GSTD5_DROME
ID GSTD5_DROME Reviewed; 216 AA.
AC Q9VG95; Q9TX92;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Glutathione S-transferase D5 {ECO:0000303|PubMed:22082028};
DE EC=2.5.1.18 {ECO:0000269|PubMed:22082028};
GN Name=GstD5 {ECO:0000312|FlyBase:FBgn0010041};
GN Synonyms=gstD24, GSTD5-5 {ECO:0000312|FlyBase:FBgn0010041};
GN ORFNames=CG12242 {ECO:0000312|FlyBase:FBgn0010041};
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=1.43 mM for glutathione {ECO:0000269|PubMed:22082028};
CC KM=2.98 mM for 1-chloro-2,4-dinitrobenzene
CC {ECO:0000269|PubMed:22082028};
CC Vmax=9.9 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as
CC substrate {ECO:0000269|PubMed:22082028};
CC Vmax=1.48 umol/min/mg enzyme with 4-hydroxy-2-nonenal as substrate
CC {ECO:0000269|PubMed:22082028};
CC Vmax=3.5 nmol/min/mg enzyme with adrenochrome as substrate
CC {ECO:0000269|PubMed:22082028};
CC Vmax=0.203 umol/min/mg enzyme with phenethyl isothiocyanate as
CC substrate {ECO:0000269|PubMed:22082028};
CC Vmax=0.165 umol/min/mg enzyme with 2-hydroxyethyl disulfide 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}.
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DR EMBL; M97702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE014297; AAF54790.3; -; Genomic_DNA.
DR PIR; C46681; C46681.
DR RefSeq; NP_524914.3; NM_080175.3.
DR AlphaFoldDB; Q9VG95; -.
DR SMR; Q9VG95; -.
DR BioGRID; 71335; 6.
DR STRING; 7227.FBpp0082044; -.
DR PaxDb; Q9VG95; -.
DR PRIDE; Q9VG95; -.
DR EnsemblMetazoa; FBtr0082572; FBpp0082044; FBgn0010041.
DR GeneID; 48338; -.
DR KEGG; dme:Dmel_CG12242; -.
DR CTD; 48338; -.
DR FlyBase; FBgn0010041; GstD5.
DR VEuPathDB; VectorBase:FBgn0010041; -.
DR eggNOG; KOG0867; Eukaryota.
DR GeneTree; ENSGT00940000164816; -.
DR HOGENOM; CLU_011226_2_1_1; -.
DR InParanoid; Q9VG95; -.
DR OMA; QYRAYFE; -.
DR OrthoDB; 1231780at2759; -.
DR PhylomeDB; Q9VG95; -.
DR SABIO-RK; Q9VG95; -.
DR BioGRID-ORCS; 48338; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 48338; -.
DR PRO; PR:Q9VG95; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010041; Expressed in seminal fluid secreting gland and 11 other tissues.
DR ExpressionAtlas; Q9VG95; baseline and differential.
DR Genevisible; Q9VG95; 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..216
FT /note="Glutathione S-transferase D5"
FT /id="PRO_0000185957"
FT DOMAIN 1..80
FT /note="GST N-terminal"
FT DOMAIN 86..207
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"
SQ SEQUENCE 216 AA; 24713 MW; 9136816534D39A18 CRC64;
MDFYYSPRGS GCRTVIMVAK ALGVKLNMKL LNTLEKDQLK PEFVKLNPQH TIPTLVDNGF
SIWESRAIAV YLVEKYGKDD TLFPKDPKKQ ALVNQRLYFD MGTLYDSFAK YYYPLFHTGK
PGSDEDFKKI ESSFEYLNIF LEGQNYVAGD HLTVADIAIL STVSTFEIFD FDLNKYPNVA
RWYANAKKVT PGWEENWKGA VELKGVFDAR QAAAKQ
