GST1_YEAST
ID GST1_YEAST Reviewed; 234 AA.
AC P40582; D6VVW9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Glutathione S-transferase 1;
DE EC=2.5.1.18;
DE AltName: Full=GST-I;
GN Name=GTT1; OrderedLocusNames=YIR038C;
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 CHARACTERIZATION.
RX PubMed=9792709; DOI=10.1074/jbc.273.45.29915;
RA Choi J.H., Lou W., Vancura A.;
RT "A novel membrane-bound glutathione S-transferase functions in the
RT stationary phase of the yeast Saccharomyces cerevisiae.";
RL J. Biol. Chem. 273:29915-29922(1998).
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 -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; Z38061; CAA86198.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08585.1; -; Genomic_DNA.
DR PIR; S48500; S48500.
DR RefSeq; NP_012304.1; NM_001179560.1.
DR AlphaFoldDB; P40582; -.
DR SMR; P40582; -.
DR BioGRID; 35029; 106.
DR DIP; DIP-2103N; -.
DR IntAct; P40582; 72.
DR MINT; P40582; -.
DR STRING; 4932.YIR038C; -.
DR iPTMnet; P40582; -.
DR MaxQB; P40582; -.
DR PaxDb; P40582; -.
DR PRIDE; P40582; -.
DR EnsemblFungi; YIR038C_mRNA; YIR038C; YIR038C.
DR GeneID; 854856; -.
DR KEGG; sce:YIR038C; -.
DR SGD; S000001477; GTT1.
DR VEuPathDB; FungiDB:YIR038C; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_15_1_1; -.
DR InParanoid; P40582; -.
DR OMA; ADVQMSF; -.
DR BioCyc; MetaCyc:YIR038C-MON; -.
DR BioCyc; YEAST:YIR038C-MON; -.
DR SABIO-RK; P40582; -.
DR PRO; PR:P40582; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40582; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:SGD.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:SGD.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:SGD.
DR GO; GO:0010731; P:protein glutathionylation; IMP:SGD.
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; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
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 Endoplasmic reticulum; Membrane; Reference proteome; Transferase.
FT CHAIN 1..234
FT /note="Glutathione S-transferase 1"
FT /id="PRO_0000185987"
FT DOMAIN 3..90
FT /note="GST N-terminal"
FT DOMAIN 96..234
FT /note="GST C-terminal"
SQ SEQUENCE 234 AA; 26795 MW; 3C07D40D29F60DFF CRC64;
MSLPIIKVHW LDHSRAFRLL WLLDHLNLEY EIVPYKRDAN FRAPPELKKI HPLGRSPLLE
VQDRETGKKK ILAESGFIFQ YVLQHFDHSH VLMSEDADIA DQINYYLFYV EGSLQPPLMI
EFILSKVKDS GMPFPISYLA RKVADKISQA YSSGEVKNQF DFVEGEISKN NGYLVDGKLS
GADILMSFPL QMAFERKFAA PEDYPAISKW LKTITSEESY AASKEKARAL GSNF
