ID   GSTT1_DROYA             Reviewed;         209 AA.
AC   P30108; B4PNR1;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 2.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Glutathione S-transferase 1-1;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-theta;
GN   Name=GstD1; Synonyms=GST, Gst1; ORFNames=GE24527;
OS   Drosophila yakuba (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01;
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   [2]
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.
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.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {ECO:0000305}.
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DR   EMBL; CM000160; EDW97076.1; -; Genomic_DNA.
DR   EMBL; M84580; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_002097364.1; XM_002097328.2.
DR   AlphaFoldDB; P30108; -.
DR   SMR; P30108; -.
DR   STRING; 7245.FBpp0269537; -.
DR   EnsemblMetazoa; FBtr0271045; FBpp0269537; FBgn0013168.
DR   GeneID; 6536794; -.
DR   KEGG; dya:Dyak_GE24527; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   HOGENOM; CLU_011226_2_1_1; -.
DR   OMA; KYEVLQW; -.
DR   OrthoDB; 1231780at2759; -.
DR   PhylomeDB; P30108; -.
DR   ChiTaRS; GstS1; fly.
DR   Proteomes; UP000002282; Chromosome 3R.
DR   GO; GO:0018833; F:DDT-dehydrochlorinase activity; IEA:EnsemblMetazoa.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:EnsemblMetazoa.
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   Transferase.
FT   CHAIN           1..209
FT                   /note="Glutathione S-transferase 1-1"
FT                   /id="PRO_0000185953"
FT   DOMAIN          1..81
FT                   /note="GST N-terminal"
FT   DOMAIN          87..209
FT                   /note="GST C-terminal"
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        195
FT                   /note="E -> S (in Ref. 2; M84580)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   209 AA;  23725 MW;  5FAF3267E4F1410D CRC64;
     MADFYYLPGS SPCRSVIMTA KAVGVELNKK LLNLQAGEHL KPEFLKINPQ HTIPTLVDNG
     FALWESRAIQ VYLVEKYGKT DSLYPKCPKK RAVINQRLYF DMGTLYQSFA NYYYPQVFAK
     APADPEAFKK IEAAFEFLNT FLEGQDYAAG DSLTVADIAL VASVSTFEVA GFEISKYANV
     NKWYENAKKV TPGWEENWAG CLEFKKYFE