Alcohol dehydrogenase 2 (P00331)

Identification
NameAlcohol dehydrogenase 2
Synonyms
  • Alcohol dehydrogenase II
  • YADH-2
Gene NameADH2
Enzyme Class
Biological Properties
General FunctionInvolved in zinc ion binding
Specific FunctionThis isozyme preferentially catalyzes the conversion of ethanol to acetaldehyde. Acts on a variety of primary unbranched aliphatic 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 + NAD ↔ NADH + Acetaldehyde + hydron
2-Methylbutanal + NADH + hydron → NAD + 2-methylbutan-1-ol
NADH + Phenylacetaldehyde + hydron → NAD + 2-phenylethanol
NADH + 3-methylbutanal + hydron → NAD + isoamylol
NADH + isobutyraldehyde + hydron → NAD + 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
binding
ion binding
cation binding
metal ion binding
transition metal ion binding
oxidoreductase activity
zinc ion binding
catalytic activity
Process
oxidation reduction
metabolic process
Gene Properties
Chromosome Locationchromosome 13
LocusYMR303C
Gene Sequence>1047 bp ATGTCTATTCCAGAAACTCAAAAAGCCATTATCTTCTACGAATCCAACGGCAAGTTGGAG CATAAGGATATCCCAGTTCCAAAGCCAAAGCCCAACGAATTGTTAATCAACGTCAAGTAC TCTGGTGTCTGCCACACCGATTTGCACGCTTGGCATGGTGACTGGCCATTGCCAACTAAG TTACCATTAGTTGGTGGTCACGAAGGTGCCGGTGTCGTTGTCGGCATGGGTGAAAACGTT AAGGGCTGGAAGATCGGTGACTACGCCGGTATCAAATGGTTGAACGGTTCTTGTATGGCC TGTGAATACTGTGAATTGGGTAACGAATCCAACTGTCCTCACGCTGACTTGTCAGGTTAC ACCCACGACGGTTCTTTCCAAGAATACGCTACCGCTGACGCTGTTCAAGCCGCTCACATT CCTCAAGGTACTGACTTGGCTGAAGTCGCGCCAATCTTGTGTGCTGGTATCACCGTATAC AAGGCTTTGAAGTCTGCCAACTTGAGAGCAGGCCACTGGGCGGCCATTTCTGGTGCTGCT GGTGGTCTAGGTTCTTTGGCTGTTCAATATGCTAAGGCGATGGGTTACAGAGTCTTAGGT ATTGATGGTGGTCCAGGAAAGGAAGAATTGTTTACCTCGCTCGGTGGTGAAGTATTCATC GACTTCACCAAAGAGAAGGACATTGTTAGCGCAGTCGTTAAGGCTACCAACGGCGGTGCC CACGGTATCATCAATGTTTCCGTTTCCGAAGCCGCTATCGAAGCTTCTACCAGATACTGT AGGGCGAACGGTACTGTTGTCTTGGTTGGTTTGCCAGCCGGTGCAAAGTGCTCCTCTGAT GTCTTCAACCACGTTGTCAAGTCTATCTCCATTGTCGGCTCTTACGTGGGGAACAGAGCT GATACCAGAGAAGCCTTAGATTTCTTTGCCAGAGGTCTAGTCAAGTCTCCAATAAAGGTA GTTGGCTTATCCAGTTTACCAGAAATTTACGAAAAGATGGAGAAGGGCCAAATTGCTGGT AGATACGTTGTTGACACTTCTAAATAA
Protein Properties
Pfam Domain Function
Protein Residues348
Protein Molecular Weight36731.60156
Protein Theoretical pI6.73
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Alcohol dehydrogenase 2 MSIPETQKAIIFYESNGKLEHKDIPVPKPKPNELLINVKYSGVCHTDLHAWHGDWPLPTK LPLVGGHEGAGVVVGMGENVKGWKIGDYAGIKWLNGSCMACEYCELGNESNCPHADLSGY THDGSFQEYATADAVQAAHIPQGTDLAEVAPILCAGITVYKALKSANLRAGHWAAISGAA GGLGSLAVQYAKAMGYRVLGIDGGPGKEELFTSLGGEVFIDFTKEKDIVSAVVKATNGGA HGIINVSVSEAAIEASTRYCRANGTVVLVGLPAGAKCSSDVFNHVVKSISIVGSYVGNRA DTREALDFFARGLVKSPIKVVGLSSLPEIYEKMEKGQIAGRYVVDTSK
References
External Links
ResourceLink
Saccharomyces Genome Database ADH2
Uniprot IDP00331
Uniprot NameADH2_YEAST
GenBank Gene IDJ01314
Genebank Protein ID171021
General Reference
  • Russell, D. W., Smith, M., Williamson, V. M., Young, E. T. (1983). "Nucleotide sequence of the yeast alcohol dehydrogenase II gene." J Biol Chem 258:2674-2682.6337160
  • 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
  • Bowman, S., Churcher, C., Badcock, K., Brown, D., Chillingworth, T., Connor, R., Dedman, K., Devlin, K., Gentles, S., Hamlin, N., Hunt, S., Jagels, K., Lye, G., Moule, S., Odell, C., Pearson, D., Rajandream, M., Rice, P., Skelton, J., Walsh, S., Whitehead, S., Barrell, B. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Nature 387:90-93.9169872
  • 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
  • Garrels, J. I., McLaughlin, C. S., Warner, J. R., Futcher, B., Latter, G. I., Kobayashi, R., Schwender, B., Volpe, T., Anderson, D. S., Mesquita-Fuentes, R., Payne, W. E. (1997). "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins." Electrophoresis 18:1347-1360.9298649
  • 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
  • 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
  • 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
  • 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