ZTA1/YBR046C Summary Help

ZTA1 BASIC INFORMATION

Standard Name ZTA1
Systematic Name YBR046C
Feature Type ORF, Verified
Description NADPH-dependent quinone reductase, GFP-tagged protein localizes to the cytoplasm and nucleus; has similarity to E. coli quinone oxidoreductase and to human zeta-crystallin (1, 2, 3 and see Summary Paragraph)
Name Description ZeTA-crystallin
GO Annotations All ZTA1 GO evidence and references
    View Computational GO annotations for ZTA1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
High-throughput
Mutant Phenotype All ZTA1 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions ZTA1 All interactions details and references
2 total interaction(s) for 2 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 1
  • Two-hybrid: 1
Sequence Information
ChrII:331509 to 330505 | ORF Map | GBrowse
Note: this feature is encoded on the Crick strand.
Gbrowse
Last Update Coordinates: 2004-07-16 | Sequence: 1997-01-28
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1005 331509..330505 2004-07-16 1997-01-28
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000000250

ZTA1 RESOURCES

Click on map for expanded view
SGD ORF mapGBrowse
SGD ORF map
 GBrowse
  • Literature
  • Retrieve Sequences
  • Sequence Analysis Tools
  • Protein Info & Structure
  • Localization Resources
  • Interactions
  • Phenotype Resources
  • Maps & Displays
  • Comparison Resources
  • Functional Analysis

Click on histogram for expression summary
Expression Summary histogram

ADDITIONAL INFORMATION for ZTA1

SUMMARY PARAGRAPH for ZTA1

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, 6). 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, 6). They contain 0, 1, or 2 zinc atoms (7). 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, 6). 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 (6) 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. (6) 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 (6) or MRF; mitochondrial respiratory function (5) family - ETR1
- QOR; quinone oxidoreductase family - ZTA1 (5, 6), AST1, AST2, YCR102C, YLR460C, YMR152W, YNL134C (6)
- LTD; leukotriene B4 dehydrogenases - YML131W
- ER; enoyl reductases (6) 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 ZTA1]

1) Huh WK, et al.  (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91
2) Fernandez MR, et al.  (2007) Human and yeast zeta-crystallins bind AU-rich elements in RNA. Cell Mol Life Sci 64(11):1419-27
3) Porte S, et al.  (2009) MDR quinone oxidoreductases: the human and yeast zeta-crystallins. Chem Biol Interact 178(1-3):288-94
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) Riveros-Rosas H, et al.  (2003) Diversity, taxonomy and evolution of medium-chain dehydrogenase/reductase superfamily. Eur J Biochem 270(16):3309-34
7) Persson B, et al.  (1999) Bioinformatics in studies of SDR and MDR enzymes. Adv Exp Med Biol 463:373-7