YLR460C Summary Help

YLR460C BASIC INFORMATION

Systematic Name YLR460C
Feature Type ORF, Uncharacterized
Description Member of the quinone oxidoreductase family, up-regulated in response to the fungicide mancozeb; possibly up-regulated by iodine (1, 2, 3 and see Summary Paragraph)
GO Annotations All YLR460C GO evidence and references
    View Computational GO annotations for YLR460C
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All YLR460C Phenotype details and references
Large-scale survey
null
Interactions YLR460C All interactions details and references
  View additional details at BioGRID
5 total interaction(s) for 5 unique genes/features.
Physical Interactions
  • Biochemical Activity: 2
Genetic Interactions
  • Negative Genetic: 3
Sequence Information
ChrXII:1060885 to 1059755 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 2006-01-09 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1131 1060885..1059755 2006-01-09 1996-07-31
Post-translational Modifications PhosphoGRID | PhosphoPep Database
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000004452

YLR460C RESOURCES

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SGD ORF mapGBrowse
SGD ORF map
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  • Localization Resources
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  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for YLR460C

SUMMARY PARAGRAPH for YLR460C

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

Medium-chain dehydrogenase/reductases (MDRs), sometimes referred to as long-chain dehydrogenases (4), constitute an ancient and widespread enzyme superfamily with members found in Bacteria, Archaea, and Eukaryota (5, 2). 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 (5). 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 (5).

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) (5, 2). They contain 0, 1, or 2 zinc atoms (6). 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 (5, 2). 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 (5) or twenty-one (2) 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. (2) but not by Nordling et al. (5).

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 (2) or MRF; mitochondrial respiratory function (5) family - ETR1
- QOR; quinone oxidoreductase family - ZTA1 (5, 2), AST1, AST2, YCR102C, YLR460C, YMR152W, YNL134C (2)
- LTD; leukotriene B4 dehydrogenases - YML131W
- ER; enoyl reductases (2) or ACR; acyl-CoA reductase (5) family - no members in S. cerevisiae

Last updated: 2008-08-19

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for YLR460C]

1) Kitagawa E, et al.  (2005) Effects of Iodine on Global Gene Expression in Saccharomyces cerevisiae. Biosci Biotechnol Biochem 69(12):2285-93
2) Riveros-Rosas H, et al.  (2003) Diversity, taxonomy and evolution of medium-chain dehydrogenase/reductase superfamily. Eur J Biochem 270(16):3309-34
3) Santos PM, et al.  (2009) Insights into yeast adaptive response to the agricultural fungicide mancozeb: a toxicoproteomics approach. Proteomics 9(3):657-70
4) 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
5) 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
6) Persson B, et al.  (1999) Bioinformatics in studies of SDR and MDR enzymes. Adv Exp Med Biol 463:373-7