ID   GSTT1_DROSI             Reviewed;         209 AA.
AC   P67805; B4QSX6; P30105; Q963F1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   03-AUG-2022, entry version 90.
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;
GN   Name=GstD1; Synonyms=gst, GST1; ORFNames=GD20577;
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Le Goff G., Berge J.-B., Amichot M.;
RT   "Cloning of the Drosophila simulans glutathione S-transferase D1.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-208.
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; AF386788; AAK66764.1; -; mRNA.
DR   EMBL; CM000364; EDX13236.1; -; Genomic_DNA.
DR   EMBL; M84577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; P67805; -.
DR   SMR; P67805; -.
DR   STRING; 7240.P67805; -.
DR   EnsemblMetazoa; FBtr0220487; FBpp0218979; FBgn0012838.
DR   HOGENOM; CLU_011226_2_1_1; -.
DR   OMA; KYEVLQW; -.
DR   PhylomeDB; P67805; -.
DR   ChiTaRS; GstS1; fly.
DR   Proteomes; UP000000304; Chromosome 3r.
DR   Bgee; FBgn0012838; Expressed in female reproductive system and 3 other tissues.
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; IPR040079; Glutathione_S-Trfase.
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   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   Lyase; Reference proteome; Transferase.
FT   CHAIN           1..209
FT                   /note="Glutathione S-transferase 1-1"
FT                   /id="PRO_0000185951"
FT   DOMAIN          1..81
FT                   /note="GST N-terminal"
FT   DOMAIN          87..209
FT                   /note="GST C-terminal"
FT   BINDING         10
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         51..53
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         65..67
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        2
FT                   /note="A -> V (in Ref. 1; AAK66764)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="E -> S (in Ref. 3; M84577)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        207
FT                   /note="Y -> F (in Ref. 3; M84577)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   209 AA;  23755 MW;  E1FED3D6423D9B1A CRC64;
     MADFYYLPGS SPCRSVIMTA KAVGVELNKK LLNLQAGEHL KPEFLKINPQ HTIPTLVDNG
     FALWESRAIQ VYLVEKYGKT DSLYPKCPKK RAVINQRLYF DMGTLYQSFA NYYYPQVFAK
     APADPEAFKK IESAFEFLNT FLEGQEYAAG DSLTVADIAL VASVSTFEVA GFEISKYANV
     NKWYENAKKV TPGWEENWAG CLEFKKYFE