GSTD7_DROME
ID GSTD7_DROME Reviewed; 224 AA.
AC Q9VG93; Q4V3S1; Q9TX87;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Glutathione S-transferase D7 {ECO:0000303|PubMed:22082028};
DE EC=2.5.1.18 {ECO:0000269|PubMed:22082028};
GN Name=GstD7 {ECO:0000312|FlyBase:FBgn0010043};
GN Synonyms=gstD26, GSTD7-7 {ECO:0000312|FlyBase:FBgn0010043};
GN ORFNames=CG4371 {ECO:0000312|FlyBase:FBgn0010043};
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 PRELIMINARY 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;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAY-2005) 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=1.68 mM for glutathione {ECO:0000269|PubMed:22082028};
CC KM=1.16 mM for 1-chloro-2,4-dinitrobenzene
CC {ECO:0000269|PubMed:22082028};
CC Vmax=9.76 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as
CC substrate {ECO:0000269|PubMed:22082028};
CC Vmax=0.66 umol/min/mg enzyme with 4-hydroxy-2-nonenal as substrate
CC {ECO:0000269|PubMed:22082028};
CC Vmax=41.5 nmol/min/mg enzyme with adrenochrome as substrate
CC {ECO:0000269|PubMed:22082028};
CC Vmax=0.16 umol/min/mg enzyme with phenethyl isothiocyanate as
CC substrate {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 -!- SEQUENCE CAUTION:
CC Sequence=M97702; Type=Frameshift; 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; AAF54792.1; -; Genomic_DNA.
DR EMBL; BT023285; AAY55701.1; -; mRNA.
DR PIR; H46681; H46681.
DR RefSeq; NP_525114.1; NM_080375.3.
DR AlphaFoldDB; Q9VG93; -.
DR SMR; Q9VG93; -.
DR BioGRID; 71337; 5.
DR IntAct; Q9VG93; 11.
DR STRING; 7227.FBpp0082046; -.
DR PaxDb; Q9VG93; -.
DR DNASU; 48340; -.
DR EnsemblMetazoa; FBtr0082574; FBpp0082046; FBgn0010043.
DR GeneID; 48340; -.
DR KEGG; dme:Dmel_CG4371; -.
DR CTD; 48340; -.
DR FlyBase; FBgn0010043; GstD7.
DR VEuPathDB; VectorBase:FBgn0010043; -.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00940000164816; -.
DR HOGENOM; CLU_011226_2_1_1; -.
DR InParanoid; Q9VG93; -.
DR OMA; PGWEQNI; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q9VG93; -.
DR SABIO-RK; Q9VG93; -.
DR BioGRID-ORCS; 48340; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 48340; -.
DR PRO; PR:Q9VG93; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010043; Expressed in midgut and 15 other tissues.
DR Genevisible; Q9VG93; DM.
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 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 Detoxification; Reference proteome; Transferase.
FT CHAIN 1..224
FT /note="Glutathione S-transferase D7"
FT /id="PRO_0000185959"
FT DOMAIN 2..83
FT /note="GST N-terminal"
FT DOMAIN 90..210
FT /note="GST C-terminal"
FT BINDING 53..55
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 67..69
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
SQ SEQUENCE 224 AA; 25419 MW; D4478B93C59E565A CRC64;
MPNLDLYNFP MAPASRAIQM VAKALGLELN SKLINTMEGD QLKPEFVRIN PQHTIPTLVD
NGFVIWESRA IAVYLVEKYG KPDSPLYPND PQKRALINQR LYFDMGTLYD ALTKYFFLIF
RTGKFGDQEA LDKVNSAFGF LNTFLEGQDF VAGSQLTVAD IVILATVSTV EWFSFDLSKF
PNVERWLKNA PKVTPGWEQN LESLQQGKKF LQDLQAAKEK EVKA
