NADP-dependent alcohol dehydrogenase 6 (Q04894)

Identification
NameNADP-dependent alcohol dehydrogenase 6
Synonyms
  • NADP-dependent alcohol dehydrogenase VI
  • ScADHVI
Gene NameADH6
Enzyme Class
Biological Properties
General FunctionInvolved in zinc ion binding
Specific FunctionNADP-dependent alcohol dehydrogenase with a broad substrate specificity
Cellular LocationNot Available
SMPDB Pathways
Pyruvate metabolismPW002447 ThumbThumb?image type=greyscaleThumb?image type=simple
Tryptophan metabolismPW002442 ThumbThumb?image type=greyscaleThumb?image type=simple
Tyrosine metabolismPW002441 ThumbThumb?image type=greyscaleThumb?image type=simple
Valine DegradationPW002489 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Tyrosine metabolismec00350 Map00350
SMPDB Reactions
Acetaldehyde + hydron + NADH ↔ Ethanol + NAD
isobutyraldehyde + NADH + hydron → isobutanol + NAD
3-methylbutanal + NADH + hydron ↔ NAD + isoamylol
2-Methylbutanal + NADH + hydron → 2-methylbutan-1-ol + NAD
KEGG Reactions
2-Methylbutanal + NADPH + hydron → NADP + 2-methylbutan-1-ol
Phenylacetaldehyde + NADPH + hydron → NADP + 2-phenylethanol
3-methylbutanal + NADPH + hydron → NADP + isoamylol
isobutyraldehyde + NADPH + hydron → NADP + isobutanol
Metabolites
YMDB IDNameView
YMDB00022AcetaldehydeShow
YMDB00110NADShow
YMDB00116PhenylacetaldehydeShow
YMDB00143NADHShow
YMDB00214L-ThreonineShow
YMDB00283GlycerolShow
YMDB00354IndoleacetaldehydeShow
YMDB00426NADPHShow
YMDB00427NADPShow
YMDB00482isobutyraldehydeShow
YMDB004852-MethylbutanalShow
YMDB004993-methylbutanalShow
YMDB005672-methylbutan-1-olShow
YMDB00570isoamylolShow
YMDB00573isobutanolShow
YMDB00577tryptopholShow
YMDB00695L-2-amino-3-oxobutanoic acidShow
YMDB00862hydronShow
YMDB00883EthanolShow
YMDB010722-phenylethanolShow
YMDB01798TyrosolShow
YMDB16128GlyceraldehydeShow
YMDB161644-HydroxyphenylacetaldehydeShow
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
LocusYMR318C
Gene Sequence>1083 bp ATGTCTTATCCTGAGAAATTTGAAGGTATCGCTATTCAATCACACGAAGATTGGAAAAAC CCAAAGAAGACAAAGTATGACCCAAAACCATTTTACGATCATGACATTGACATTAAGATC GAAGCATGTGGTGTCTGCGGTAGTGATATTCATTGTGCAGCTGGTCATTGGGGCAATATG AAGATGCCGCTAGTCGTTGGTCATGAAATCGTTGGTAAAGTTGTCAAGCTAGGGCCCAAG TCAAACAGTGGGTTGAAAGTCGGTCAACGTGTTGGTGTAGGTGCTCAAGTCTTTTCATGC TTGGAATGTGACCGTTGTAAGAATGATAATGAACCATACTGCACCAAGTTTGTTACCACA TACAGTCAGCCTTATGAAGACGGCTATGTGTCGCAGGGTGGCTATGCAAACTACGTCAGA GTTCATGAACATTTTGTGGTGCCTATCCCAGAGAATATTCCATCACATTTGGCTGCTCCA CTATTATGTGGTGGTTTGACTGTGTACTCTCCATTGGTTCGTAACGGTTGCGGTCCAGGT AAAAAAGTTGGTATAGTTGGTCTTGGTGGTATCGGCAGTATGGGTACATTGATTTCCAAA GCCATGGGGGCAGAGACGTATGTTATTTCTCGTTCTTCGAGAAAAAGAGAAGATGCAATG AAGATGGGCGCCGATCACTACATTGCTACATTAGAAGAAGGTGATTGGGGTGAAAAGTAC TTTGACACCTTCGACCTGATTGTAGTCTGTGCTTCCTCCCTTACCGACATTGACTTCAAC ATTATGCCAAAGGCTATGAAGGTTGGTGGTAGAATTGTCTCAATCTCTATACCAGAACAA CACGAAATGTTATCGCTAAAGCCATATGGCTTAAAGGCTGTCTCCATTTCTTACAGTGCT TTAGGTTCCATCAAAGAATTGAACCAACTCTTGAAATTAGTCTCTGAAAAAGATATCAAA ATTTGGGTGGAAACATTACCTGTTGGTGAAGCCGGCGTCCATGAAGCCTTCGAAAGGATG GAAAAGGGTGACGTTAGATATAGATTTACCTTAGTCGGCTACGACAAAGAATTTTCAGAC TAG
Protein Properties
Pfam Domain Function
Protein Residues360
Protein Molecular Weight39617.30078
Protein Theoretical pI6.73
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>NADP-dependent alcohol dehydrogenase 6 MSYPEKFEGIAIQSHEDWKNPKKTKYDPKPFYDHDIDIKIEACGVCGSDIHCAAGHWGNM KMPLVVGHEIVGKVVKLGPKSNSGLKVGQRVGVGAQVFSCLECDRCKNDNEPYCTKFVTT YSQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPG KKVGIVGLGGIGSMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEGDWGEKY FDTFDLIVVCASSLTDIDFNIMPKAMKVGGRIVSISIPEQHEMLSLKPYGLKAVSISYSA LGSIKELNQLLKLVSEKDIKIWVETLPVGEAGVHEAFERMEKGDVRYRFTLVGYDKEFSD
References
External Links
ResourceLink
Saccharomyces Genome Database ADH6
Uniprot IDQ04894
Uniprot NameADH6_YEAST
GenBank Gene IDZ54141
Genebank Protein ID984691
PDB ID
1Q1N
General Reference
  • 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
  • Valencia, E., Rosell, A., Larroy, C., Farres, J., Biosca, J. A., Fita, I., Pares, X., Ochoa, W. F. (2003). "Crystallization and preliminary X-ray analysis of NADP(H)-dependent alcohol dehydrogenases from Saccharomyces cerevisiae and Rana perezi." Acta Crystallogr D Biol Crystallogr 59:334-337.12554944
  • 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
  • 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