GSTT2_ANOGA
ID GSTT2_ANOGA Reviewed; 209 AA.
AC Q94999; Q7PH22;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Glutathione S-transferase 2;
DE EC=2.5.1.18;
DE AltName: Full=Aggst1-2;
DE AltName: Full=GST class-theta;
GN Name=GstD2; Synonyms=GST1-2; ORFNames=AGAP004165;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=Suakoko;
RX PubMed=9038148; DOI=10.1074/jbc.272.9.5464;
RA Ranson H., Cornel A.J., Fournier D., Vaughan A., Collins F.H.,
RA Hemingway J.;
RT "Cloning and localization of a glutathione S-transferase class I gene from
RT Anopheles gambiae.";
RL J. Biol. Chem. 272:5464-5468(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000269|PubMed:9038148}.
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}.
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DR EMBL; Z71480; CAA96104.1; -; Genomic_DNA.
DR EMBL; AAAB01008880; EAA44715.1; -; Genomic_DNA.
DR RefSeq; XP_313052.1; XM_313052.1.
DR AlphaFoldDB; Q94999; -.
DR SMR; Q94999; -.
DR STRING; 7165.AGAP004165-PA; -.
DR PaxDb; Q94999; -.
DR GeneID; 1273989; -.
DR KEGG; aga:AgaP_AGAP004165; -.
DR CTD; 1273989; -.
DR VEuPathDB; VectorBase:AGAP004165; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_2_1_1; -.
DR InParanoid; Q94999; -.
DR OMA; FFDACVL; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q94999; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0004364; F:glutathione transferase activity; IBA:GO_Central.
DR GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
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; PF13417; GST_N_3; 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 3: Inferred from homology;
KW Reference proteome; Transferase.
FT CHAIN 1..209
FT /note="Glutathione S-transferase 2"
FT /id="PRO_0000185960"
FT DOMAIN 1..81
FT /note="GST N-terminal"
FT DOMAIN 88..209
FT /note="GST C-terminal"
FT BINDING 10
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 51..53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 65..67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT CONFLICT 62
FT /note="I -> V (in Ref. 1; CAA96104)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 209 AA; 23543 MW; 875B863BE805A8D3 CRC64;
MLDFYYLPGS APCRAVQMVA EAVHVKLNLK YLDLMAGAHR SPQFTKLNPQ RTIPTLVDGS
LILSESRAAL IYLCDQYGDE DNDWYPRDTI QRAIVNQRLF FDACVLYPRF ADFYHPQVFG
NAAPDGRKRL AFEKAVELLN IFLSEHEFVA GSKMTIADIS LFATLATACT LGFILRPYVH
VDRWYVTMVA SCPGAQANVS GAKEFLTYK
