ID   GST2_MANSE              Reviewed;         203 AA.
AC   P46429;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Glutathione S-transferase 2;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-sigma;
GN   Name=GST2;
OS   Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Bombycoidea;
OC   Sphingidae; Sphinginae; Sphingini; Manduca.
OX   NCBI_TaxID=7130;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Midgut;
RX   PubMed=7742833; DOI=10.1016/0965-1748(94)00083-b;
RA   Snyder M.J., Walding J.K., Feyereisen R.;
RT   "Glutathione S-transferases from larval Manduca sexta midgut: sequence of
RT   two cDNAs and enzyme induction.";
RL   Insect Biochem. Mol. Biol. 25:455-465(1995).
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INDUCTION: By dietary chemicals.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC       {ECO:0000305}.
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DR   EMBL; L32092; AAA92881.1; -; mRNA.
DR   AlphaFoldDB; P46429; -.
DR   SMR; P46429; -.
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; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   2: Evidence at transcript level;
KW   Transferase.
FT   CHAIN           1..203
FT                   /note="Glutathione S-transferase 2"
FT                   /id="PRO_0000185918"
FT   DOMAIN          1..78
FT                   /note="GST N-terminal"
FT   DOMAIN          80..203
FT                   /note="GST C-terminal"
FT   BINDING         8
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         38
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         42
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P46088"
FT   BINDING         48..50
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         62..63
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
SQ   SEQUENCE   203 AA;  23596 MW;  D5EC67F119DE470D CRC64;
     MPKVVFHYFG AKGWARPTML LAYGGQEFED HRVEYEQWPE FKPNTPFGQM PVLEIDGKKY
     AQSLAISRYL GRKYGLAGND IEEDFEIDQI VDFVNDIRAS AASVEYEQDA ANKEVKHEEN
     MKNKYPFQLN KLSEIITKNN GFLALGRLTW ADFVFVGMFD YLKKMLRMPD LEEQYPIFKK
     PIETVLSNPK LKAYLDSAPK KEF