ID GSTT3_MUSDO Reviewed; 210 AA. AC P46432; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 24-JAN-2024, entry version 101. DE RecName: Full=Glutathione S-transferase 3; DE EC=2.5.1.18; DE AltName: Full=GST class-theta; GN Name=Gst3; Synonyms=Gst-3; 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 [MRNA]. RC STRAIN=Cornell-R; RX PubMed=7845356; DOI=10.1007/bf00279747; RA Syvanen M., Zhou Z., Wang J.; RT "Glutathione transferase gene family from the housefly Musca domestica."; RL Mol. Gen. Genet. 245:25-31(1994). 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; X73575; CAA51977.1; -; mRNA. DR EMBL; X94279; CAA63944.1; -; Genomic_DNA. DR PIR; S51567; S51567. DR AlphaFoldDB; P46432; -. DR SMR; P46432; -. DR STRING; 7370.P46432; -. DR VEuPathDB; VectorBase:MDOA011215; -. 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; PF13417; GST_N_3; 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 2: Evidence at transcript level; KW Reference proteome; Transferase. FT CHAIN 1..210 FT /note="Glutathione S-transferase 3" FT /id="PRO_0000185967" FT DOMAIN 1..80 FT /note="GST N-terminal" FT DOMAIN 87..208 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 210 AA; 24343 MW; EC8ADA3F40AA3B2C CRC64; MDFYYLPLSA PCRSVIMTAK ALGIELNKKL LNLFEGEHLK PEFLKINPQH TIPTLVDNGF AMWESRAIMV YLVEKYGKQN DPLYPSCPKK RALINQRLYF DMGTLWKSYA DYTYPQFREN KPADPELFKK FESALEFLNI FLSQSKYAAG QTMTLADLAI LASVSTFDVV QMDLSKYEHI LRWYNMLKDT APGAAENWAG CLEMKKYFKK //