GST_ANOGA
ID GST_ANOGA Reviewed; 203 AA.
AC P46428; Q7PGA2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 4.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Glutathione S-transferase;
DE EC=2.5.1.18;
DE AltName: Full=GST class-sigma;
GN Name=GstS1; ORFNames=AGAP010404;
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 [MRNA] (ISOFORM B).
RC STRAIN=G3;
RX PubMed=9087540; DOI=10.1111/j.1365-2583.1993.tb00122.x;
RA Reiss R.A., James A.A.;
RT "A glutathione S-transferase gene of the vector mosquito, Anopheles
RT gambiae.";
RL Insect Mol. Biol. 2:25-32(1993).
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 -!- 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=P46428-1; Sequence=Displayed;
CC Name=B;
CC IsoId=P46428-2; Sequence=VSP_029900;
CC -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA29358.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=EAA45010.4; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; L07880; AAA29358.1; ALT_INIT; mRNA.
DR EMBL; AAAB01008849; EAA45010.4; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_311546.4; XM_311546.4.
DR AlphaFoldDB; P46428; -.
DR SMR; P46428; -.
DR STRING; 7165.AGAP010404-PA; -.
DR GeneID; 1272645; -.
DR KEGG; aga:AgaP_AGAP010404; -.
DR CTD; 1272645; -.
DR VEuPathDB; VectorBase:AGAP010404; -.
DR eggNOG; KOG1695; Eukaryota.
DR HOGENOM; CLU_039475_1_0_1; -.
DR InParanoid; P46428; -.
DR OrthoDB; 1162336at2759; -.
DR Proteomes; UP000007062; Chromosome 3L.
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; PF14497; GST_C_3; 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 Alternative splicing; Reference proteome; Transferase.
FT CHAIN 1..203
FT /note="Glutathione S-transferase"
FT /id="PRO_0000185915"
FT DOMAIN 2..79
FT /note="GST N-terminal"
FT DOMAIN 81..203
FT /note="GST C-terminal"
FT BINDING 8
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 39
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 43
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:P46088"
FT BINDING 49..51
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT BINDING 63..64
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250|UniProtKB:O60760"
FT VAR_SEQ 60..95
FT /note="KVHQSVAMSRYLANQVGLAGADDWENLMIDTVVDTV -> RVHQSLAMCRYV
FT AKQINLAGDNPLEALQIDAIVDTI (in isoform B)"
FT /evidence="ECO:0000303|PubMed:9087540"
FT /id="VSP_029900"
FT CONFLICT 49
FT /note="G -> R (in Ref. 1; AAA29358)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 23246 MW; 99EF5E78AA1A7595 CRC64;
MPDYKVYYFN VKALGEPLRF LLSYGNLPFD DVRITREEWP ALKPTMPMGQ MPVLEVDGKK
VHQSVAMSRY LANQVGLAGA DDWENLMIDT VVDTVNDFRL KIAIVAYEPD DMVKEKKMVT
LNNEVIPFYL TKLNVIAKEN NGHLVLGKPT WADVYFAGIL DYLNYLTKTN LLENFPNLQE
VVQKVLDNEN VKAYIAKRPI TEV
