevisiae." J Biol Chem 272:26871-26878.9341119
  • Dickinson, J. R., Harrison, S. J., Hewlins, M. J. (1998). "An investigation of the metabolism of valine to isobutyl alcohol in Saccharomyces cerevisiae." J Biol Chem 273:25751-25756.9748245
  • Dickinson, J. R., Harrison, S. J., Dickinson, J. A., Hewlins, M. J. (2000). "An investigation of the metabolism of isoleucine to active Amyl alcohol in Saccharomyces cerevisiae." J Biol Chem 275:10937-10942.10753893
  • Dickinson, J. R., Salgado, L. E., Hewlins, M. J. (2003). "The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae." J Biol Chem 278:8028-8034.12499363
  • Vuralhan, Z., Morais, M. A., Tai, S. L., Piper, M. D., Pronk, J. T. (2003). "Identification and characterization of phenylpyruvate decarboxylase genes in Saccharomyces cerevisiae." Appl Environ Microbiol 69:4534-4541.12902239
  • Huh, W. K., Falvo, J. V., Gerke, L. C., Carroll, A. S., Howson, R. W., Weissman, J. S., O'Shea, E. K. (2003). "Global analysis of protein localization in budding yeast." Nature 425:686-691.14562095
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956