ID C3V9V2_CHITE Unreviewed; 221 AA.
AC C3V9V2;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 45.
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};
GN Name=GSTu4 {ECO:0000313|EMBL:ACP27604.1};
OS Chironomus tentans (Midge) (Camptochironomus tentans).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Chironominae; Chironomus.
OX NCBI_TaxID=7153 {ECO:0000313|EMBL:ACP27604.1};
RN [1] {ECO:0000313|EMBL:ACP27604.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=19744561; DOI=10.1016/j.ibmb.2009.08.010;
RA Li X., Zhang X., Zhang J., Zhang X., Starkey S.R., Zhu K.Y.;
RT "Identification and characterization of eleven glutathione S-transferase
RT genes from the aquatic midge Chironomus tentans (Diptera: Chironomidae).";
RL Insect Biochem. Mol. Biol. 39:745-754(2009).
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; FJ851374; ACP27604.1; -; mRNA.
DR AlphaFoldDB; C3V9V2; -.
DR GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR CDD; cd03177; GST_C_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 Transferase {ECO:0000313|EMBL:ACP27604.1}.
FT DOMAIN 2..83
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
FT DOMAIN 90..221
FT /note="GST C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50405"
SQ SEQUENCE 221 AA; 25793 MW; AFC26D245E728E18 CRC64;
MSKPVFYYHP LSPPARSVVM VARENNIDIE LNVIDFVNGE HTSEYFTKIN PAQTIPALVD
GDVMICDSQA ICLYLIEKFA KDDYLYPKNN FLLRSVINER LFFNASFLFP RAYNIFYPVI
MQGKADVPQE RIDQIHRGYR VLETYLTKTK WIACNEQMTV ADLAIFAWME SMVQCFTTEK
YPKINAWLAE MRKLSYYEDA NKKGADVHIQ IFKNALEKNK K
//
