ID   GST2_ASCSU              Reviewed;          20 AA.
AC   P48429;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 43.
DE   RecName: Full=Glutathione S-transferase 2;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-sigma;
DE   Flags: Fragment;
GN   Name=GST2;
OS   Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX   NCBI_TaxID=6253;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8183318; DOI=10.1016/0166-6851(94)90021-3;
RA   Liebau E., Schoenberger O.L., Walter R.D., Henkle-Duehrsen K.J.;
RT   "Molecular cloning and expression of a cDNA encoding glutathione S-
RT   transferase from Ascaris suum.";
RL   Mol. Biochem. Parasitol. 63:167-170(1994).
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   -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC       {ECO:0000305}.
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DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Transferase.
FT   CHAIN           1..>20
FT                   /note="Glutathione S-transferase 2"
FT                   /id="PRO_0000185924"
FT   DOMAIN          1..>20
FT                   /note="GST N-terminal"
FT   BINDING         6
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2249 MW;  A506D5F2B144FB20 CRC64;
     GYKVTYFAIR GLAEPIXLLL