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   27-MAR-2024, entry version 186.
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; 16.
DR   DIP; DIP-17237N; -.
DR   IntAct; P20432; 10.
DR   STRING; 7227.FBpp0099824; -.
DR   GlyGen; P20432; 1 site, 1 O-linked glycan (1 site).
DR   PaxDb; 7227-FBpp0099824; -.
DR   DNASU; 41503; -.
DR   EnsemblMetazoa; FBtr0082607; FBpp0082077; FBgn0001149.
DR   EnsemblMetazoa; FBtr0100410; FBpp0099824; FBgn0001149.
DR   GeneID; 41503; -.
DR   KEGG; dme:Dmel_CG10045; -.
DR   AGR; FB:FBgn0001149; -.
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; RYTNEAR; -.
DR   OrthoDB; 2318861at2759; -.
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 cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0018833; F:DDT-dehydrochlorinase activity; IDA:FlyBase.
DR   GO; GO:0004602; F:glutathione peroxidase activity; IDA:FlyBase.
DR   GO; GO:0004364; F:glutathione transferase activity; IDA:FlyBase.
DR   GO; GO:0006749; P:glutathione metabolic process; IDA:FlyBase.
DR   CDD; cd03177; GST_C_Delta_Epsilon; 1.
DR   CDD; cd03045; GST_N_Delta_Epsilon; 1.
DR   Gene3D; 1.20.1050.10; -; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
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   PANTHER; PTHR43969; GLUTATHIONE S TRANSFERASE D10, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR43969:SF9; GLUTATHIONE S TRANSFERASE D10, ISOFORM A-RELATED; 1.
DR   Pfam; PF00043; GST_C; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SFLD; SFLDG01153; Main.4:_Theta-like; 1.
DR   SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
DR   Genevisible; P20432; DM.
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
//