ID   GST_MUSDO               Reviewed;         241 AA.
AC   P46437;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Glutathione S-transferase;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-sigma;
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=Cooper; TISSUE=Head;
RA   Franciosa H.;
RL   Submitted (OCT-1993) 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. Sigma family.
CC       {ECO:0000305}.
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DR   EMBL; U02616; AAA03434.1; -; mRNA.
DR   RefSeq; NP_001273827.1; NM_001286898.1.
DR   RefSeq; XP_011295686.1; XM_011297384.2.
DR   AlphaFoldDB; P46437; -.
DR   SMR; P46437; -.
DR   STRING; 7370.XP_005191089.1; -.
DR   GeneID; 101890455; -.
DR   KEGG; mde:101890455; -.
DR   CTD; 101890455; -.
DR   VEuPathDB; VectorBase:MDOA005193; -.
DR   eggNOG; KOG1695; Eukaryota.
DR   Proteomes; UP000095301; Unplaced.
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; PF14497; GST_C_3; 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   2: Evidence at transcript level;
KW   Transferase.
FT   CHAIN           1..241
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000185919"
FT   DOMAIN          40..117
FT                   /note="GST N-terminal"
FT   DOMAIN          119..241
FT                   /note="GST C-terminal"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         46
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         77
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         81
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:P46088"
FT   BINDING         87..89
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
FT   BINDING         101..102
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250|UniProtKB:O60760"
SQ   SEQUENCE   241 AA;  26964 MW;  6A8FBD67ADDDEDFA CRC64;
     MADEAPAAPP AEGEAPAAPA EGEAPPPAEG EAPPAEPVKN TYTLFYFNVK ALAEPLRYLF
     AYGGIEYEDV RVTRDEWPAL KPTMPMGQMP VLEVNGKRVH QSISMARFLA KTVGLCGATP
     WEDLQVDIVV DTINDFRLKI AVVSYEPEDE IKEKKLVTLN NEVIPFYLEK LEQTVKDNDG
     HLALNKLTWA DVYFAGILDY MNYMVKRDIL EQYPALRGVV DSVNALEPIK AWIEKRPQTE
     V