ID   GSTT2_MUSDO             Reviewed;         210 AA.
AC   P46431;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Glutathione S-transferase 2;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-theta;
GN   Name=Gst2; Synonyms=Gst-2;
OS   Musca domestica (House fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea;
OC   Muscidae; Musca.
OX   NCBI_TaxID=7370;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Cornell-R;
RX   PubMed=7845356; DOI=10.1007/bf00279747;
RA   Syvanen M., Zhou Z., Wang J.;
RT   "Glutathione transferase gene family from the housefly Musca domestica.";
RL   Mol. Gen. Genet. 245:25-31(1994).
RN   [2]
RP   SEQUENCE REVISION.
RA   Syvanen M.;
RL   Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {ECO:0000305}.
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DR   EMBL; X73574; CAA51976.1; -; mRNA.
DR   PIR; S70851; S70851.
DR   RefSeq; NP_001295926.1; NM_001308997.1.
DR   AlphaFoldDB; P46431; -.
DR   SMR; P46431; -.
DR   STRING; 7370.XP_005180100.1; -.
DR   GeneID; 101897277; -.
DR   KEGG; mde:101897277; -.
DR   VEuPathDB; VectorBase:MDOA011215; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   Proteomes; UP000095301; Whole Genome Shotgun Assembly.
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; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 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..210
FT                   /note="Glutathione S-transferase 2"
FT                   /id="PRO_0000185966"
FT   DOMAIN          1..80
FT                   /note="GST N-terminal"
FT   DOMAIN          87..208
FT                   /note="GST C-terminal"
FT   BINDING         9
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         50..52
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..66
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   210 AA;  24344 MW;  EC8ADA2B54AA2F38 CRC64;
     MDFYYLPLSA PCRSVIMTAK ALGIELNKKL LNLFEGEHLK PEFLKINPQH TIPTLVDNGF
     AMWESRAIMV YLVEKYGKQN DPLYPSCPKK RALINQRLYF DMGTLWKSYA DYTYPQFREN
     KPADPELFKK FESALEFLNI FLSQSKYAAG ETMTLADLAI LASVSTFDVV QMDLSKYEHI
     LRWYNMLKDT APGAAENWAG CLEMKKYFKK