GTO2_YEAST
ID GTO2_YEAST Reviewed; 370 AA.
AC P36156; D6VXD6;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Glutathione S-transferase omega-like 2;
DE EC=2.5.1.18;
DE AltName: Full=Extracellular mutant protein 4;
DE AltName: Full=Glutathione-dependent dehydroascorbate reductase;
DE EC=1.8.5.1;
GN Name=ECM4; Synonyms=GTO2; OrderedLocusNames=YKR076W;
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=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 IDENTIFICATION.
RX PubMed=9335584; DOI=10.1093/genetics/147.2.435;
RA Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J.,
RA Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C.,
RA Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M.,
RA Davies J., Klis F.M., Robbins P.W., Bussey H.;
RT "Large scale identification of genes involved in cell surface biosynthesis
RT and architecture in Saccharomyces cerevisiae.";
RL Genetics 147:435-450(1997).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP FUNCTION, ENZYME ACTIVITY, ACTIVE SITE, BIOPHYSICOCHEMICAL PROPERTIES,
RP INDUCTION, AND MUTAGENESIS OF CYS-46; ARG-51; GLU-173; SER-174; LEU-246;
RP GLY-280 AND ASP-287.
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 [7]
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). May be involved in cell wall
CC organization and biogenesis. {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 -!- 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:16709151};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.42 mM for reduced glutathione (GSH)
CC {ECO:0000269|PubMed:16709151};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:16936141}.
CC -!- INDUCTION: Under oxidative stress conditions. By agents such as
CC diamide, 1-chloro-2,4-dinitrobenzene, tert-butyl hydroperoxide (t-BOOH)
CC and cadmium in a transcriptional factors YAP1 and/or MSN2/4-dependent
CC manner. {ECO:0000269|PubMed:16709151, ECO:0000269|PubMed:16936141}.
CC -!- MISCELLANEOUS: Present with 1670 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: A version of this protein truncated after amino acid 200
CC is not active in the beta-hydroxyethyl disulfide (HED) assay.
CC -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC {ECO:0000305}.
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DR EMBL; Z28301; CAA82155.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09226.1; -; Genomic_DNA.
DR PIR; S38153; S38153.
DR RefSeq; NP_013002.3; NM_001179866.3.
DR PDB; 5LKB; X-ray; 1.45 A; A/B=1-370.
DR PDB; 5LKD; X-ray; 1.68 A; A/B=1-370.
DR PDBsum; 5LKB; -.
DR PDBsum; 5LKD; -.
DR AlphaFoldDB; P36156; -.
DR SMR; P36156; -.
DR BioGRID; 34207; 264.
DR STRING; 4932.YKR076W; -.
DR MaxQB; P36156; -.
DR PaxDb; P36156; -.
DR PRIDE; P36156; -.
DR EnsemblFungi; YKR076W_mRNA; YKR076W; YKR076W.
DR GeneID; 853951; -.
DR KEGG; sce:YKR076W; -.
DR SGD; S000001784; ECM4.
DR VEuPathDB; FungiDB:YKR076W; -.
DR eggNOG; KOG2903; Eukaryota.
DR GeneTree; ENSGT00530000065151; -.
DR HOGENOM; CLU_037263_0_1_1; -.
DR InParanoid; P36156; -.
DR OMA; PWANRAI; -.
DR BioCyc; YEAST:G3O-32040-MON; -.
DR BRENDA; 1.8.5.7; 984.
DR SABIO-RK; P36156; -.
DR PRO; PR:P36156; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36156; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0045174; F:glutathione dehydrogenase (ascorbate) activity; IEA:UniProtKB-EC.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:SGD.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006749; P:glutathione metabolic process; IDA: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 3D-structure; Cell wall biogenesis/degradation; Cytoplasm; Oxidoreductase;
KW Reference proteome; Transferase.
FT CHAIN 1..370
FT /note="Glutathione S-transferase omega-like 2"
FT /id="PRO_0000086922"
FT DOMAIN 201..353
FT /note="GST C-terminal"
FT ACT_SITE 46
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:16709151"
FT MUTAGEN 46
FT /note="C->S,Y: Completely inactive as thiol transferase. No
FT activity recovered against 1-chloro-2,4-dinitrobenzene
FT (CDNB)."
FT /evidence="ECO:0000269|PubMed:16709151"
FT MUTAGEN 51
FT /note="R->A: No effect on thiol transferase activity. No
FT effect on thiol transferase activity; when associated with
FT D-173."
FT /evidence="ECO:0000269|PubMed:16709151"
FT MUTAGEN 173
FT /note="E->A,D: No effect on thiol transferase activity."
FT /evidence="ECO:0000269|PubMed:16709151"
FT MUTAGEN 174
FT /note="S->A: No effect on thiol transferase activity."
FT /evidence="ECO:0000269|PubMed:16709151"
FT MUTAGEN 246
FT /note="L->A: No effect on thiol transferase activity."
FT /evidence="ECO:0000269|PubMed:16709151"
FT MUTAGEN 280
FT /note="G->L: No effect on thiol transferase activity."
FT /evidence="ECO:0000269|PubMed:16709151"
FT MUTAGEN 287
FT /note="D->G: Abolishes thiol transferase activity."
FT /evidence="ECO:0000269|PubMed:16709151"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:5LKB"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:5LKB"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:5LKB"
FT TURN 101..104
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 106..109
FT /evidence="ECO:0007829|PDB:5LKD"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:5LKB"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:5LKB"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:5LKB"
FT TURN 164..167
FT /evidence="ECO:0007829|PDB:5LKB"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:5LKB"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 205..218
FT /evidence="ECO:0007829|PDB:5LKB"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 232..264
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 269..273
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 285..297
FT /evidence="ECO:0007829|PDB:5LKB"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 317..329
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:5LKB"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:5LKB"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:5LKB"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:5LKB"
SQ SEQUENCE 370 AA; 43274 MW; 2ED6659ADD4CA6ED CRC64;
MSKQWASGTN GAFKRQVSSF RETISKQHPI YKPAKGRYWL YVSLACPWAH RTLITRALKG
LTSVIGCSVV HWHLDEKGWR FLDMEKQLED SEDFLEHWHD VAGGIRTAKE DSSKSFAEIK
NDSQRFMVDA TNEPHYGYKR ISDLYYKSDP QYSARFTVPV LWDLETQTIV NNESSEIIRI
LNSSAFDEFV DDDHKKTDLV PAQLKTQIDD FNSWVYDSIN NGVYKTGFAE KAEVYESEVN
NVFEHLDKVE KILSDKYSKL KAKYGEEDRQ KILGEFFTVG DQLTEADIRL YTTVIRFDPV
YVQHFKCNFT SIRAGYPFIH LWVRNLYWNY DAFRYTTDFD HIKLHYTRSH TRINPLGITP
LGPKPDIRPL
