GSTO1_CAEEL
ID GSTO1_CAEEL Reviewed; 250 AA.
AC P34345;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Glutathione transferase omega-1;
DE EC=2.5.1.18 {ECO:0000269|PubMed:17901115};
DE AltName: Full=Glutathione-dependent dehydroascorbate reductase;
DE EC=1.8.5.1 {ECO:0000269|PubMed:17901115};
DE AltName: Full=Monomethylarsonic acid reductase;
DE Short=MMA(V) reductase;
DE EC=1.20.4.2 {ECO:0000269|PubMed:17901115};
GN Name=gsto-1; ORFNames=C29E4.7;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-33.
RX PubMed=17901115; DOI=10.1096/fj.06-7426com;
RA Burmeister C., Luersen K., Heinick A., Hussein A., Domagalski M.,
RA Walter R.D., Liebau E.;
RT "Oxidative stress in Caenorhabditis elegans: protective effects of the
RT Omega class glutathione transferase (GSTO-1).";
RL FASEB J. 22:343-354(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Exhibits glutathione-dependent thiol transferase activity (By
CC similarity). Has dehydroascorbate reductase activity and may contribute
CC to the recycling of ascorbic acid (By similarity). Participates in the
CC biotransformation of inorganic arsenic and reduces monomethylarsonic
CC acid (MMA) (By similarity). Protects against environmental stress and
CC oxidative stress (PubMed:17901115). {ECO:0000250|UniProtKB:P78417,
CC ECO:0000269|PubMed:17901115}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC Evidence={ECO:0000250|UniProtKB:P78417};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + L-dehydroascorbate = glutathione disulfide +
CC L-ascorbate; Xref=Rhea:RHEA:24424, ChEBI:CHEBI:38290,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297, ChEBI:CHEBI:58539; EC=1.8.5.1;
CC Evidence={ECO:0000269|PubMed:17901115};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 glutathione + H(+) + methylarsonate = glutathione disulfide
CC + H2O + methylarsonous acid; Xref=Rhea:RHEA:15969, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17826, ChEBI:CHEBI:33409,
CC ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.20.4.2;
CC Evidence={ECO:0000269|PubMed:17901115};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=51.52 uM for 1-chloro-2,4-dintrobenzene
CC {ECO:0000269|PubMed:17901115};
CC KM=184.1 uM for dehydroascorbate {ECO:0000269|PubMed:17901115};
CC KM=70.77 uM for 2-hydroxyethyl disulfide
CC {ECO:0000269|PubMed:17901115};
CC Vmax=106 nmol/min/mg enzyme towards 1-chloro-2,4-dintrobenzene
CC {ECO:0000269|PubMed:17901115};
CC Vmax=32 nmol/min/mg enzyme towards cumene hydroperoxide
CC {ECO:0000269|PubMed:17901115};
CC Vmax=186 nmol/min/mg enzyme towards dehydroascorbate
CC {ECO:0000269|PubMed:17901115};
CC Vmax=192 nmol/min/mg enzyme towards 2-hydroxyethyl disulfide
CC {ECO:0000269|PubMed:17901115};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the intestinal cells.
CC {ECO:0000269|PubMed:17901115}.
CC -!- DEVELOPMENTAL STAGE: Expressed in late embryos, during the L1 to L4
CC stages of larval development and in adult hermaphrodites.
CC {ECO:0000269|PubMed:17901115}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in increased
CC sensitivity and reduced survival in response to oxidative stress
CC inducers cumene hydroperoxide, jugalone, paraquat and arsenite, and to
CC heat shock treatment. {ECO:0000269|PubMed:17901115}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC {ECO:0000305}.
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DR EMBL; FO080706; CCD66006.1; -; Genomic_DNA.
DR PIR; S44768; S44768.
DR RefSeq; NP_498728.1; NM_066327.1.
DR AlphaFoldDB; P34345; -.
DR SMR; P34345; -.
DR BioGRID; 47837; 2.
DR DIP; DIP-24588N; -.
DR STRING; 6239.C29E4.7; -.
DR EPD; P34345; -.
DR PaxDb; P34345; -.
DR PeptideAtlas; P34345; -.
DR PRIDE; P34345; -.
DR EnsemblMetazoa; C29E4.7.1; C29E4.7.1; WBGene00016204.
DR GeneID; 183000; -.
DR KEGG; cel:CELE_C29E4.7; -.
DR CTD; 183000; -.
DR WormBase; C29E4.7; CE00089; WBGene00016204; gsto-1.
DR eggNOG; KOG0406; Eukaryota.
DR HOGENOM; CLU_011226_9_2_1; -.
DR InParanoid; P34345; -.
DR OMA; ESMVICE; -.
DR OrthoDB; 1225872at2759; -.
DR PhylomeDB; P34345; -.
DR Reactome; R-CEL-156581; Methylation.
DR Reactome; R-CEL-156590; Glutathione conjugation.
DR Reactome; R-CEL-196836; Vitamin C (ascorbate) metabolism.
DR SABIO-RK; P34345; -.
DR PRO; PR:P34345; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00016204; Expressed in larva and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IDA:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0050610; F:methylarsonate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0031668; P:cellular response to extracellular stimulus; IDA:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
DR GO; GO:0010731; P:protein glutathionylation; IDA:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
DR GO; GO:0000303; P:response to superoxide; IMP:WormBase.
DR InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR004046; GST_C.
DR InterPro; IPR005442; GST_omega.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR PRINTS; PR01625; GSTRNSFRASEO.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SUPFAM; SSF47616; SSF47616; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS50405; GST_CTER; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Oxidoreductase; Reference proteome; Transferase.
FT CHAIN 1..250
FT /note="Glutathione transferase omega-1"
FT /id="PRO_0000185889"
FT DOMAIN 21..101
FT /note="GST N-terminal"
FT DOMAIN 106..234
FT /note="GST C-terminal"
FT ACT_SITE 33
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P78417"
FT BINDING 60
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9H4Y5"
FT BINDING 85..86
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:Q9H4Y5"
FT MUTAGEN 33
FT /note="C->A: Increased sensitivity to oxidative stress when
FT exposed to cumene hydroperoxide."
FT /evidence="ECO:0000269|PubMed:17901115"
SQ SEQUENCE 250 AA; 28478 MW; 4EB0E85351217C55 CRC64;
MVLTGVTSKA IRKGDAEPPL SKGSFRVYNM RFCPWAERAM LYVAAKGIEA EVVNLNVTDK
LEWYWTKHYQ GKAPAVEHNG KVVIESGFIP EYLDDAFPET RILPTDPYEK VQQKLLADRL
TAVAHAVPLL FAVMRDRTLK DEKQRKVFEV LKQAENLLAN DFYAGSQPGY PDYLSFPFFE
KIWWSASLDG VVDLPTIEFP GEEEYPKLTK WFQKMISSDV VQSVTQSLEH GAAFMNAYAT
HQELNYDLGL
