GSTD1_DROME
ID GSTD1_DROME Reviewed; 209 AA.
AC P20432; Q4JFI6; Q8MR98; Q9TX88; Q9VG99;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Glutathione S-transferase D1 {ECO:0000303|PubMed:20417639, ECO:0000303|PubMed:22082028};
DE EC=2.5.1.18 {ECO:0000269|PubMed:20417639, ECO:0000269|PubMed:22082028};
DE EC=4.5.1.1 {ECO:0000269|PubMed:20417639};
DE AltName: Full=DDT-dehydrochlorinase {ECO:0000303|PubMed:20417639};
GN Name=GstD1 {ECO:0000312|FlyBase:FBgn0001149};
GN Synonyms=GST, Gst1, GSTD1-1 {ECO:0000312|FlyBase:FBgn0001149};
GN ORFNames=CG10045 {ECO:0000312|FlyBase:FBgn0001149};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 1-20.
RC STRAIN=Oregon-R;
RX PubMed=2296588; DOI=10.1073/pnas.87.1.31;
RA Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.;
RT "Drosophila glutathione S-transferase 1-1 shares a region of sequence
RT homology with the maize glutathione S-transferase III.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:31-35(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=1872839; DOI=10.1016/0006-291x(91)91021-4;
RA Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.;
RT "The Drosophila glutathione S-transferase 1-1 is encoded by an intronless
RT gene at 87B.";
RL Biochem. Biophys. Res. Commun. 178:1205-1211(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7683659; DOI=10.1016/s0021-9258(18)98410-3;
RA Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.;
RT "The glutathione S-transferase D genes. A divergently organized, intronless
RT gene family in Drosophila melanogaster.";
RL J. Biol. Chem. 268:9737-9746(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22082028; DOI=10.1042/bj20111747;
RA Saisawang C., Wongsantichon J., Ketterman A.J.;
RT "A preliminary characterization of the cytosolic glutathione transferase
RT proteome from Drosophila melanogaster.";
RL Biochem. J. 442:181-190(2012).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.13 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=20417639; DOI=10.1016/j.jmb.2010.04.020;
RA Low W.Y., Feil S.C., Ng H.L., Gorman M.A., Morton C.J., Pyke J.,
RA McConville M.J., Bieri M., Mok Y.F., Robin C., Gooley P.R., Parker M.W.,
RA Batterham P.;
RT "Recognition and detoxification of the insecticide DDT by Drosophila
RT melanogaster glutathione S-transferase D1.";
RL J. Mol. Biol. 399:358-366(2010).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles (PubMed:22082028,
CC PubMed:20417639). Has DDT dehydrochlorinase activity (PubMed:20417639).
CC May be involved in detoxification (PubMed:22082028).
CC {ECO:0000269|PubMed:20417639, ECO:0000269|PubMed:22082028}.
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:20417639, ECO:0000269|PubMed:22082028};
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:20417639};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 mM for glutathione {ECO:0000269|PubMed:22082028};
CC KM=0.45 mM for 1-chloro-2,4-dinitrobenzene
CC {ECO:0000269|PubMed:22082028};
CC Vmax=84.2 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as
CC substrate {ECO:0000269|PubMed:22082028};
CC Vmax=7.51 umol/min/mg enzyme with 4-hydroxy-2-nonenal as substrate
CC {ECO:0000269|PubMed:22082028};
CC Vmax=77 nmol/min/mg enzyme with adrenochrome as substrate
CC {ECO:0000269|PubMed:22082028};
CC Vmax=0.33 umol/min/mg enzyme with phenethyl isothiocyanate as
CC substrate {ECO:0000269|PubMed:22082028};
CC Vmax=0.517 umol/min/mg enzyme with prostaglandin A2 as substrate
CC {ECO:0000269|PubMed:22082028};
CC Vmax=0.012 umol/min/mg enzyme with 5-hydroperoxyeicosatetraenoic acid
CC as substrate {ECO:0000269|PubMed:22082028};
CC Vmax=0.22 umol/min/mg enzyme with 2-hydroxyethyl disulfide as
CC substrate {ECO:0000269|PubMed:22082028};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20417639}.
CC -!- INTERACTION:
CC P20432; Q9VGA1: GstD10; NbExp=4; IntAct=EBI-97726, EBI-149969;
CC P20432; Q9VG92: GstD8; NbExp=4; IntAct=EBI-97726, EBI-15116229;
CC -!- MISCELLANEOUS: Has a specific activity toward 1-chloro-2,4-
CC dinitrobenzene comparable to that for the mammalian glutathione S-
CC transferases but did not have as broad a substrate specificity pattern.
CC Has no GSH peroxidase activity.
CC -!- SIMILARITY: Belongs to the GST superfamily. Delta family.
CC {ECO:0000303|PubMed:22082028}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM52032.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X14233; CAA32449.1; -; mRNA.
DR EMBL; S51044; AAA04220.1; -; mRNA.
DR EMBL; M97702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE014297; AAF54786.1; -; Genomic_DNA.
DR EMBL; AE014297; ABC66168.1; -; Genomic_DNA.
DR EMBL; AY121705; AAM52032.1; ALT_INIT; mRNA.
DR PIR; A34798; XUFF11.
DR RefSeq; NP_001034042.1; NM_001038953.2.
DR RefSeq; NP_524326.1; NM_079602.5.
DR PDB; 3EIN; X-ray; 1.13 A; A=1-209.
DR PDB; 3MAK; X-ray; 1.80 A; A=1-209.
DR PDBsum; 3EIN; -.
DR PDBsum; 3MAK; -.
DR AlphaFoldDB; P20432; -.
DR SMR; P20432; -.
DR BioGRID; 66612; 15.
DR DIP; DIP-17237N; -.
DR IntAct; P20432; 10.
DR STRING; 7227.FBpp0099824; -.
DR PaxDb; P20432; -.
DR PRIDE; P20432; -.
DR DNASU; 41503; -.
DR EnsemblMetazoa; FBtr0082607; FBpp0082077; FBgn0001149.
DR EnsemblMetazoa; FBtr0100410; FBpp0099824; FBgn0001149.
DR GeneID; 41503; -.
DR KEGG; dme:Dmel_CG10045; -.
DR CTD; 41503; -.
DR FlyBase; FBgn0001149; GstD1.
DR VEuPathDB; VectorBase:FBgn0001149; -.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00940000164816; -.
DR HOGENOM; CLU_011226_2_1_1; -.
DR InParanoid; P20432; -.
DR OMA; KYEVLQW; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; P20432; -.
DR SABIO-RK; P20432; -.
DR BioGRID-ORCS; 41503; 0 hits in 1 CRISPR screen.
DR ChiTaRS; GstS1; fly.
DR EvolutionaryTrace; P20432; -.
DR GenomeRNAi; 41503; -.
DR PRO; PR:P20432; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0001149; Expressed in seminal fluid secreting gland and 43 other tissues.
DR Genevisible; P20432; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0018833; F:DDT-dehydrochlorinase activity; IDA:FlyBase.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:FlyBase.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:FlyBase.
DR GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
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; Detoxification; Direct protein sequencing; Lyase;
KW Reference proteome; Transferase.
FT CHAIN 1..209
FT /note="Glutathione S-transferase D1"
FT /id="PRO_0000185947"
FT DOMAIN 1..81
FT /note="GST N-terminal"
FT DOMAIN 87..208
FT /note="GST C-terminal"
FT BINDING 10
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:20417639"
FT BINDING 51..53
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT BINDING 65..67
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:3EIN"
FT HELIX 11..23
FT /evidence="ECO:0007829|PDB:3EIN"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:3EIN"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:3EIN"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:3EIN"
FT HELIX 42..45
FT /evidence="ECO:0007829|PDB:3EIN"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:3EIN"
FT STRAND 61..64
FT /evidence="ECO:0007829|PDB:3EIN"
FT HELIX 66..77
FT /evidence="ECO:0007829|PDB:3EIN"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:3EIN"
FT HELIX 88..103
FT /evidence="ECO:0007829|PDB:3EIN"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:3EIN"
FT HELIX 125..141
FT /evidence="ECO:0007829|PDB:3EIN"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3EIN"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:3EIN"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:3EIN"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:3EIN"
FT HELIX 178..190
FT /evidence="ECO:0007829|PDB:3EIN"
FT HELIX 194..204
FT /evidence="ECO:0007829|PDB:3EIN"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:3EIN"
SQ SEQUENCE 209 AA; 23866 MW; 4AD8E237CCF804F2 CRC64;
MVDFYYLPGS SPCRSVIMTA KAVGVELNKK LLNLQAGEHL KPEFLKINPQ HTIPTLVDNG
FALWESRAIQ VYLVEKYGKT DSLYPKCPKK RAVINQRLYF DMGTLYQSFA NYYYPQVFAK
APADPEAFKK IEAAFEFLNT FLEGQDYAAG DSLTVADIAL VATVSTFEVA KFEISKYANV
NRWYENAKKV TPGWEENWAG CLEFKKYFE
