ID Q9GN60_9DIPT Unreviewed; 219 AA.
AC Q9GN60;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 119.
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};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EMBL:AAG38506.1};
RN [1] {ECO:0000313|EMBL:AAG38506.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11439246; DOI=10.1016/S0965-1748(01)00032-7;
RA Jirajaroenrat K., Pongjaroenkit S., Krittanai C., Prapanthadara L.,
RA Ketterman A.J.;
RT "Heterologous expression and characterization of alternatively spliced
RT glutathione S-transferases from a single Anopheles gene.";
RL Insect Biochem. Mol. Biol. 31:867-875(2001).
RN [2] {ECO:0007829|PDB:3F63, ECO:0007829|PDB:3F6D}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH S-HEXYLGLUTATHIONE.
RX PubMed=20196771; DOI=10.1042/BJ20091939;
RA Wongsantichon J., Robinson R.C., Ketterman A.J.;
RT "Structural contributions of delta class glutathione transferase active-
RT site residues to catalysis.";
RL Biochem. J. 428:25-32(2010).
RN [3] {ECO:0007829|PDB:3G7I}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE.
RX PubMed=22475449; DOI=10.1016/j.abb.2012.03.023;
RA Wongsantichon J., Robinson R.C., Ketterman A.J.;
RT "Structural evidence for conformational changes of Delta class glutathione
RT transferases after ligand binding.";
RL Arch. Biochem. Biophys. 521:77-83(2012).
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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC {ECO:0000256|ARBA:ARBA00009899}.
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DR EMBL; AF273040; AAG38506.1; -; mRNA.
DR PDB; 3F63; X-ray; 1.80 A; A/B=1-219.
DR PDB; 3F6D; X-ray; 1.70 A; A/B=1-219.
DR PDB; 3G7I; X-ray; 2.05 A; A/B=1-219.
DR PDB; 3G7J; X-ray; 2.20 A; A/B=1-219.
DR PDBsum; 3F63; -.
DR PDBsum; 3F6D; -.
DR PDBsum; 3G7I; -.
DR PDBsum; 3G7J; -.
DR AlphaFoldDB; Q9GN60; -.
DR SMR; Q9GN60; -.
DR VEuPathDB; VectorBase:ADIR006123; -.
DR BRENDA; 2.5.1.18; 7177.
DR EvolutionaryTrace; Q9GN60; -.
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; 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; PF13410; GST_C_2; 1.
DR Pfam; PF02798; GST_N; 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 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:3F63, ECO:0007829|PDB:3F6D};
KW Transferase {ECO:0000313|EMBL:AAG38506.1}.
FT DOMAIN 1..81
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 92..219
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
FT BINDING 50
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0007829|PDB:3G7I"
FT BINDING 52
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0007829|PDB:3G7I"
FT BINDING 66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0007829|PDB:3G7I"
FT BINDING 67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0007829|PDB:3G7I"
SQ SEQUENCE 219 AA; 24975 MW; C4FF2DD1A0A7AFD8 CRC64;
MDFYYLPGSA PCRAVQMTAA AVGVELNLKL TNLMAGEHMK PEFLKLNPQH CIPTLVDEDG
FVLWESRAIQ IYLVEKYGAH DADLAERLYP SDPRRRAVVH QRLFFDVAVL YQRFAEYYYP
QIFGQKVPVG DPGRLRSMEQ ALEFLNTFLE GEQYVAGGDD PTIADLSILA TIATYEVAGY
DLRRYENVQR WYERTSAIVP GADKNVEGAK VFGRYFTQK
//
