ID GSTT1_DROTE Reviewed; 200 AA.
AC P30107;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 22-FEB-2023, entry version 94.
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 teissieri (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7243;
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; M84579; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P30107; -.
DR SMR; P30107; -.
DR FlyBase; FBgn0013016; Dtei\GstD1.
DR GO; GO:0018833; F:DDT-dehydrochlorinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR CDD; cd03177; GST_C_Delta_Epsilon; 1.
DR CDD; cd03045; GST_N_Delta_Epsilon; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
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 PANTHER; PTHR43969; GLUTATHIONE S TRANSFERASE D10, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR43969:SF9; GLUTATHIONE S TRANSFERASE D10, ISOFORM A-RELATED; 1.
DR Pfam; PF00043; GST_C; 1.
DR Pfam; PF02798; GST_N; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG01153; Main.4:_Theta-like; 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 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_0000185952"
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; 22595 MW; C3169316B12D9FA1 CRC64;
GSSPCRSVIM TAKAVGVELN KKLLNLQAGE HLKPEFVKIN PQHTIPTLVD NGFALWESRA
IQVYLVEKYG KTDSLYPKCP KKRAVINQRL YFDMGTLYQS FANYYYPQVF AKAPADPEAF
KKIEAAFEFL NTFLEGQEYA AGDSLTVADI ALVASVSTFE VAGFEISKYA NVNKWYENAK
KVTPGWEENW AGCLEFKKYF
//
