GST1B_ANOGA
ID GST1B_ANOGA Reviewed; 216 AA.
AC O77473; Q7PH26;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Glutathione S-transferase 1, isoform B;
DE EC=2.5.1.18;
DE AltName: Full=AgGst1-alpha;
DE AltName: Full=Aggst1-4;
DE AltName: Full=GST class-theta;
GN Name=GstD1 {ECO:0000303|PubMed:9826692};
GN Synonyms=GST1a {ECO:0000312|EMBL:AAC79994.1}; ORFNames=AGAP004164;
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:0000305, ECO:0000312|EMBL:AAC79998.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RC STRAIN=ZAN/U {ECO:0000312|EMBL:AAC79998.1};
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).
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:P30711};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30711}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=B {ECO:0000269|PubMed:9826692}; Synonyms=1-4
CC {ECO:0000269|PubMed:9826692};
CC IsoId=O77473-1; Sequence=Displayed;
CC Name=A {ECO:0000269|PubMed:9826692}; Synonyms=1-3
CC {ECO:0000269|PubMed:9826692};
CC IsoId=O77462-1; Sequence=External;
CC Name=C {ECO:0000269|PubMed:9826692}; Synonyms=1-5
CC {ECO:0000269|PubMed:9826692};
CC IsoId=Q93112-1; Sequence=External;
CC Name=D {ECO:0000269|PubMed:9826692}; Synonyms=1-1, 1-6
CC {ECO:0000269|PubMed:9826692}, 2-1;
CC IsoId=Q93113-1; Sequence=External;
CC -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC {ECO:0000255}.
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DR EMBL; AF071160; AAC79994.1; -; Genomic_DNA.
DR EMBL; AF071162; AAC79998.1; -; mRNA.
DR EMBL; AAAB01008880; EAA44711.1; -; Genomic_DNA.
DR RefSeq; XP_313048.1; XM_313048.4.
DR AlphaFoldDB; O77473; -.
DR SMR; O77473; -.
DR STRING; 7165.AGAP004164-PC; -.
DR PaxDb; O77473; -.
DR PRIDE; O77473; -.
DR GeneID; 1273988; -.
DR KEGG; aga:AgaP_AGAP004164; -.
DR CTD; 1273988; -.
DR VEuPathDB; VectorBase:AGAP004164; -.
DR eggNOG; KOG0867; Eukaryota.
DR InParanoid; O77473; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; O77473; -.
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; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF02798; GST_N; 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..216
FT /note="Glutathione S-transferase 1, isoform B"
FT /id="PRO_0000283093"
FT DOMAIN 1..80
FT /note="GST N-terminal"
FT DOMAIN 89..210
FT /note="GST C-terminal"
FT BINDING 9
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 50..52
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 64..66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT CONFLICT 58
FT /note="N -> S (in Ref. 1; AAC79994/AAC79998)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="T -> A (in Ref. 1; AAC79994/AAC79998)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24492 MW; 0E764BDFB98038D1 CRC64;
MDFYYLPGSA PCRAVQMTAA AVGVELNLKL TDLMKGEHMK PEFLKLNPQH CVPTLVDNGF
ALWESRAIMC YLVEKYGKPC NNDSLYPTDP QKRAIVNQRL YFDMGTLYQR FGDYYYPQIF
EGAPANETNF AKIGEALAFL DTFLEGERFV AGGNGYSLAD ISLYATLTTF EVAGYDFSAY
VNVLRWYKSM PELIPASDTN RSWAEAARPF FDKVKH
