GSTD2_DROME
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 03-AUG-2022, entry version 149.
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=0.50 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; Q9VG98; -.
DR DNASU; 48335; -.
DR EnsemblMetazoa; FBtr0082569; FBpp0082041; FBgn0010038.
DR GeneID; 48335; -.
DR KEGG; dme:Dmel_CG4181; -.
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; FKMFAPE; -.
DR OrthoDB; 1231780at2759; -.
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 tissues.
DR ExpressionAtlas; Q9VG98; baseline and differential.
DR Genevisible; Q9VG98; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0004602; F:glutathione peroxidase activity; TAS:FlyBase.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:FlyBase.
DR GO; GO:0006749; P:glutathione metabolic process; IDA:FlyBase.
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; 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
