BDH1/YAL060W Summary Help

BDH1 BASIC INFORMATION

Standard Name BDH1
Systematic Name YAL060W
Feature Type ORF, Verified
Description NAD-dependent (R,R)-butanediol dehydrogenase, catalyzes oxidation of (R,R)-2,3-butanediol to (3R)-acetoin, oxidation of meso-butanediol to (3S)-acetoin, and reduction of acetoin; enhances use of 2,3-butanediol as an aerobic carbon source (1 and see Summary Paragraph)
Also known as: BDH 1
Name Description Butanediol DeHydrogenase 1
Gene Product Alias (2R,3R)-2,3-butanediol dehydrogenase 1
GO Annotations All BDH1 GO evidence and references
    View Computational GO annotations for BDH1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Pathways
Mutant Phenotype All BDH1 Phenotype details and references
Classical genetics
null
Large-scale survey
null
overexpression
Interactions BDH1 All interactions details and references
  View additional details at BioGRID
29 total interaction(s) for 25 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 3
  • Affinity Capture-RNA: 1
  • Biochemical Activity: 1
  • Two-hybrid: 1
Genetic Interactions
  • Negative Genetic: 21
  • Positive Genetic: 1
  • Synthetic Lethality: 1
Sequence Information
ChrI:35156 to 36304 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 1998-09-13 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1149 35156..36304 1998-09-13 1996-07-31
Post-translational Modifications PhosphoGRID | PhosphoPep Database
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000000056

BDH1 RESOURCES

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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for BDH1

SUMMARY PARAGRAPH for BDH1

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

Medium-chain dehydrogenase/reductases (MDRs), sometimes referred to as long-chain dehydrogenases (2), constitute an ancient and widespread enzyme superfamily with members found in Bacteria, Archaea, and Eukaryota (3, 4). 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 (3). 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 (3).

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) (3, 4). They contain 0, 1, or 2 zinc atoms (5). 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 (3, 4). 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 (3) or twenty-one (4) 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. (4) but not by Nordling et al. (3).

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 (4) or MRF; mitochondrial respiratory function (3) family - ETR1
- QOR; quinone oxidoreductase family - ZTA1 (3, 4), AST1, AST2, YCR102C, YLR460C, YMR152W, YNL134C (4)
- LTD; leukotriene B4 dehydrogenases - YML131W
- ER; enoyl reductases (4) or ACR; acyl-CoA reductase (3) family - no members in S. cerevisiae

Last updated: 2008-08-19

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for BDH1]

1) 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
2) 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
3) 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
4) Riveros-Rosas H, et al.  (2003) Diversity, taxonomy and evolution of medium-chain dehydrogenase/reductase superfamily. Eur J Biochem 270(16):3309-34
5) Persson B, et al.  (1999) Bioinformatics in studies of SDR and MDR enzymes. Adv Exp Med Biol 463:373-7