ID   GSTD2_DROME             Reviewed;         215 AA.
AC   Q9VG98; Q9TX91;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Glutathione S-transferase D2 {ECO:0000303|PubMed:22082028};
DE            EC=2.5.1.18 {ECO:0000269|PubMed:22082028};
GN   Name=GstD2 {ECO:0000312|FlyBase:FBgn0010038};
GN   Synonyms=GSTD2-2, gstD21 {ECO:0000312|FlyBase:FBgn0010038};
GN   ORFNames=CG4181 {ECO:0000312|FlyBase:FBgn0010038};
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   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=1.84 mM for glutathione {ECO:0000269|PubMed:22082028};
CC         KM=0.81 mM for 1-chloro-2,4-dinitrobenzene
CC         {ECO:0000269|PubMed:22082028};
CC         Vmax=0.53 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as
CC         substrate {ECO:0000269|PubMed:22082028};
CC         Vmax=0.5 umol/min/mg enzyme with 4-hydroxy-2-nonenal as substrate
CC         {ECO:0000269|PubMed:22082028};
CC         Vmax=0.013 umol/min/mg enzyme with phenethyl isothiocyanate as
CC         substrate {ECO:0000269|PubMed:22082028};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P30711}.
CC   -!- INTERACTION:
CC       Q9VG98; Q9VG92: GstD8; NbExp=4; IntAct=EBI-15126376, EBI-15116229;
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; AAF54787.1; -; Genomic_DNA.
DR   PIR; D46681; D46681.
DR   RefSeq; NP_524912.1; NM_080173.2.
DR   PDB; 5F0G; X-ray; 1.60 A; A/B=1-215.
DR   PDBsum; 5F0G; -.
DR   AlphaFoldDB; Q9VG98; -.
DR   SMR; Q9VG98; -.
DR   BioGRID; 71332; 7.
DR   IntAct; Q9VG98; 4.
DR   STRING; 7227.FBpp0082041; -.
DR   PaxDb; 7227-FBpp0082041; -.
DR   DNASU; 48335; -.
DR   EnsemblMetazoa; FBtr0082569; FBpp0082041; FBgn0010038.
DR   GeneID; 48335; -.
DR   KEGG; dme:Dmel_CG4181; -.
DR   AGR; FB:FBgn0010038; -.
DR   CTD; 48335; -.
DR   FlyBase; FBgn0010038; GstD2.
DR   VEuPathDB; VectorBase:FBgn0010038; -.
DR   eggNOG; KOG0867; Eukaryota.
DR   GeneTree; ENSGT00940000164816; -.
DR   HOGENOM; CLU_011226_2_1_1; -.
DR   InParanoid; Q9VG98; -.
DR   OMA; RHEWHDI; -.
DR   OrthoDB; 2318861at2759; -.
DR   PhylomeDB; Q9VG98; -.
DR   BRENDA; 2.5.1.18; 1994.
DR   SABIO-RK; Q9VG98; -.
DR   BioGRID-ORCS; 48335; 0 hits in 1 CRISPR screen.
DR   ChiTaRS; GstS1; fly.
DR   GenomeRNAi; 48335; -.
DR   PRO; PR:Q9VG98; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0010038; Expressed in midgut and 23 other cell types or tissues.
DR   ExpressionAtlas; Q9VG98; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS: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; 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; Q9VG98; DM.
PE   1: Evidence at protein level;
KW   3D-structure; Detoxification; Reference proteome; Transferase.
FT   CHAIN           1..215
FT                   /note="Glutathione S-transferase D2"
FT                   /id="PRO_0000185954"
FT   DOMAIN          1..80
FT                   /note="GST N-terminal"
FT   DOMAIN          86..212
FT                   /note="GST C-terminal"
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   STRAND          2..5
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   HELIX           10..21
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   HELIX           33..35
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   HELIX           37..39
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   HELIX           41..46
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   STRAND          52..57
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   STRAND          60..64
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   HELIX           65..76
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   HELIX           87..102
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   HELIX           104..112
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   HELIX           124..140
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   TURN            141..143
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   STRAND          149..151
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   HELIX           154..168
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   HELIX           177..189
FT                   /evidence="ECO:0007829|PDB:5F0G"
FT   HELIX           193..211
FT                   /evidence="ECO:0007829|PDB:5F0G"
SQ   SEQUENCE   215 AA;  24535 MW;  221A9961BBF0E5B5 CRC64;
     MDFYYMPGGG GCRTVIMVAK ALGLELNKKL LNTMEGEQLK PEFVKLNPQH TIPTLVDNGF
     SIWESRAIAV YLVEKYGKDD YLLPNDPKKR AVINQRLYFD MGTLYESFAK YYYPLFRTGK
     PGSDEDLKRI ETAFGFLDTF LEGQEYVAGD QLTVADIAIL STVSTFEVSE FDFSKYSNVS
     RWYDNAKKVT PGWDENWEGL MAMKALFDAR KLAAK
//