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 24-JAN-2024, entry version 90. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 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 //