ID   GSTT1_LUCCU             Reviewed;         208 AA.
AC   P42860;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Glutathione S-transferase 1-1;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-theta;
GN   Name=GST1;
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=LS-2;
RX   PubMed=8172603; DOI=10.1042/bj2990425;
RA   Board P.G., Russell R., Marano R., Oakeshott J.G.;
RT   "Purification, molecular cloning and heterologous expression of a
RT   glutathione S-transferase from the Australian sheep blowfly (Lucilia
RT   cuprina).";
RL   Biochem. J. 299:425-430(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SEQUENCE REVISION TO 10-13.
RX   PubMed=7774571; DOI=10.1002/j.1460-2075.1995.tb07207.x;
RA   Wilce M.J.C., Board P.G., Feil S.C., Parker M.W.;
RT   "Crystal structure of a theta-class glutathione transferase.";
RL   EMBO J. 14:2133-2143(1995).
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; L23126; AAA29287.1; -; mRNA.
DR   PIR; S43851; S43851.
DR   AlphaFoldDB; P42860; -.
DR   SMR; P42860; -.
DR   BRENDA; 2.5.1.18; 3079.
DR   SABIO-RK; P42860; -.
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   1: Evidence at protein level;
KW   Transferase.
FT   CHAIN           1..208
FT                   /note="Glutathione S-transferase 1-1"
FT                   /id="PRO_0000185963"
FT   DOMAIN          1..80
FT                   /note="GST N-terminal"
FT   DOMAIN          86..207
FT                   /note="GST C-terminal"
FT   BINDING         9
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         50..52
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         64..66
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   208 AA;  23644 MW;  89E274EA07F07CE5 CRC64;
     MDFYYLPGSA PCRSVLMTAK ALGIELNKKL LNLQAGEHLK PEFLKINPQH TIPTLVDGDF
     ALWESRAIMV YLVEKYGKND SLFPKCPKKR AVINQRLYFD MGTLYKSFAD YYYPQIFAKA
     PADPELYKKM EAAFDFLNTF LEGHQYVAGD SLTVADLALL ASVSTFEVAG FDFSKYANVA
     KWYANAKTVA PGFDENWEGC LEFKKFFN