GSTT1_MUSDO
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 03-AUG-2022, entry version 102.
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.XP_005180114.1; -.
DR VEuPathDB; VectorBase:MDOA006158; -.
DR eggNOG; KOG0867; Eukaryota.
DR Proteomes; UP000095301; Whole Genome Shotgun Assembly.
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 3D-structure; 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
