Alcohol dehydrogenase 3, mitochondrial (P07246)

Identification
NameAlcohol dehydrogenase 3, mitochondrial
Synonyms
  • Alcohol dehydrogenase III
  • YADH-3
Gene NameADH3
Enzyme Class
Biological Properties
General FunctionInvolved in zinc ion binding
Specific FunctionAn alcohol + NAD(+) = an aldehyde or ketone + NADH
Cellular LocationMitochondrion matrix
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
NADH + Acetaldehyde + hydron → Ethanol + NAD
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
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 13
LocusYMR083W
Gene Sequence>1128 bp ATGTTGAGAACGTCAACATTGTTCACCAGGCGTGTCCAACCAAGCCTATTTTCTAGAAAC ATTCTTAGATTGCAATCCACAGCTGCAATCCCTAAGACTCAAAAAGGTGTCATCTTTTAT GAGAATAAGGGGAAGCTGCATTACAAAGATATCCCTGTCCCCGAGCCTAAGCCAAATGAA ATTTTAATCAACGTTAAATATTCTGGTGTATGTCACACCGATTTACATGCTTGGCACGGC GATTGGCCATTACCTGTTAAACTACCATTAGTAGGTGGTCATGAAGGTGCTGGTGTAGTT GTCAAACTAGGTTCCAATGTCAAGGGCTGGAAAGTCGGTGATTTAGCAGGTATCAAATGG CTGAACGGTTCTTGTATGACATGCGAATTCTGTGAATCAGGTCATGAATCAAATTGTCCA GATGCTGATTTATCTGGTTACACTCATGATGGTTCTTTCCAACAATTTGCGACCGCTGAT GCTATTCAAGCCGCCAAAATTCAACAGGGTACCGACTTGGCCGAAGTAGCCCCAATATTA TGTGCTGGTGTTACTGTATATAAAGCACTAAAAGAGGCAGACTTGAAAGCTGGTGACTGG GTTGCCATCTCTGGTGCTGCAGGTGGCTTGGGTTCCTTGGCCGTTCAATATGCAACTGCG ATGGGTTACAGAGTTCTAGGTATTGATGCAGGTGAGGAAAAGGAAAAACTTTTCAAGAAA TTGGGGGGTGAAGTATTCATCGACTTTACTAAAACAAAGAATATGGTTTCTGACATTCAA GAAGCTACCAAAGGTGGCCCTCATGGTGTCATTAACGTTTCCGTTTCTGAAGCCGCTATT TCTCTATCTACGGAATATGTTAGACCATGTGGTACCGTCGTTTTGGTTGGTTTGCCCGCT AACGCCTACGTTAAATCAGAGGTATTCTCTCATGTGGTGAAGTCCATCAATATCAAGGGT TCTTATGTTGGTAACAGAGCTGATACGAGAGAAGCCTTAGACTTCTTTAGCAGAGGTTTG ATCAAATCACCAATCAAAATTGTTGGATTATCTGAATTACCAAAGGTTTATGACTTGATG GAAAAGGGCAAGATTTTGGGTAGATACGTCGTCGATACTAGTAAATAA
Protein Properties
Pfam Domain Function
Protein Residues375
Protein Molecular Weight40369.19922
Protein Theoretical pI8.62
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Alcohol dehydrogenase 3, mitochondrial MLRTSTLFTRRVQPSLFSRNILRLQSTAAIPKTQKGVIFYENKGKLHYKDIPVPEPKPNE ILINVKYSGVCHTDLHAWHGDWPLPVKLPLVGGHEGAGVVVKLGSNVKGWKVGDLAGIKW LNGSCMTCEFCESGHESNCPDADLSGYTHDGSFQQFATADAIQAAKIQQGTDLAEVAPIL CAGVTVYKALKEADLKAGDWVAISGAAGGLGSLAVQYATAMGYRVLGIDAGEEKEKLFKK LGGEVFIDFTKTKNMVSDIQEATKGGPHGVINVSVSEAAISLSTEYVRPCGTVVLVGLPA NAYVKSEVFSHVVKSINIKGSYVGNRADTREALDFFSRGLIKSPIKIVGLSELPKVYDLM EKGKILGRYVVDTSK
References
External Links
ResourceLink
Saccharomyces Genome Database ADH3
Uniprot IDP07246
Uniprot NameADH3_YEAST
GenBank Gene IDAY692988
Genebank Protein ID51013427
General Reference
  • Young, E. T., Pilgrim, D. (1985). "Isolation and DNA sequence of ADH3, a nuclear gene encoding the mitochondrial isozyme of alcohol dehydrogenase in Saccharomyces cerevisiae." Mol Cell Biol 5:3024-3034.2943982
  • 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
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • 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
  • 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