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GSTT1_DROMA
ID   GSTT1_DROMA             Reviewed;         200 AA.
AC   P67804; P30105;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Glutathione S-transferase 1-1;
DE            EC=2.5.1.18;
DE            EC=4.5.1.1;
DE   AltName: Full=DDT-dehydrochlorinase;
DE   AltName: Full=GST class-theta;
DE   Flags: Fragment;
GN   Name=GstD1; Synonyms=gst, GST1;
OS   Drosophila mauritiana (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Hargis M.T., Cochrane B.J.;
RT   "Sequence divergence of glutathione S-transferase coding regions among
RT   seven species in the melanogaster subgroup of Drosophila.";
RL   Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles. Has DDT
CC       dehydrochlorinase activity (By similarity). {ECO:0000250}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-
CC         2,2-bis(4-chlorophenyl)ethylene + chloride + H(+);
CC         Xref=Rhea:RHEA:19217, ChEBI:CHEBI:15378, ChEBI:CHEBI:16130,
CC         ChEBI:CHEBI:16598, ChEBI:CHEBI:17996; EC=4.5.1.1;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {ECO:0000305}.
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DR   EMBL; M84581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P67804; -.
DR   SMR; P67804; -.
DR   FlyBase; FBgn0012503; Dmau\GstD1.
DR   GO; GO:0018833; F:DDT-dehydrochlorinase activity; IEA:UniProtKB-EC.
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; 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   3: Inferred from homology;
KW   Lyase; Transferase.
FT   CHAIN           <1..200
FT                   /note="Glutathione S-transferase 1-1"
FT                   /id="PRO_0000185949"
FT   DOMAIN          <1..73
FT                   /note="GST N-terminal"
FT   DOMAIN          79..200
FT                   /note="GST C-terminal"
FT   BINDING         2
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         43..45
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         57..59
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   200 AA;  22567 MW;  E0F93FFA2C48CA26 CRC64;
     GSSPCRSVIM TAKAVGVELN KKLLNLQAGE HLKPEFLKIN PQHTIPTLVD NGFALWESRA
     IQVYLVEKYG KTDSLYPKCP KKRAVINQRL YFDMGTLYQS FANYYYPQVF AKAPADPEAF
     KKIESAFEFL NTFLEGQEYA AGDSLTVADI ALVASVSTFE VAGFEISKYA NVNKWYENAK
     KVTPGWSENW AGCLEFKKFF
 
 
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