GTO1_YEAST
ID GTO1_YEAST Reviewed; 356 AA.
AC P48239; D6VUT4;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Glutathione S-transferase omega-like 1;
DE EC=2.5.1.18;
DE AltName: Full=Glutathione-dependent dehydroascorbate reductase;
DE EC=1.8.5.1;
GN Name=GTO1; OrderedLocusNames=YGR154C; ORFNames=G6664;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8585325; DOI=10.1002/yea.320111410;
RA Skala J., Nawrocki A., Goffeau A.;
RT "The sequence of a 27 kb segment on the right arm of chromosome VII from
RT Saccharomyces cerevisiae reveals MOL1, NAT2, RPL30B, RSR1, CYS4, PEM1/CHO2,
RT NSR1 genes and ten new open reading frames.";
RL Yeast 11:1421-1427(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [3]
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 [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 DISRUPTION PHENOTYPE, 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 -!- 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=1.13 mM for reduced glutathione (GSH)
CC {ECO:0000269|PubMed:16709151};
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:16936141}.
CC -!- INDUCTION: By diamide and 1-chloro-2,4-dinitrobenzene (CDNB) in a
CC transcriptional factors YAP1 and/or MSN2/4-dependent manner.
CC {ECO:0000269|PubMed:16936141}.
CC -!- DISRUPTION PHENOTYPE: Null mutants display increased sensitivity to
CC cadmium in the absence of GTT1 and GTT2. Null mutants also show growth
CC defects on oleic acid-based medium, indicative of abnormal peroxisomal
CC functions and altered expression of genes related to sulfur amino acid
CC metabolism, and have low levels of reduced glutathione.
CC {ECO:0000269|PubMed:16936141}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Omega family.
CC {ECO:0000305}.
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DR EMBL; X85807; CAA59811.1; -; Genomic_DNA.
DR EMBL; Z72939; CAA97168.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08245.1; -; Genomic_DNA.
DR PIR; S60444; S60444.
DR RefSeq; NP_011670.3; NM_001181283.3.
DR AlphaFoldDB; P48239; -.
DR SMR; P48239; -.
DR BioGRID; 33402; 77.
DR DIP; DIP-1867N; -.
DR IntAct; P48239; 2.
DR MINT; P48239; -.
DR STRING; 4932.YGR154C; -.
DR PaxDb; P48239; -.
DR PRIDE; P48239; -.
DR EnsemblFungi; YGR154C_mRNA; YGR154C; YGR154C.
DR GeneID; 853058; -.
DR KEGG; sce:YGR154C; -.
DR SGD; S000003386; GTO1.
DR VEuPathDB; FungiDB:YGR154C; -.
DR eggNOG; KOG2903; Eukaryota.
DR GeneTree; ENSGT00530000065151; -.
DR HOGENOM; CLU_037263_0_1_1; -.
DR InParanoid; P48239; -.
DR OMA; AHQPYLF; -.
DR BioCyc; YEAST:G3O-30856-MON; -.
DR SABIO-RK; P48239; -.
DR PRO; PR:P48239; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P48239; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; 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:0006749; P:glutathione metabolic process; ISS:SGD.
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.
PE 1: Evidence at protein level;
KW Coiled coil; Oxidoreductase; Peroxisome; Reference proteome; Transferase.
FT CHAIN 1..356
FT /note="Glutathione S-transferase omega-like 1"
FT /id="PRO_0000202833"
FT COILED 214..257
FT /evidence="ECO:0000255"
FT ACT_SITE 31
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
SQ SEQUENCE 356 AA; 41301 MW; B4639BD195CDF7F5 CRC64;
MSVSYKGTIS KTHSVFKPEK GRYYIYGALG CPFTHRAILA RSLKKLEPVL GLVLSHWQLD
SKGARFLPAP HRPEKYKERF FTATGGIASA KLDESEELGD VNNDSARLFV DGAFDPVENI
SRLSELYYLN DPKYPGTKFT VPVLWDSKTR KIVNNESGDI IRILNSGVFD EFIQSEETNV
IDLVPHDLID EIDKNIKWVH PKINLGVYKV GLAENGKIYE TEVKTLFENL QKMECVLKEN
YKRLEEQFSG NKQKILAKYF VLGQRLTEAD IRLYPSIIRF DVVYVQHFKC NLKTIRDGFP
YLHLWLINLY WNYAEFRFTT DFNHIKLFYI RMEVSRNKIN QFGIVPLGPK PDISRL
