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 27-MAR-2024, entry version 153. 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=1.4 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 4932-YMR251W; -. DR PeptideAtlas; Q04806; -. DR EnsemblFungi; YMR251W_mRNA; YMR251W; YMR251W. DR GeneID; 855292; -. DR KEGG; sce:YMR251W; -. DR AGR; SGD:S000004863; -. 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 OrthoDB; 35622at2759; -. DR BioCyc; YEAST:G3O-32927-MONOMER; -. DR SABIO-RK; Q04806; -. DR BioGRID-ORCS; 855292; 0 hits in 10 CRISPR screens. 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 CDD; cd03190; GST_C_Omega_like; 1. DR Gene3D; 1.20.1050.10; -; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 1. 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; IPR047047; GST_Omega-like_C. DR InterPro; IPR016639; GST_Omega/GSH. DR InterPro; IPR036249; Thioredoxin-like_sf. DR PANTHER; PTHR32419:SF6; GLUTATHIONE S-TRANSFERASE OMEGA-LIKE 1-RELATED; 1. DR PANTHER; PTHR32419; GLUTATHIONYL-HYDROQUINONE REDUCTASE; 1. DR Pfam; PF13410; GST_C_2; 1. DR Pfam; PF13409; GST_N_2; 1. DR PIRSF; PIRSF015753; GST; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 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 //