GSTY2_PICKU
ID GSTY2_PICKU Reviewed; 191 AA.
AC P30102;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Glutathione S-transferase Y-2;
DE EC=2.5.1.18;
GN Name=GSTY2;
OS Pichia kudriavzevii (Yeast) (Issatchenkia orientalis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Pichia.
OX NCBI_TaxID=4909;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2054388; DOI=10.1016/0167-4781(91)90025-h;
RA Tamaki H., Kumagai H., Tochikura T.;
RT "Nucleotide sequence of the yeast glutathione S-transferase cDNA.";
RL Biochim. Biophys. Acta 1089:276-279(1991).
RN [2]
RP PROTEIN SEQUENCE OF 2-16 AND 164-189.
RX PubMed=2241960; DOI=10.1016/0006-291x(90)90726-4;
RA Tamaki H., Kumagai H., Tochikura T.;
RT "Glutathione S-transferase in yeast: induction of mRNA, cDNA cloning and
RT expression in Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 172:669-675(1990).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
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 -!- INDUCTION: By O-dinitrobenzene.
CC -!- SIMILARITY: Belongs to the GST superfamily. {ECO:0000305}.
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DR EMBL; X57957; CAA41025.1; -; mRNA.
DR PIR; S16178; S16178.
DR AlphaFoldDB; P30102; -.
DR SMR; P30102; -.
DR VEuPathDB; FungiDB:C5L36_0D05800; -.
DR eggNOG; KOG0867; Eukaryota.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
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 Direct protein sequencing; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2241960"
FT CHAIN 2..191
FT /note="Glutathione S-transferase Y-2"
FT /id="PRO_0000185983"
FT DOMAIN 2..80
FT /note="GST N-terminal"
FT DOMAIN 85..191
FT /note="GST C-terminal"
SQ SEQUENCE 191 AA; 21652 MW; 3BD1849C2C91363D CRC64;
MTFATVYIKP HTPRGDWLAS LGQYVGLEIK TVDYKSAEAS KFEELFPLKR VPALVTPNGF
QLTELIAIVE YIVAKGSKPE LSGKTTEERA TNTRWLSFFN SDFVQAAGGY FMGPNDEIKQ
QSLQTMLSLL EYIDKHLSQS KYFTNNTILT ADIFAFQIFA MAKQFGVDFT HYPNVERFTG
EVSQHPIIKN M