GST1D_ANOGA
ID GST1D_ANOGA Reviewed; 209 AA.
AC Q93113; Q7PH24; Q94998;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Glutathione S-transferase 1, isoform D;
DE EC=2.5.1.18;
DE EC=4.5.1.1;
DE AltName: Full=AgGst1-alpha;
DE AltName: Full=Aggst1-1;
DE AltName: Full=Aggst1-6;
DE AltName: Full=Aggst2-1;
DE AltName: Full=DDT-dehydrochlorinase;
DE AltName: Full=GST class-theta;
GN Name=GstD1; Synonyms=GST1a; 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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=G3, and Zands; TISSUE=Larva;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=ZAN/U;
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 [3]
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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=Zands;
RX PubMed=9164846; DOI=10.1042/bj3240097;
RA Ranson H., Prapanthadara L., Hemingway J.;
RT "Cloning and characterization of two glutathione S-transferases from a DDT-
RT resistant strain of Anopheles gambiae.";
RL Biochem. J. 324:97-102(1997).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH S-HEXYLGLUTATHIONE
RP INHIBITOR, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=14646079; DOI=10.1107/s0907444903018493;
RA Chen L., Hall P.R., Zhou X.E., Ranson H., Hemingway J., Meehan E.J.;
RT "Structure of an insect delta-class glutathione S-transferase from a DDT-
RT resistant strain of the malaria vector Anopheles gambiae.";
RL Acta Crystallogr. D 59:2211-2217(2003).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Has DDT
CC dehydrochlorinase activity. {ECO:0000269|PubMed:9038148,
CC ECO:0000269|PubMed:9164846}.
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:0000269|PubMed:9164846};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-
CC 2,2-bis(4-chlorophenyl)ethylene + chloride + H(+);
CC Xref=Rhea:RHEA:19217, ChEBI:CHEBI:15378, ChEBI:CHEBI:16130,
CC ChEBI:CHEBI:16598, ChEBI:CHEBI:17996; EC=4.5.1.1;
CC Evidence={ECO:0000269|PubMed:9164846};
CC -!- ACTIVITY REGULATION: Inhibited by S-hexylglutathione.
CC {ECO:0000269|PubMed:14646079}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14646079}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=D; Synonyms=1-1, 1-6, 2-1;
CC IsoId=Q93113-1; Sequence=Displayed;
CC Name=A; Synonyms=1-3;
CC IsoId=O77462-1; Sequence=External;
CC Name=B; Synonyms=1-4;
CC IsoId=O77473-1; Sequence=External;
CC Name=C; Synonyms=1-5;
CC IsoId=Q93112-1; Sequence=External;
CC -!- DEVELOPMENTAL STAGE: Expressed in larvae. {ECO:0000269|PubMed:9038148}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Theta family.
CC {ECO:0000305}.
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DR EMBL; Z71481; CAA96105.1; -; mRNA.
DR EMBL; Z81292; CAB03593.1; -; mRNA.
DR EMBL; AF071160; AAC79995.1; -; Genomic_DNA.
DR EMBL; AAAB01008880; EAA44713.3; -; Genomic_DNA.
DR RefSeq; XP_313050.3; XM_313050.4.
DR PDB; 1PN9; X-ray; 2.00 A; A/B=1-209.
DR PDBsum; 1PN9; -.
DR AlphaFoldDB; Q93113; -.
DR SMR; Q93113; -.
DR GeneID; 1273988; -.
DR CTD; 1273988; -.
DR VEuPathDB; VectorBase:AGAP004164; -.
DR HOGENOM; CLU_011226_2_1_1; -.
DR OrthoDB; 1231780at2759; -.
DR BRENDA; 2.5.1.18; 358.
DR EvolutionaryTrace; Q93113; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0018833; F:DDT-dehydrochlorinase activity; IEA:UniProtKB-EC.
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; 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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Lyase; Reference proteome; Transferase.
FT CHAIN 1..209
FT /note="Glutathione S-transferase 1, isoform D"
FT /id="PRO_0000185962"
FT DOMAIN 1..80
FT /note="GST N-terminal"
FT DOMAIN 86..207
FT /note="GST C-terminal"
FT BINDING 9
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT BINDING 50..52
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT BINDING 64..66
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT CONFLICT 24
FT /note="V -> A (in Ref. 1; CAA96105)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:1PN9"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:1PN9"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:1PN9"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:1PN9"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1PN9"
FT HELIX 41..46
FT /evidence="ECO:0007829|PDB:1PN9"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:1PN9"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:1PN9"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:1PN9"
FT HELIX 87..102
FT /evidence="ECO:0007829|PDB:1PN9"
FT HELIX 104..118
FT /evidence="ECO:0007829|PDB:1PN9"
FT HELIX 124..140
FT /evidence="ECO:0007829|PDB:1PN9"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:1PN9"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:1PN9"
FT HELIX 154..169
FT /evidence="ECO:0007829|PDB:1PN9"
FT HELIX 177..189
FT /evidence="ECO:0007829|PDB:1PN9"
FT HELIX 193..207
FT /evidence="ECO:0007829|PDB:1PN9"
SQ SEQUENCE 209 AA; 23445 MW; 3B262EEE21FAA9D0 CRC64;
MDFYYLPGSA PCRAVQMTAA AVGVELNLKL TDLMKGEHMK PEFLKLNPQH CIPTLVDNGF
ALWESRAIQI YLAEKYGKDD KLYPKDPQKR AVVNQRLYFD MGTLYQRFAD YHYPQIFAKQ
PANPENEKKM KDAVGFLNTF LEGQEYAAGN DLTIADLSLA ATIATYEVAG FDFAPYPNVA
AWFARCKANA PGYALNQAGA DEFKAKFLS
