ID GSTT1_MUSDO Reviewed; 208 AA. AC P28338; DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 1. DT 24-JAN-2024, entry version 108. DE RecName: Full=Glutathione S-transferase 1; DE EC=2.5.1.18; DE AltName: Full=GST class-theta; GN Name=Gst1; Synonyms=Gst-1; OS Musca domestica (House fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Muscoidea; OC Muscidae; Musca. OX NCBI_TaxID=7370; RN [1] RP NUCLEOTIDE SEQUENCE. RX PubMed=2062307; DOI=10.1007/bf00259679; RA Wang J., McCommas S., Syvanen M.; RT "Molecular cloning of a glutathione S-transferase overproduced in an RT insecticide-resistant strain of the housefly (Musca domestica)."; RL Mol. Gen. Genet. 227:260-266(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1730722; DOI=10.1016/s0021-9258(18)46023-1; RA Fournier D., Bride J.-M., Poirie M., Berge J.-B., Plapp F.W.; RT "Insect glutathione S-transferases. Biochemical characteristics of the RT major forms from houseflies susceptible and resistant to insecticides."; RL J. Biol. Chem. 267:1840-1845(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1648169; DOI=10.1007/bf00259680; RA Britt A.B., Walbot V.; RT "Germinal and somatic products of Mu1 excision from the Bronze-1 gene of RT Zea mays."; RL Mol. Gen. Genet. 227:267-276(1991). 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. {ECO:0000250}. 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; X61302; CAA43599.1; -; Genomic_DNA. DR EMBL; M83249; AAA29294.1; -; mRNA. DR PIR; A42045; A42045. DR PDB; 5ZWP; X-ray; 1.40 A; A/B=1-208. DR PDBsum; 5ZWP; -. DR AlphaFoldDB; P28338; -. DR SMR; P28338; -. DR STRING; 7370.P28338; -. DR VEuPathDB; VectorBase:MDOA006158; -. DR eggNOG; KOG0867; Eukaryota. DR Proteomes; UP000095301; Unassembled WGS sequence. DR Proteomes; UP000694905; Genome assembly. 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 3D-structure; Reference proteome; Transferase. FT CHAIN 1..208 FT /note="Glutathione S-transferase 1" FT /id="PRO_0000185965" 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" FT STRAND 2..5 FT /evidence="ECO:0007829|PDB:5ZWP" FT HELIX 10..21 FT /evidence="ECO:0007829|PDB:5ZWP" FT STRAND 27..30 FT /evidence="ECO:0007829|PDB:5ZWP" FT TURN 33..36 FT /evidence="ECO:0007829|PDB:5ZWP" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:5ZWP" FT HELIX 41..46 FT /evidence="ECO:0007829|PDB:5ZWP" FT STRAND 54..57 FT /evidence="ECO:0007829|PDB:5ZWP" FT STRAND 60..64 FT /evidence="ECO:0007829|PDB:5ZWP" FT HELIX 65..76 FT /evidence="ECO:0007829|PDB:5ZWP" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:5ZWP" FT HELIX 87..102 FT /evidence="ECO:0007829|PDB:5ZWP" FT HELIX 104..118 FT /evidence="ECO:0007829|PDB:5ZWP" FT HELIX 124..140 FT /evidence="ECO:0007829|PDB:5ZWP" FT TURN 141..143 FT /evidence="ECO:0007829|PDB:5ZWP" FT STRAND 149..151 FT /evidence="ECO:0007829|PDB:5ZWP" FT HELIX 154..168 FT /evidence="ECO:0007829|PDB:5ZWP" FT HELIX 173..175 FT /evidence="ECO:0007829|PDB:5ZWP" FT HELIX 177..189 FT /evidence="ECO:0007829|PDB:5ZWP" FT HELIX 193..204 FT /evidence="ECO:0007829|PDB:5ZWP" SQ SEQUENCE 208 AA; 23651 MW; 9CB1649F1184EE25 CRC64; MDFYYLPGSA PCRSVLMTAK ALGIELNKKL LNLQAGEHLK PEFLKINPQH TIPTLVDGDF ALWESRAIMV YLVEKYGKTD SLFPKCPKKR AVINQRLYFD MGTLYKSFAD YYYPQIFAKA PADPELFKKI ETAFDFLNTF LKGHEYAAGD SLTVADLALL ASVSTFEVAS FDFSKYPNVA KWYANLKTVA PGWEENWAGC LEFKKYFG //