ID   GTO3_YEAST              Reviewed;         366 AA.
AC   Q04806; D6W077;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Glutathione S-transferase omega-like 3;
DE            EC=2.5.1.18;
GN   Name=GTO3; OrderedLocusNames=YMR251W; ORFNames=YM9920.05;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [4]
RP   FUNCTION, ENZYME ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=16709151; DOI=10.1042/bj20060034;
RA   Garcera A., Barreto L., Piedrafita L., Tamarit J., Herrero E.;
RT   "Saccharomyces cerevisiae cells have three Omega class glutathione S-
RT   transferases acting as 1-Cys thiol transferases.";
RL   Biochem. J. 398:187-196(2006).
RN   [5]
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=16936141; DOI=10.1128/ec.00216-06;
RA   Barreto L., Garcera A., Jansson K., Sunnerhagen P., Herrero E.;
RT   "A peroxisomal glutathione transferase of Saccharomyces cerevisiae is
RT   functionally related to sulfur amino acid metabolism.";
RL   Eukaryot. Cell 5:1748-1759(2006).
CC   -!- FUNCTION: Active as '1-Cys' thiol transferase against beta-hydroxyethyl
CC       disulfide (HED), as dehydroascorbate reductase and as dimethylarsinic
CC       acid reductase, while not active against the standard GST substrate 1-
CC       chloro-2,4-dinitrobenzene (CDNB). {ECO:0000269|PubMed:16709151}.
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:0000269|PubMed:16709151};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.40 mM for reduced glutathione (GSH)
CC         {ECO:0000269|PubMed:16709151};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16936141}.
CC   -!- INDUCTION: Up-regulated by tert-butyl hydroperoxide (t-BOOH) in an
CC       MSN2/4-dependent manner. {ECO:0000269|PubMed:16936141}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC       {ECO:0000305}.
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DR   EMBL; Z48639; CAA88578.1; -; Genomic_DNA.
DR   EMBL; AY692580; AAT92599.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10151.1; -; Genomic_DNA.
DR   PIR; S53073; S53073.
DR   RefSeq; NP_013977.1; NM_001182757.1.
DR   AlphaFoldDB; Q04806; -.
DR   SMR; Q04806; -.
DR   BioGRID; 35429; 31.
DR   DIP; DIP-6643N; -.
DR   IntAct; Q04806; 1.
DR   STRING; 4932.YMR251W; -.
DR   PaxDb; Q04806; -.
DR   PRIDE; Q04806; -.
DR   EnsemblFungi; YMR251W_mRNA; YMR251W; YMR251W.
DR   GeneID; 855292; -.
DR   KEGG; sce:YMR251W; -.
DR   SGD; S000004863; GTO3.
DR   VEuPathDB; FungiDB:YMR251W; -.
DR   eggNOG; KOG2903; Eukaryota.
DR   GeneTree; ENSGT00530000065151; -.
DR   HOGENOM; CLU_037263_0_1_1; -.
DR   InParanoid; Q04806; -.
DR   OMA; YQLFVSY; -.
DR   BioCyc; YEAST:G3O-32927-MON; -.
DR   SABIO-RK; Q04806; -.
DR   PRO; PR:Q04806; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q04806; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:SGD.
DR   GO; GO:0006749; P:glutathione metabolic process; ISS:SGD.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR016639; GST_Omega/GSH.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR32419; PTHR32419; 1.
DR   Pfam; PF13409; GST_N_2; 1.
DR   PIRSF; PIRSF015753; GST; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; Transferase.
FT   CHAIN           1..366
FT                   /note="Glutathione S-transferase omega-like 3"
FT                   /id="PRO_0000203338"
FT   DOMAIN          197..349
FT                   /note="GST C-terminal"
FT   ACT_SITE        46
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   366 AA;  42403 MW;  C0BF9F2D3AB5C15B CRC64;
     MSEKSASNNK AEFKRQSSPF REIISADHPI YKPAKGRYWL YVALPCPWAQ RTLITRALKG
     LAPIIGCSVA HWHLDDKGWR FLEEGDGKTN ERHWFDIAGG ISSVNLNTST PVANIPNNAH
     RLLVDGTDEP HYGYKRLSDF YFKTKPDYKG RFTVPVLWDL ETCTIVNNES SDIIGIMNSA
     AFDEFVGEEY RQVRLVPRSL EAQITEFNSW VYDKINNGVY KAGFAECAEV YEREVTSLFQ
     YLDKLENLLD KKYTDLEAEY GKNNKDKILD RYFAIGDTLT EADVRLYPTI VRFDVVYHQH
     FKCNLATIRD DYSRIHTWLK NIYWRHEAFQ RTTDFTHIKL GYTRSQPRVN PIGITPLGPK
     PDIRPP