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Database: UniProt/SWISS-PROT
Entry: GSTT1_DROSE
LinkDB: GSTT1_DROSE
Original site: 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   05-DEC-2018, entry version 93.
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;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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-
CC         dichloro-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}.
DR   EMBL; CH480815; EDW42478.1; -; Genomic_DNA.
DR   EMBL; M84578; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_002031492.1; XM_002031456.1.
DR   ProteinModelPortal; P30106; -.
DR   SMR; P30106; -.
DR   PRIDE; P30106; -.
DR   EnsemblMetazoa; FBtr0209004; FBpp0207496; FBgn0012785.
DR   GeneID; 6606692; -.
DR   KEGG; dse:Dsec_GM26019; -.
DR   FlyBase; FBgn0012785; Dsec\GstD1.
DR   KO; K00799; -.
DR   OMA; RFIQFYL; -.
DR   OrthoDB; EOG091G0MS3; -.
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   Complete proteome; Lyase; Reference proteome; Transferase.
FT   CHAIN         1    209       Glutathione S-transferase 1-1.
FT                                /FTId=PRO_0000185950.
FT   DOMAIN        1     81       GST N-terminal.
FT   DOMAIN       87    209       GST C-terminal.
FT   REGION       51     53       Glutathione binding. {ECO:0000250}.
FT   REGION       65     67       Glutathione binding. {ECO:0000250}.
FT   BINDING      10     10       Glutathione. {ECO:0000250}.
FT   CONFLICT    195    195       E -> S (in Ref. 2; M84578).
FT                                {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
//
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