ID   GSTD4_DROME             Reviewed;         215 AA.
AC   Q9VG96; Q541F8; Q9TX90;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=Glutathione S-transferase D4 {ECO:0000303|PubMed:22082028};
DE            EC=2.5.1.18 {ECO:0000269|PubMed:22082028};
GN   Name=GstD4 {ECO:0000312|FlyBase:FBgn0010040};
GN   Synonyms=gstD23, GSTD4-4 {ECO:0000312|FlyBase:FBgn0010040};
GN   ORFNames=CG11512 {ECO:0000312|FlyBase:FBgn0010040};
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 [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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley; TISSUE=Embryo;
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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).
CC   -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC       exogenous and endogenous hydrophobic electrophiles (PubMed:22082028).
CC       May be involved in detoxification (PubMed:22082028).
CC       {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:22082028};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.47 mM for glutathione {ECO:0000269|PubMed:22082028};
CC         KM=2.04 mM for 1-chloro-2,4-dinitrobenzene
CC         {ECO:0000269|PubMed:22082028};
CC         Vmax=0.26 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as
CC         substrate {ECO:0000269|PubMed:22082028};
CC         Vmax=1.45 umol/min/mg enzyme with 4-hydroxy-2-nonenal as substrate
CC         {ECO:0000269|PubMed:22082028};
CC         Vmax=99.5 nmol/min/mg enzyme with adrenochrome as substrate
CC         {ECO:0000269|PubMed:22082028};
CC         Vmax=0.044 umol/min/mg enzyme with phenethyl isothiocyanate as
CC         substrate {ECO:0000269|PubMed:22082028};
CC         Vmax=0.047 umol/min/mg enzyme with 2-hydroxyethyl disulfide as
CC         substrate {ECO:0000269|PubMed:22082028};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30711}.
CC   -!- INTERACTION:
CC       Q9VG96; Q9VG94: GstD6; NbExp=3; IntAct=EBI-117276, EBI-152218;
CC   -!- SIMILARITY: Belongs to the GST superfamily. Delta family.
CC       {ECO:0000303|PubMed:22082028}.
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DR   EMBL; M97702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AE014297; AAF54789.1; -; Genomic_DNA.
DR   EMBL; AY071648; AAL49270.1; -; mRNA.
DR   PIR; E46681; E46681.
DR   RefSeq; NP_524913.1; NM_080174.4.
DR   AlphaFoldDB; Q9VG96; -.
DR   SMR; Q9VG96; -.
DR   BioGRID; 71334; 9.
DR   DIP; DIP-19902N; -.
DR   IntAct; Q9VG96; 5.
DR   STRING; 7227.FBpp0082043; -.
DR   PaxDb; 7227-FBpp0082043; -.
DR   EnsemblMetazoa; FBtr0082571; FBpp0082043; FBgn0010040.
DR   GeneID; 48337; -.
DR   KEGG; dme:Dmel_CG11512; -.
DR   AGR; FB:FBgn0010040; -.
DR   CTD; 48337; -.
DR   FlyBase; FBgn0010040; GstD4.
DR   VEuPathDB; VectorBase:FBgn0010040; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   GeneTree; ENSGT00940000164816; -.
DR   HOGENOM; CLU_011226_2_1_1; -.
DR   InParanoid; Q9VG96; -.
DR   OMA; GWSENQE; -.
DR   OrthoDB; 2318861at2759; -.
DR   PhylomeDB; Q9VG96; -.
DR   SABIO-RK; Q9VG96; -.
DR   BioGRID-ORCS; 48337; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 48337; -.
DR   PRO; PR:Q9VG96; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0010040; Expressed in midgut and 10 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS: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   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; 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; SFLDG01153; Main.4:_Theta-like; 1.
DR   SFLD; SFLDG00358; Main_(cytGST); 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; Q9VG96; DM.
PE   1: Evidence at protein level;
KW   Detoxification; Reference proteome; Transferase.
FT   CHAIN           1..215
FT                   /note="Glutathione S-transferase D4"
FT                   /id="PRO_0000185956"
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                   /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        142
FT                   /note="E -> V (in Ref. 1; M97702)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   215 AA;  24736 MW;  9556E0A1A54BBE1F CRC64;
     MDFYYSPRSS GSRTIIMVAK ALGLELNKKQ LRITEGEHLK PEFLKLNPQH TIPTLVDNGF
     AIWESRAIAV YLVEKYGKDD SLFPNDPQKR ALINQRLYFD MGTLHDSFMK YYYPFIRTGQ
     LGNAENYKKV EAAFEFLDIF LEGQDYVAGS QLTVADIAIL SSVSTFEVVE FDISKYPNVA
     RWYANAKKIT PGWDENWKGL LQMKTMYEAQ KASLK
//