GSTT7_ANOGA
ID GSTT7_ANOGA Reviewed; 218 AA.
AC O76483; A0NDD6; Q7QB62; Q8WQM2;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Glutathione S-transferase D7;
DE EC=2.5.1.18;
DE AltName: Full=Aggst1-7;
DE AltName: Full=GST class-theta;
DE AltName: Full=Gst1-beta;
GN Name=GstD7 {ECO:0000303|PubMed:9826692};
GN Synonyms=GST1-7 {ECO:0000312|EMBL:AAC79997.1}; ORFNames=AGAP004163;
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] {ECO:0000312|EMBL:AAC79997.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ZAN/U {ECO:0000312|EMBL:AAC79997.1};
RX PubMed=9826692; DOI=10.1073/pnas.95.24.14284;
RA Ranson H., Collins F.H., Hemingway J.;
RT "The role of alternative mRNA splicing in generating heterogeneity within
RT the Anopheles gambiae class I glutathione S-transferase family.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:14284-14289(1998).
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).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAL59657.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RC STRAIN=Zands {ECO:0000312|EMBL:AAL59657.1};
RA Ortelli F., Hemingway J.;
RT "Analysis of a GST promoter in the malaria mosquito Anopheles gambiae.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles.
CC {ECO:0000250|UniProtKB:P30711}.
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:0000250|UniProtKB:Q93113};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30711}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC {ECO:0000250|UniProtKB:Q93113}.
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DR EMBL; AF071161; AAC79997.1; -; mRNA.
DR EMBL; AAAB01008880; EAL40657.3; -; Genomic_DNA.
DR EMBL; AY063775; AAL59657.1; -; Genomic_DNA.
DR RefSeq; XP_562676.3; XM_562676.3.
DR AlphaFoldDB; O76483; -.
DR SMR; O76483; -.
DR STRING; 7165.AGAP004163-PB; -.
DR PaxDb; O76483; -.
DR GeneID; 1273987; -.
DR KEGG; aga:AgaP_AGAP004163; -.
DR CTD; 1273987; -.
DR VEuPathDB; VectorBase:AGAP004163; -.
DR eggNOG; KOG0867; Eukaryota.
DR HOGENOM; CLU_011226_2_1_1; -.
DR InParanoid; O76483; -.
DR OMA; TCLWESN; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; O76483; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; ISS:UniProtKB.
DR GO; GO:0006749; P:glutathione metabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Reference proteome; Transferase.
FT CHAIN 1..218
FT /note="Glutathione S-transferase D7"
FT /id="PRO_0000284749"
FT DOMAIN 1..82
FT /note="GST N-terminal"
FT DOMAIN 88..207
FT /note="GST C-terminal"
FT BINDING 11
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 52..54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 66..68
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
SQ SEQUENCE 218 AA; 24998 MW; 60060000B2ED836C CRC64;
MTPVLYYLPP SPPCRSVLLL AKMIGVELEL KALNVMEGEQ LKPDFVELNP QHCIPTLDDH
GLVLWESRVI LAYLVSAYGK DENLYPKDFR SRAIVDQRLH FDLGTLYQRV VDYYFPTIQL
GAHLDQTKKA KLAEALGWFE AMLKQYQWSA ANHFTIADIA LCVTVSQIEA FQFDLHPYPR
VRAWLQKCKD ELQGHGYKEI NETGAETLAG LFRSKLKQ
