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   22-FEB-2023, entry version 87.
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   OrthoDB; 159792at2759; -.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   CDD; cd03044; GST_N_EF1Bgamma; 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; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43986; ELONGATION FACTOR 1-GAMMA; 1.
DR   PANTHER; PTHR43986:SF1; ELONGATION FACTOR 1-GAMMA; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 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
//