YLR460C Summary Help

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)
Chromosomal Location
ChrXII:1060887 to 1059757 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Gene Ontology 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
Regulators 10 genes
Resources
Large-scale survey
null
Resources
8 total interaction(s) for 8 unique genes/features.
Physical Interactions
  • Affinity Capture-RNA: 1
  • Biochemical Activity: 2
  • Protein-peptide: 1

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

Resources
Expression Summary
histogram
Resources
Length (a.a.) 376
Molecular Weight (Da) 41,127
Isoelectric Point (pI) 7.21
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXII:1060887 to 1059757 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
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..1131 1060887..1059757 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 | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004452
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 Contact SGD

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