ID   GSTD3_DROME             Reviewed;         199 AA.
AC   Q9VG97; Q8MT68;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 153.
DE   RecName: Full=Inactive glutathione S-transferase D3 {ECO:0000303|PubMed:22082028};
GN   Name=GstD3 {ECO:0000312|FlyBase:FBgn0010039};
GN   Synonyms=gstD22, GSTD3-3 {ECO:0000312|FlyBase:FBgn0010039};
GN   ORFNames=CG4381 {ECO:0000312|FlyBase:FBgn0010039};
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=Larva, and Pupae;
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   [5]
RP   SEQUENCE REVISION.
RA   Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   LACK OF ENZYME ACTIVITY.
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: Has no glutathione S-transferase activity.
CC       {ECO:0000269|PubMed:22082028}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30711}.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Delta family.
CC       {ECO:0000303|PubMed:22082028}.
CC   -!- CAUTION: In vitro shows no activity towards glutathione. Lacks 16 amino
CC       acids at the N-terminus including a glutathione binding site known to
CC       be important for catalysis. {ECO:0000269|PubMed:22082028}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM48379.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M97702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AE014297; AAO41561.1; -; Genomic_DNA.
DR   EMBL; AY118350; AAM48379.3; ALT_INIT; mRNA.
DR   PIR; A46681; A46681.
DR   RefSeq; NP_788656.1; NM_176479.2.
DR   AlphaFoldDB; Q9VG97; -.
DR   SMR; Q9VG97; -.
DR   BioGRID; 71333; 2.
DR   IntAct; Q9VG97; 1.
DR   STRING; 7227.FBpp0082042; -.
DR   PaxDb; 7227-FBpp0082042; -.
DR   DNASU; 48336; -.
DR   EnsemblMetazoa; FBtr0082570; FBpp0082042; FBgn0010039.
DR   GeneID; 48336; -.
DR   KEGG; dme:Dmel_CG4381; -.
DR   AGR; FB:FBgn0010039; -.
DR   CTD; 48336; -.
DR   FlyBase; FBgn0010039; GstD3.
DR   VEuPathDB; VectorBase:FBgn0010039; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   GeneTree; ENSGT00940000164816; -.
DR   HOGENOM; CLU_011226_2_1_1; -.
DR   InParanoid; Q9VG97; -.
DR   OMA; EDGTCLW; -.
DR   OrthoDB; 2318861at2759; -.
DR   PhylomeDB; Q9VG97; -.
DR   BioGRID-ORCS; 48336; 0 hits in 1 CRISPR screen.
DR   GenomeRNAi; 48336; -.
DR   PRO; PR:Q9VG97; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0010039; Expressed in wing disc and 36 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0006749; P:glutathione metabolic process; IBA:GO_Central.
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; 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; PF13410; GST_C_2; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 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; Q9VG97; DM.
PE   2: Evidence at transcript level;
KW   Reference proteome.
FT   CHAIN           1..199
FT                   /note="Inactive glutathione S-transferase D3"
FT                   /id="PRO_0000185955"
FT   DOMAIN          1..64
FT                   /note="GST N-terminal"
FT   DOMAIN          70..199
FT                   /note="GST C-terminal"
FT   BINDING         34..36
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
FT   BINDING         48..50
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   199 AA;  22907 MW;  0B4D0EF24ADBBC60 CRC64;
     MVGKALGLEF NKKIINTLKG EQMNPDFIKI NPQHSIPTLV DNGFTIWESR AILVYLVEKY
     GKDDALYPKD IQKQAVINQR LYFDMALMYP TLANYYYKAF TTGQFGSEED YKKVQETFDF
     LNTFLEGQDY VAGDQYTVAD IAILANVSNF DVVGFDISKY PNVARWYDHV KKITPGWEEN
     WAGALDVKKR IEEKQNAAK
//