P48239 · GTO1_YEAST

Function

function

Active as '1-Cys' thiol transferase against beta-hydroxyethyl disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic acid reductase, while not active against the standard GST substrate 1-chloro-2,4-dinitrobenzene (CDNB).

Catalytic activity

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
1.13 mMreduced glutathione (GSH)

Features

Showing features for active site.

TypeIDPosition(s)Description
Active site31Nucleophile

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentperoxisome
Molecular Functionglutathione dehydrogenase (ascorbate) activity
Molecular Functionglutathione transferase activity
Biological Processglutathione metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Glutathione S-transferase omega-like 1
  • EC number
  • Alternative names
    • Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.1) . EC:1.8.5.1 (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      GTO1
    • ORF names
      G6664
    • Ordered locus names
      YGR154C

Organism names

Accessions

  • Primary accession
    P48239
  • Secondary accessions
    • D6VUT4

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Disruption phenotype

Null mutants display increased sensitivity to cadmium in the absence of GTT1 and GTT2. Null mutants also show growth defects on oleic acid-based medium, indicative of abnormal peroxisomal functions and altered expression of genes related to sulfur amino acid metabolism, and have low levels of reduced glutathione.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002028331-356Glutathione S-transferase omega-like 1

Proteomic databases

Expression

Induction

By diamide and 1-chloro-2,4-dinitrobenzene (CDNB) in a transcriptional factors YAP1 and/or MSN2/4-dependent manner.

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for coiled coil.

TypeIDPosition(s)Description
Coiled coil214-257

Sequence similarities

Belongs to the GST superfamily. Omega family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    356
  • Mass (Da)
    41,301
  • Last updated
    1996-02-01 v1
  • Checksum
    B4639BD195CDF7F5
MSVSYKGTISKTHSVFKPEKGRYYIYGALGCPFTHRAILARSLKKLEPVLGLVLSHWQLDSKGARFLPAPHRPEKYKERFFTATGGIASAKLDESEELGDVNNDSARLFVDGAFDPVENISRLSELYYLNDPKYPGTKFTVPVLWDSKTRKIVNNESGDIIRILNSGVFDEFIQSEETNVIDLVPHDLIDEIDKNIKWVHPKINLGVYKVGLAENGKIYETEVKTLFENLQKMECVLKENYKRLEEQFSGNKQKILAKYFVLGQRLTEADIRLYPSIIRFDVVYVQHFKCNLKTIRDGFPYLHLWLINLYWNYAEFRFTTDFNHIKLFYIRMEVSRNKINQFGIVPLGPKPDISRL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X85807
EMBL· GenBank· DDBJ
CAA59811.1
EMBL· GenBank· DDBJ
Genomic DNA
Z72939
EMBL· GenBank· DDBJ
CAA97168.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006941
EMBL· GenBank· DDBJ
DAA08245.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp