BDH2/YAL061W Summary Help

Standard Name BDH2 1
Systematic Name YAL061W
Feature Type ORF, Uncharacterized
Description Putative medium-chain alcohol dehydrogenase with similarity to BDH1; transcription induced by constitutively active PDR1 and PDR3 (1, 2, 3, 4 and see Summary Paragraph)
Chromosomal Location
ChrI:33448 to 34701 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All BDH2 GO evidence and references
  View Computational GO annotations for BDH2
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Regulators 151 genes
Resources
Classical genetics
null
Large-scale survey
null
unspecified
Resources
8 total interaction(s) for 7 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 2
  • Affinity Capture-RNA: 2

Genetic Interactions
  • Negative Genetic: 3
  • Synthetic Lethality: 1

Resources
Expression Summary
histogram
Resources
Length (a.a.) 417
Molecular Weight (Da) 46,098
Isoelectric Point (pI) 6.04
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrI:33448 to 34701 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates
Chromosomal
Coordinates
Most Recent Updates
Coordinates Sequence
CDS 1..1254 33448..34701 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000000057
SUMMARY PARAGRAPH for BDH2

About the medium-chain dehydrogenase/reductase (MDR) family

Medium-chain dehydrogenase/reductases (MDRs), sometimes referred to as long-chain dehydrogenases (5), constitute an ancient and widespread enzyme superfamily with members found in Bacteria, Archaea, and Eukaryota (6, 7). Many MDR members are basic metabolic enzymes acting on alcohols or aldehydes, and thus these enzymes may have roles in detoxifying alcohols and related compounds, protecting against environmental stresses such as osmotic shock, reduced or elevated temperatures, or oxidative stress (6). The family also includes the mammalian zeta-crystallin lens protein, which may protect the lens against oxidative damage and enzymes which produce lignocellulose in plants (6).

MDR enzymes typically have subunits of about 350 aa residues and are two-domain proteins, with a catalytic domain and a second domain for binding to the nicotinamide cofactor, either NAD(H) or NADP(H) (6, 7). They contain 0, 1, or 2 zinc atoms (8). When zinc is present, it is involved in catalysis at the active site.

Based on phylogenetic and sequence analysis, the members of the MDR superfamily can be further divided into more closely related subgroups (6, 7). In families which are widespread from prokaryotes to eukaryotes, some members appear conserved across all species, while others appear to be due to lineage specific duplications. Some subgroups are only found in certain taxa. S. cerevisiae contains fifteen (6) or twenty-one (7) members of the MDR superfamily, listed below. The difference in number is due to six sequences that were included as members of the quinone oxidoreductase family by Riveros-Rosas et al. (7) but not by Nordling et al. (6).

Zinc-containing enzyme groups:
- PDH; "polyol" dehydrogenase family - BDH1, BDH2, SOR1, SOR2, XYL2
- ADH; class III alcohol dehydrogenase family - SFA1
- Y-ADH; "yeast" alcohol dehydrogenase family - ADH1, ADH2, ADH3, ADH5
- CADH; cinnamyl alcohol dehydrogenase family - ADH6, ADH7

Non-zinc-containing enzyme groups:
- NRBP; nuclear receptor binding protein (7) or MRF; mitochondrial respiratory function (6) family - ETR1
- QOR; quinone oxidoreductase family - ZTA1 (6, 7), AST1, AST2, YCR102C, YLR460C, YMR152W, YNL134C (7)
- LTD; leukotriene B4 dehydrogenases - YML131W
- ER; enoyl reductases (7) or ACR; acyl-CoA reductase (6) family - no members in S. cerevisiae

Last updated: 2008-08-19 Contact SGD

References cited on this page View Complete Literature Guide for BDH2
1) Dickinson JR, et al.  (2003) The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae. J Biol Chem 278(10):8028-34
2) Gonzalez E, et al.  (2000) Characterization of a (2R,3R)-2,3-butanediol dehydrogenase as the Saccharomyces cerevisiae YAL060W gene product. Disruption and induction of the gene. J Biol Chem 275(46):35876-85
3) do Valle Matta MA, et al.  (2001) Novel target genes of the yeast regulator Pdr1p: a contribution of the TPO1 gene in resistance to quinidine and other drugs. Gene 272(1-2):111-9
4) Devaux F, et al.  (2002) Genome-wide studies on the nuclear PDR3-controlled response to mitochondrial dysfunction in yeast. FEBS Lett 515(1-3):25-8
5) Jornvall H, et al.  (1981) Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. Proc Natl Acad Sci U S A 78(7):4226-30
6) Nordling E, et al.  (2002) Medium-chain dehydrogenases/reductases (MDR). Family characterizations including genome comparisons and active site modeling. Eur J Biochem 269(17):4267-76
7) Riveros-Rosas H, et al.  (2003) Diversity, taxonomy and evolution of medium-chain dehydrogenase/reductase superfamily. Eur J Biochem 270(16):3309-34
8) Persson B, et al.  (1999) Bioinformatics in studies of SDR and MDR enzymes. Adv Exp Med Biol 463():373-7