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Protein

Glutathione transferase omega-1

Gene

gsto-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Exhibits glutathione-dependent thiol transferase activity. Has dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) (By similarity). Protects against environmental stress and oxidative stress.By similarity1 Publication

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication
2 glutathione + dehydroascorbate = glutathione disulfide + ascorbate.1 Publication
Methylarsonate + 2 glutathione = methylarsonite + glutathione disulfide + H2O.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei33 – 331NucleophileBy similarity
Binding sitei60 – 601GlutathioneBy similarity

GO - Molecular functioni

  • glutathione dehydrogenase (ascorbate) activity Source: UniProtKB
  • glutathione transferase activity Source: UniProtKB
  • methylarsonate reductase activity Source: UniProtKB-EC

GO - Biological processi

  • cellular response to extracellular stimulus Source: UniProtKB
  • oxidation-reduction process Source: WormBase
  • protein glutathionylation Source: UniProtKB
  • response to oxidative stress Source: UniProtKB
  • response to superoxide Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Transferase

Enzyme and pathway databases

ReactomeiREACT_271650. Vitamin C (ascorbate) metabolism.
REACT_326456. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione transferase omega-1 (EC:2.5.1.18)
Alternative name(s):
Glutathione-dependent dehydroascorbate reductase (EC:1.8.5.1)
Monomethylarsonic acid reductase (EC:1.20.4.2)
Short name:
MMA(V) reductase
Gene namesi
Name:gsto-1
ORF Names:C29E4.7
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome III

Organism-specific databases

WormBaseiC29E4.7; CE00089; WBGene00016204; gsto-1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 250250Glutathione transferase omega-1PRO_0000185889Add
BLAST

Proteomic databases

PaxDbiP34345.
PRIDEiP34345.

Expressioni

Tissue specificityi

Expressed in the intestinal cells.1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi47837. 1 interaction.
DIPiDIP-24588N.
MINTiMINT-1080999.
STRINGi6239.C29E4.7.

Structurei

3D structure databases

ProteinModelPortaliP34345.
SMRiP34345. Positions 8-248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 10181GST N-terminalAdd
BLAST
Domaini106 – 234129GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni85 – 862Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Omega family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiNOG288793.
GeneTreeiENSGT00390000005479.
HOGENOMiHOG000006560.
InParanoidiP34345.
KOiK00799.
OMAiHYQGKAP.
OrthoDBiEOG71CFNG.
PhylomeDBiP34345.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01625. GSTRNSFRASEO.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P34345-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLTGVTSKA IRKGDAEPPL SKGSFRVYNM RFCPWAERAM LYVAAKGIEA
60 70 80 90 100
EVVNLNVTDK LEWYWTKHYQ GKAPAVEHNG KVVIESGFIP EYLDDAFPET
110 120 130 140 150
RILPTDPYEK VQQKLLADRL TAVAHAVPLL FAVMRDRTLK DEKQRKVFEV
160 170 180 190 200
LKQAENLLAN DFYAGSQPGY PDYLSFPFFE KIWWSASLDG VVDLPTIEFP
210 220 230 240 250
GEEEYPKLTK WFQKMISSDV VQSVTQSLEH GAAFMNAYAT HQELNYDLGL
Length:250
Mass (Da):28,478
Last modified:February 1, 1994 - v1
Checksum:i4EB0E85351217C55
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080706 Genomic DNA. Translation: CCD66006.1.
PIRiS44768.
RefSeqiNP_498728.1. NM_066327.1.
UniGeneiCel.10781.

Genome annotation databases

EnsemblMetazoaiC29E4.7; C29E4.7; WBGene00016204.
GeneIDi183000.
KEGGicel:CELE_C29E4.7.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
FO080706 Genomic DNA. Translation: CCD66006.1.
PIRiS44768.
RefSeqiNP_498728.1. NM_066327.1.
UniGeneiCel.10781.

3D structure databases

ProteinModelPortaliP34345.
SMRiP34345. Positions 8-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi47837. 1 interaction.
DIPiDIP-24588N.
MINTiMINT-1080999.
STRINGi6239.C29E4.7.

Proteomic databases

PaxDbiP34345.
PRIDEiP34345.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiC29E4.7; C29E4.7; WBGene00016204.
GeneIDi183000.
KEGGicel:CELE_C29E4.7.

Organism-specific databases

CTDi183000.
WormBaseiC29E4.7; CE00089; WBGene00016204; gsto-1.

Phylogenomic databases

eggNOGiNOG288793.
GeneTreeiENSGT00390000005479.
HOGENOMiHOG000006560.
InParanoidiP34345.
KOiK00799.
OMAiHYQGKAP.
OrthoDBiEOG71CFNG.
PhylomeDBiP34345.

Enzyme and pathway databases

ReactomeiREACT_271650. Vitamin C (ascorbate) metabolism.
REACT_326456. Glutathione conjugation.

Miscellaneous databases

NextBioi919570.
PROiP34345.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR005442. GST_omega.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
PRINTSiPR01625. GSTRNSFRASEO.
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Oxidative stress in Caenorhabditis elegans: protective effects of the Omega class glutathione transferase (GSTO-1)."
    Burmeister C., Luersen K., Heinick A., Hussein A., Domagalski M., Walter R.D., Liebau E.
    FASEB J. 22:343-354(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  3. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.

Entry informationi

Entry nameiGSTO1_CAEEL
AccessioniPrimary (citable) accession number: P34345
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 29, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Miscellaneous

Worms lacking gsto-1 exhibit increased sensitivity to heat shock and oxidative stress induced by several prooxidants and arsenite.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.