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Glutathione S-transferase S1 (EC 2.5.1.18) (GST class-sigma 1) (Glutathione S-transferase 2)

 GSTS1_DROME             Reviewed;         249 AA.
P41043; Q0E945; Q9V7Y4;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
27-JAN-2003, sequence version 2.
25-OCT-2017, entry version 144.
RecName: Full=Glutathione S-transferase S1 {ECO:0000303|PubMed:12547198, ECO:0000303|PubMed:22082028};
EC=2.5.1.18 {ECO:0000269|PubMed:12547198, ECO:0000269|PubMed:22082028};
AltName: Full=GST class-sigma 1;
AltName: Full=Glutathione S-transferase 2;
Name=GstS1 {ECO:0000312|FlyBase:FBgn0010226};
Synonyms=GST2, GSTS1-1 {ECO:0000312|FlyBase:FBgn0010226};
ORFNames=CG8938 {ECO:0000312|FlyBase:FBgn0010226};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=1445191; DOI=10.1007/BF01037590;
Beall C., Fyrberg C., Song S., Fyrberg E.;
"Isolation of a Drosophila gene encoding glutathione S-transferase.";
Biochem. Genet. 30:515-527(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=22082028; DOI=10.1042/BJ20111747;
Saisawang C., Wongsantichon J., Ketterman A.J.;
"A preliminary characterization of the cytosolic glutathione
transferase proteome from Drosophila melanogaster.";
Biochem. J. 442:181-190(2012).
[6]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
FUNCTION, SUBUNIT, AND CATALYTIC ACTIVITY.
PubMed=12547198; DOI=10.1016/S0022-2836(02)01327-X;
Agianian B., Tucker P.A., Schouten A., Leonard K., Bullard B.,
Gros P.;
"Structure of a Drosophila sigma class glutathione S-transferase
reveals a novel active site topography suited for lipid peroxidation
products.";
J. Mol. Biol. 326:151-165(2003).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles
(PubMed:22082028). May be involved in the detoxification of
metabolites produced during cellular division and morphogenesis
(PubMed:1445191, PubMed:12547198). {ECO:0000269|PubMed:12547198,
ECO:0000269|PubMed:1445191, ECO:0000269|PubMed:22082028}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000269|PubMed:12547198, ECO:0000269|PubMed:22082028}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.52 mM for glutathione {ECO:0000269|PubMed:22082028};
KM=1.24 mM for 1-chloro-2,4-dinitrobenzene
{ECO:0000269|PubMed:22082028};
Vmax=4.53 umol/min/mg enzyme with 1-chloro-2,4-dinitrobenzene as
substrate {ECO:0000269|PubMed:22082028};
Vmax=2.81 umol/min/mg enzyme with 4-hydroxy-2-nonenal as
substrate {ECO:0000269|PubMed:22082028};
Vmax=84.3 nmol/min/mg enzyme with adrenochrome as substrate
{ECO:0000269|PubMed:22082028};
Vmax=0.112 umol/min/mg enzyme with phenethyl isothiocyanate as
substrate {ECO:0000269|PubMed:22082028};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12547198}.
-!- DEVELOPMENTAL STAGE: Expressed throughout development with highest
levels being observed in nonfeeding stages, i.e. during embryonic
and pupal development. {ECO:0000269|PubMed:1445191}.
-!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
{ECO:0000303|PubMed:22082028}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M95198; AAA28596.1; -; mRNA.
EMBL; AE013599; AAF57901.1; -; Genomic_DNA.
EMBL; AY118328; AAM48357.1; -; mRNA.
PIR; A48982; A48982.
RefSeq; NP_523767.2; NM_079043.3.
RefSeq; NP_725653.1; NM_166216.2.
RefSeq; NP_725654.1; NM_166217.3.
UniGene; Dm.19945; -.
PDB; 1M0U; X-ray; 1.75 A; A/B=1-249.
PDBsum; 1M0U; -.
ProteinModelPortal; P41043; -.
SMR; P41043; -.
BioGrid; 62625; 32.
DIP; DIP-21396N; -.
IntAct; P41043; 1.
MINT; MINT-1625589; -.
STRING; 7227.FBpp0305731; -.
PaxDb; P41043; -.
PRIDE; P41043; -.
EnsemblMetazoa; FBtr0087005; FBpp0086156; FBgn0010226.
EnsemblMetazoa; FBtr0087006; FBpp0086157; FBgn0010226.
EnsemblMetazoa; FBtr0100258; FBpp0099646; FBgn0010226.
GeneID; 36927; -.
KEGG; dme:Dmel_CG8938; -.
CTD; 36927; -.
FlyBase; FBgn0010226; GstS1.
eggNOG; ENOG410IN5I; Eukaryota.
eggNOG; ENOG4111I69; LUCA.
GeneTree; ENSGT00670000097856; -.
InParanoid; P41043; -.
KO; K04097; -.
OrthoDB; EOG091G0MBB; -.
PhylomeDB; P41043; -.
Reactome; R-DME-156590; Glutathione conjugation.
Reactome; R-DME-2162123; Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
ChiTaRS; GstS1; fly.
EvolutionaryTrace; P41043; -.
GenomeRNAi; 36927; -.
PRO; PR:P41043; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0010226; -.
ExpressionAtlas; P41043; differential.
Genevisible; P41043; DM.
GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
GO; GO:0004602; F:glutathione peroxidase activity; IDA:FlyBase.
GO; GO:0004364; F:glutathione transferase activity; IDA:FlyBase.
GO; GO:0006749; P:glutathione metabolic process; IDA:FlyBase.
GO; GO:0008152; P:metabolic process; IC:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; NAS:FlyBase.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF14497; GST_C_3; 1.
Pfam; PF02798; GST_N; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Detoxification; Reference proteome;
Transferase.
CHAIN 1 249 Glutathione S-transferase S1.
/FTId=PRO_0000185917.
DOMAIN 48 125 GST N-terminal.
DOMAIN 127 249 GST C-terminal.
REGION 96 97 Glutathione binding.
REGION 109 110 Glutathione binding.
BINDING 54 54 Glutathione.
{ECO:0000269|PubMed:12547198}.
BINDING 85 85 Glutathione.
{ECO:0000269|PubMed:12547198}.
BINDING 89 89 Glutathione. {ECO:0000250}.
CONFLICT 61 70 AEPLRYLFAY -> PSPCATCSD (in Ref. 1;
AAA28596). {ECO:0000305}.
CONFLICT 79 85 RVTRDEW -> AHPRRV (in Ref. 1; AAA28596).
{ECO:0000305}.
CONFLICT 224 224 L -> V (in Ref. 1; AAA28596).
{ECO:0000305}.
STRAND 50 58 {ECO:0000244|PDB:1M0U}.
HELIX 59 61 {ECO:0000244|PDB:1M0U}.
HELIX 62 71 {ECO:0000244|PDB:1M0U}.
STRAND 76 80 {ECO:0000244|PDB:1M0U}.
TURN 82 84 {ECO:0000244|PDB:1M0U}.
HELIX 85 88 {ECO:0000244|PDB:1M0U}.
HELIX 89 91 {ECO:0000244|PDB:1M0U}.
HELIX 93 95 {ECO:0000244|PDB:1M0U}.
STRAND 99 102 {ECO:0000244|PDB:1M0U}.
STRAND 105 108 {ECO:0000244|PDB:1M0U}.
HELIX 110 121 {ECO:0000244|PDB:1M0U}.
HELIX 128 152 {ECO:0000244|PDB:1M0U}.
HELIX 157 169 {ECO:0000244|PDB:1M0U}.
HELIX 171 185 {ECO:0000244|PDB:1M0U}.
STRAND 188 191 {ECO:0000244|PDB:1M0U}.
HELIX 197 213 {ECO:0000244|PDB:1M0U}.
TURN 217 220 {ECO:0000244|PDB:1M0U}.
HELIX 222 232 {ECO:0000244|PDB:1M0U}.
HELIX 235 243 {ECO:0000244|PDB:1M0U}.
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


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