GSTS1_DROME
ID GSTS1_DROME Reviewed; 249 AA.
AC P41043; Q0E945; Q9V7Y4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Glutathione S-transferase S1 {ECO:0000303|PubMed:12547198, ECO:0000303|PubMed:22082028};
DE EC=2.5.1.18 {ECO:0000269|PubMed:12547198, ECO:0000269|PubMed:22082028};
DE AltName: Full=GST class-sigma 1;
DE AltName: Full=Glutathione S-transferase 2;
GN Name=GstS1 {ECO:0000312|FlyBase:FBgn0010226};
GN Synonyms=GST2, GSTS1-1 {ECO:0000312|FlyBase:FBgn0010226};
GN ORFNames=CG8938 {ECO:0000312|FlyBase:FBgn0010226};
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 [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=1445191; DOI=10.1007/bf01037590;
RA Beall C., Fyrberg C., Song S., Fyrberg E.;
RT "Isolation of a Drosophila gene encoding glutathione S-transferase.";
RL Biochem. Genet. 30:515-527(1992).
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=Embryo;
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 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).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
RP FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=12547198; DOI=10.1016/s0022-2836(02)01327-x;
RA Agianian B., Tucker P.A., Schouten A., Leonard K., Bullard B., Gros P.;
RT "Structure of a Drosophila sigma class glutathione S-transferase reveals a
RT novel active site topography suited for lipid peroxidation products.";
RL J. Mol. Biol. 326:151-165(2003).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles (PubMed:22082028).
CC May be involved in the detoxification of metabolites produced during
CC cellular division and morphogenesis (PubMed:1445191, PubMed:12547198).
CC {ECO:0000269|PubMed:12547198, ECO:0000269|PubMed:1445191,
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:12547198, ECO:0000269|PubMed:22082028};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.52 mM for glutathione {ECO:0000269|PubMed:22082028};
CC KM=1.24 mM for 1-chloro-2,4-dinitrobenzene
CC {ECO:0000269|PubMed:22082028};
CC Vmax=4.53 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as
CC substrate {ECO:0000269|PubMed:22082028};
CC Vmax=2.81 umol/min/mg enzyme with 4-hydroxy-2-nonenal as substrate
CC {ECO:0000269|PubMed:22082028};
CC Vmax=84.3 nmol/min/mg enzyme with adrenochrome as substrate
CC {ECO:0000269|PubMed:22082028};
CC Vmax=0.112 umol/min/mg enzyme with phenethyl isothiocyanate as
CC substrate {ECO:0000269|PubMed:22082028};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12547198}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development with highest
CC levels being observed in nonfeeding stages, i.e. during embryonic and
CC pupal development. {ECO:0000269|PubMed:1445191}.
CC -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC {ECO:0000303|PubMed:22082028}.
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DR EMBL; M95198; AAA28596.1; -; mRNA.
DR EMBL; AE013599; AAF57901.1; -; Genomic_DNA.
DR EMBL; AY118328; AAM48357.1; -; mRNA.
DR PIR; A48982; A48982.
DR RefSeq; NP_523767.2; NM_079043.3.
DR RefSeq; NP_725653.1; NM_166216.2.
DR RefSeq; NP_725654.1; NM_166217.3.
DR PDB; 1M0U; X-ray; 1.75 A; A/B=1-249.
DR PDBsum; 1M0U; -.
DR AlphaFoldDB; P41043; -.
DR SMR; P41043; -.
DR BioGRID; 62625; 33.
DR DIP; DIP-21396N; -.
DR IntAct; P41043; 1.
DR STRING; 7227.FBpp0305731; -.
DR PaxDb; P41043; -.
DR DNASU; 36927; -.
DR EnsemblMetazoa; FBtr0087005; FBpp0086156; FBgn0010226.
DR EnsemblMetazoa; FBtr0087006; FBpp0086157; FBgn0010226.
DR EnsemblMetazoa; FBtr0100258; FBpp0099646; FBgn0010226.
DR GeneID; 36927; -.
DR KEGG; dme:Dmel_CG8938; -.
DR CTD; 36927; -.
DR FlyBase; FBgn0010226; GstS1.
DR VEuPathDB; VectorBase:FBgn0010226; -.
DR eggNOG; KOG1695; Eukaryota.
DR GeneTree; ENSGT00940000160278; -.
DR HOGENOM; CLU_039475_1_0_1; -.
DR InParanoid; P41043; -.
DR OMA; DWENLMI; -.
DR OrthoDB; 1162336at2759; -.
DR PhylomeDB; P41043; -.
DR Reactome; R-DME-156590; Glutathione conjugation.
DR Reactome; R-DME-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
DR SABIO-RK; P41043; -.
DR SignaLink; P41043; -.
DR BioGRID-ORCS; 36927; 0 hits in 3 CRISPR screens.
DR ChiTaRS; GstS1; fly.
DR EvolutionaryTrace; P41043; -.
DR GenomeRNAi; 36927; -.
DR PRO; PR:P41043; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0010226; Expressed in testis and 51 other tissues.
DR ExpressionAtlas; P41043; baseline and differential.
DR Genevisible; P41043; DM.
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:0004667; F:prostaglandin-D synthase activity; ISS: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; PF14497; GST_C_3; 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..249
FT /note="Glutathione S-transferase S1"
FT /id="PRO_0000185917"
FT DOMAIN 48..125
FT /note="GST N-terminal"
FT DOMAIN 127..249
FT /note="GST C-terminal"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 54
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:12547198"
FT BINDING 85
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000269|PubMed:12547198"
FT BINDING 89
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 96..97
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT BINDING 109..110
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT CONFLICT 61..70
FT /note="AEPLRYLFAY -> PSPCATCSD (in Ref. 1; AAA28596)"
FT /evidence="ECO:0000305"
FT CONFLICT 79..85
FT /note="RVTRDEW -> AHPRRV (in Ref. 1; AAA28596)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="L -> V (in Ref. 1; AAA28596)"
FT /evidence="ECO:0000305"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:1M0U"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:1M0U"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:1M0U"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:1M0U"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:1M0U"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:1M0U"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:1M0U"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1M0U"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:1M0U"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1M0U"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:1M0U"
FT HELIX 128..152
FT /evidence="ECO:0007829|PDB:1M0U"
FT HELIX 157..169
FT /evidence="ECO:0007829|PDB:1M0U"
FT HELIX 171..185
FT /evidence="ECO:0007829|PDB:1M0U"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:1M0U"
FT HELIX 197..213
FT /evidence="ECO:0007829|PDB:1M0U"
FT TURN 217..220
FT /evidence="ECO:0007829|PDB:1M0U"
FT HELIX 222..232
FT /evidence="ECO:0007829|PDB:1M0U"
FT HELIX 235..243
FT /evidence="ECO:0007829|PDB:1M0U"
SQ SEQUENCE 249 AA; 27614 MW; 11AB417F550859BD CRC64;
MADEAQAPPA EGAPPAEGEA PPPAEGAEGA VEGGEAAPPA EPAEPIKHSY TLFYFNVKAL
AEPLRYLFAY GNQEYEDVRV TRDEWPALKP TMPMGQMPVL EVDGKRVHQS ISMARFLAKT
VGLCGATPWE DLQIDIVVDT INDFRLKIAV VSYEPEDEIK EKKLVTLNAE VIPFYLEKLE
QTVKDNDGHL ALGKLTWADV YFAGITDYMN YMVKRDLLEP YPALRGVVDA VNALEPIKAW
IEKRPVTEV
