GSTT1_DROSE
ID GSTT1_DROSE Reviewed; 209 AA.
AC P30106; B4HHD9;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 2.
DT 03-AUG-2022, entry version 109.
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=GM26019;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25;
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. 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; CH480815; EDW42478.1; -; Genomic_DNA.
DR EMBL; M84578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002031492.1; XM_002031456.1.
DR AlphaFoldDB; P30106; -.
DR SMR; P30106; -.
DR STRING; 7238.P30106; -.
DR EnsemblMetazoa; FBtr0209004; FBpp0207496; FBgn0012785.
DR GeneID; 6606692; -.
DR KEGG; dse:6606692; -.
DR HOGENOM; CLU_011226_2_1_1; -.
DR OMA; KYEVLQW; -.
DR PhylomeDB; P30106; -.
DR ChiTaRS; GstS1; fly.
DR Proteomes; UP000001292; Unassembled WGS sequence.
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:EnsemblMetazoa.
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 3: Inferred from homology;
KW Lyase; Reference proteome; Transferase.
FT CHAIN 1..209
FT /note="Glutathione S-transferase 1-1"
FT /id="PRO_0000185950"
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 195
FT /note="E -> S (in Ref. 2; M84578)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 23767 MW; CD023FF2D076F716 CRC64;
MADFYYLPGS SPCRSVIMTA KAVGVELNKK LLNLRAGEHL KPEFLKINPQ HTIPTLVDNG
FALWESRAIQ VYLVEKYGKT DSLYPKCPKK RAVINQRLYF DMGTLYQSFA NYYYPQVFAK
APADPEAFKK IESAFEFLNT FLEGQEYAAG DSLTVADIAL VASVSTFEVA GFEISKYANV
NKWYENAKKV TPGWEENWAG CLEFKKFFE
