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Identification
NameAlcohol dehydrogenase 1
Synonyms
  • Alcohol dehydrogenase I
  • YADH-1
Gene NameADH1
Enzyme Class
Biological Properties
General FunctionInvolved in zinc ion binding
Specific FunctionThis isozyme preferentially catalyzes the conversion of primary unbranched alcohols to their corresponding aldehydes. Also also shows activity toward secondary alcohols
Cellular LocationCytoplasm
SMPDB Pathways
Fatty acid metabolismPW002460 ThumbThumb?image type=greyscaleThumb?image type=simple
Tyrosine metabolismPW002441 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Fatty acid metabolismec00071 Map00071
Glycine, serine and threonine metabolismec00260 Map00260
Glycolysis / Gluconeogenesisec00010 Map00010
Tyrosine metabolismec00350 Map00350
SMPDB ReactionsNot Available
KEGG Reactions
Ethanol + NADNADH + Acetaldehyde + hydron
2-Methylbutanal + NADH + hydronNAD + 2-methylbutan-1-ol
NADH + Phenylacetaldehyde + hydronNAD + 2-phenylethanol
NADH + 3-methylbutanal + hydronNAD + isoamylol
NADH + isobutyraldehyde + hydronNAD + isobutanol
Metabolites
YMDB IDNameView
YMDB00022AcetaldehydeShow
YMDB00110NADShow
YMDB00116PhenylacetaldehydeShow
YMDB00143NADHShow
YMDB00354IndoleacetaldehydeShow
YMDB00412NAD(+)Show
YMDB00482isobutyraldehydeShow
YMDB004852-MethylbutanalShow
YMDB004993-methylbutanalShow
YMDB005672-methylbutan-1-olShow
YMDB00570isoamylolShow
YMDB00573isobutanolShow
YMDB00577tryptopholShow
YMDB00862hydronShow
YMDB00883EthanolShow
GO Classification
Component
Not Available
Function
metal ion binding
transition metal ion binding
oxidoreductase activity
zinc ion binding
catalytic activity
binding
ion binding
cation binding
Process
oxidation reduction
metabolic process
Gene Properties
Chromosome Locationchromosome 15
LocusYOL086C
Gene Sequence>1047 bp ATGTCTATCCCAGAAACTCAAAAAGGTGTTATCTTCTACGAATCCCACGGTAAATTGGAA CACAAGGATATTCCAGTTCCAAAGCCAAAGGCCAACGAATTGTTGATCAACGTTAAGTAC TCTGGTGTCTGTCACACCGACTTGCACGCTTGGCACGGTGACTGGCCATTGCCAGTTAAG CTACCATTAGTCGGTGGTCACGAAGGTGCCGGTGTCGTTGTCGGCATGGGTGAAAACGTT AAGGGCTGGAAGATCGGTGACTACGCCGGTATCAAATGGTTGAACGGTTCTTGTATGGCC TGTGAATACTGTGAATTGGGTAACGAATCCAACTGTCCTCACGCTGACTTGTCTGGTTAC ACCCACGACGGTTCTTTCCAACAATACGCTACCGCTGACGCTGTTCAAGCCGCTCACATT CCTCAAGGTACCGACTTGGCCCAAGTCGCCCCCATCTTGTGTGCTGGTATCACCGTCTAC AAGGCTTTGAAGTCTGCTAACTTGATGGCCGGTCATTGGGTTGCCATTTCCGGTGCTGCC GGTGGTCTAGGTTCTTTGGCTGTTCAATACGCCAAGGCTATGGGTTACAGAGTCTTGGGT ATTGACGGTGGTGAAGGTAAGGAAGAATTATTCAGATCCATCGGTGGTGAAGTCTTCATT GACTTCACTAAGGAAAAGGACATTGTCGGTGCTGTTCTAAAGGCCACTGACGGTGGTGCT CACGGTGTCATCAACGTTTCCGTTTCCGAAGCCGCTATTGAAGCTTCTACCAGATACGTT AGAGCTAACGGTACCACCGTTTTGGTCGGTATGCCAGCTGGTGCCAAGTGTTGTTCTGAT GTCTTCAACCAAGTCGTCAAGTCCATCTCTATTGTTGGTTCTTACGTCGGTAACAGAGCC GACACCAGAGAAGCTTTGGACTTCTTCGCCAGAGGTTTGGTCAAGTCTCCAATCAAGGTT GTCGGCTTGTCTACCTTGCCAGAAATTTACGAAAAGATGGAAAAGGGTCAAATCGTTGGT AGATACGTTGTTGACACTTCTAAATAA
Protein Properties
Pfam Domain Function
Protein Residues348
Protein Molecular Weight36849.0
Protein Theoretical pI6.67
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Alcohol dehydrogenase 1 MSIPETQKGVIFYESHGKLEYKDIPVPKPKANELLINVKYSGVCHTDLHAWHGDWPLPVK LPLVGGHEGAGVVVGMGENVKGWKIGDYAGIKWLNGSCMACEYCELGNESNCPHADLSGY THDGSFQQYATADAVQAAHIPQGTDLAQVAPILCAGITVYKALKSANLMAGHWVAISGAA GGLGSLAVQYAKAMGYRVLGIDGGEGKEELFRSIGGEVFIDFTKEKDIVGAVLKATDGGA HGVINVSVSEAAIEASTRYVRANGTTVLVGMPAGAKCCSDVFNQVVKSISIVGSYVGNRA DTREALDFFARGLVKSPIKVVGLSTLPEIYEKMEKGQIVGRYVVDTSK
References
External Links
ResourceLink
Saccharomyces Genome Database ADH1
Uniprot IDP00330
Uniprot NameADH1_YEAST
GenBank Gene IDM38456
Genebank Protein ID171025
General Reference
  • Bennetzen, J. L., Hall, B. D. (1982). "The primary structure of the Saccharomyces cerevisiae gene for alcohol dehydrogenase." J Biol Chem 257:3018-3025.6277922
  • Young, T., Williamson, V., Taguchi, A., Smith, M., Sledziewski, A., Russell, D., Osterman, J., Denis, C., Cox, D., Beier, D. (1982). "The alcohol dehydrogenase genes of the yeast, Saccharomyces cerevisiae: isolation, structure, and regulation." Basic Life Sci 19:335-361.6279086
  • Zumstein, E., Pearson, B. M., Kalogeropoulos, A., Schweizer, M. (1995). "A 29.425 kb segment on the left arm of yeast chromosome XV contains more than twice as many unknown as known open reading frames." Yeast 11:975-986.8533473
  • Dujon, B., Albermann, K., Aldea, M., Alexandraki, D., Ansorge, W., Arino, J., Benes, V., Bohn, C., Bolotin-Fukuhara, M., Bordonne, R., Boyer, J., Camasses, A., Casamayor, A., Casas, C., Cheret, G., Cziepluch, C., Daignan-Fornier, B., Dang, D. V., de Haan, M., Delius, H., Durand, P., Fairhead, C., Feldmann, H., Gaillon, L., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Nature 387:98-102.9169874
  • Jornvall, H. (1977). "The primary structure of yeast alcohol dehydrogenase." Eur J Biochem 72:425-442.320000
  • Williamson, V. M., Bennetzen, J., Young, E. T., Nasmyth, K., Hall, B. D. (1980). "Isolation of the structural gene for alcohol dehydrogenase by genetic complementation in yeast." Nature 283:214-216.6985717
  • Garrels, J. I., Futcher, B., Kobayashi, R., Latter, G. I., Schwender, B., Volpe, T., Warner, J. R., McLaughlin, C. S. (1994). "Protein identifications for a Saccharomyces cerevisiae protein database." Electrophoresis 15:1466-1486.7895733
  • Norbeck, J., Blomberg, A. (1995). "Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides." Electrophoresis 16:149-156.7737086
  • Leskovac, V., Trivic, S., Pericin, D. (2002). "The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae." FEMS Yeast Res 2:481-494.12702265
  • Gruhler, A., Olsen, J. V., Mohammed, S., Mortensen, P., Faergeman, N. J., Mann, M., Jensen, O. N. (2005). "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Mol Cell Proteomics 4:310-327.15665377
  • Li, X., Gerber, S. A., Rudner, A. D., Beausoleil, S. A., Haas, W., Villen, J., Elias, J. E., Gygi, S. P. (2007). "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." J Proteome Res 6:1190-1197.17330950
  • Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., Hunt, D. F. (2007). "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Proc Natl Acad Sci U S A 104:2193-2198.17287358
  • Smolka, M. B., Albuquerque, C. P., Chen, S. H., Zhou, H. (2007). "Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Proc Natl Acad Sci U S A 104:10364-10369.17563356
  • 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