ID   M9Z5L9_ANOGA            Unreviewed;       218 AA.
AC   M9Z5L9;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=glutathione transferase {ECO:0000256|ARBA:ARBA00012452};
DE            EC=2.5.1.18 {ECO:0000256|ARBA:ARBA00012452};
DE   AltName: Full=GST class-theta {ECO:0000256|ARBA:ARBA00041523};
DE   Flags: Fragment;
GN   Name=GSTe2 {ECO:0000313|EMBL:AGK30028.1};
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165 {ECO:0000313|EMBL:AGK30028.1};
RN   [1] {ECO:0000313|EMBL:AGK30028.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=402 {ECO:0000313|EMBL:AGK30028.1};
RA   Mitchell S.N., Rigden D.J., Dowd A.J., Wilding C.S., Weetman D.,
RA   Jenkins A., Regna K., Muskavitch M., Ranson H., Paine M.J.I., Mayans O.,
RA   Donnelly M.J.;
RT   "Allelic variation in Glutathione-S-Transferase E2 is associated with DDT
RT   resistance in the malaria vector Anopheles gambiae s.s.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00000710};
CC   -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC       {ECO:0000256|ARBA:ARBA00009899}.
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DR   EMBL; KC533014; AGK30028.1; -; Genomic_DNA.
DR   VEuPathDB; VectorBase:AGAP009195; -.
DR   HOGENOM; CLU_011226_2_1_1; -.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   PANTHER; PTHR43969:SF4; FI01423P-RELATED; 1.
DR   PANTHER; PTHR43969; GLUTATHIONE S TRANSFERASE D10, ISOFORM A-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF13417; GST_N_3; 1.
DR   SFLD; SFLDG01153; Main.4:_Theta-like; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 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   3: Inferred from homology;
KW   Transferase {ECO:0000313|EMBL:AGK30028.1}.
FT   DOMAIN          1..81
FT                   /note="GST N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50404"
FT   DOMAIN          87..218
FT                   /note="GST C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS50405"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AGK30028.1"
FT   NON_TER         218
FT                   /evidence="ECO:0000313|EMBL:AGK30028.1"
SQ   SEQUENCE   218 AA;  24558 MW;  270ABBE4BC8BAF9F CRC64;
     NLVLYTLHLS PPCRAVELTA KALGLELEQK TINLLTGDHL KPEFVKLNPQ HTIPVLDDNG
     TIITESHAIM IYLVTKYGKD DSLYPKDPVK QARVNSALHF ESGVLFARMR FXFERILFFG
     KSDIPEDRVE YVQKSYELLE DTLVDDFVAG PTMTIADFSC ISTISSIMGV VPLEQSKHPR
     IYAWIDRLKQ LPYYEEANGG GGTDLGKFVL AKKEENAK
//