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Protein

Glutathione S-transferase S1

Gene

GstS1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. May be involved in the detoxification of metabolites produced during cellular division and morphogenesis.

Catalytic activityi

RX + glutathione = HX + R-S-glutathione.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541Glutathione1 Publication
Binding sitei85 – 851Glutathione1 Publication
Binding sitei89 – 891GlutathioneBy similarity

GO - Molecular functioni

  1. glutathione peroxidase activity Source: FlyBase
  2. glutathione transferase activity Source: UniProtKB

GO - Biological processi

  1. glutathione metabolic process Source: FlyBase
  2. metabolic process Source: UniProtKB
  3. oxidation-reduction process Source: GOC
  4. response to oxidative stress Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Enzyme and pathway databases

ReactomeiREACT_207120. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_209269. Detoxification of Reactive Oxygen Species.
REACT_257622. Glutathione conjugation.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione S-transferase S1 (EC:2.5.1.18)
Alternative name(s):
GST class-sigma 1
Glutathione S-transferase 2
Gene namesi
Name:GstS1
Synonyms:GST2
ORF Names:CG8938
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0010226. GstS1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Glutathione S-transferase S1PRO_0000185917Add
BLAST

Proteomic databases

PaxDbiP41043.

Expressioni

Developmental stagei

Expressed throughout development with highest levels being observed in nonfeeding stages, i.e. During embryonic and pupal development.

Gene expression databases

BgeeiP41043.
ExpressionAtlasiP41043. differential.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi62625. 28 interactions.
DIPiDIP-21396N.
IntActiP41043. 1 interaction.
MINTiMINT-1625589.

Structurei

Secondary structure

1
249
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi50 – 589Combined sources
Helixi59 – 613Combined sources
Helixi62 – 7110Combined sources
Beta strandi76 – 805Combined sources
Turni82 – 843Combined sources
Helixi85 – 884Combined sources
Helixi89 – 913Combined sources
Helixi93 – 953Combined sources
Beta strandi99 – 1024Combined sources
Beta strandi105 – 1084Combined sources
Helixi110 – 12112Combined sources
Helixi128 – 15225Combined sources
Helixi157 – 16913Combined sources
Helixi171 – 18515Combined sources
Beta strandi188 – 1914Combined sources
Helixi197 – 21317Combined sources
Turni217 – 2204Combined sources
Helixi222 – 23211Combined sources
Helixi235 – 2439Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M0UX-ray1.75A/B1-249[»]
ProteinModelPortaliP41043.
SMRiP41043. Positions 47-249.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41043.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 12578GST N-terminalAdd
BLAST
Domaini127 – 249123GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni96 – 972Glutathione binding
Regioni109 – 1102Glutathione binding

Sequence similaritiesi

Belongs to the GST superfamily. Sigma family.Curated
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiNOG122057.
GeneTreeiENSGT00670000097856.
InParanoidiP41043.
KOiK00799.
OrthoDBiEOG78WKT1.
PhylomeDBiP41043.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P41043-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEAQAPPA EGAPPAEGEA PPPAEGAEGA VEGGEAAPPA EPAEPIKHSY
60 70 80 90 100
TLFYFNVKAL AEPLRYLFAY GNQEYEDVRV TRDEWPALKP TMPMGQMPVL
110 120 130 140 150
EVDGKRVHQS ISMARFLAKT VGLCGATPWE DLQIDIVVDT INDFRLKIAV
160 170 180 190 200
VSYEPEDEIK EKKLVTLNAE VIPFYLEKLE QTVKDNDGHL ALGKLTWADV
210 220 230 240
YFAGITDYMN YMVKRDLLEP YPALRGVVDA VNALEPIKAW IEKRPVTEV
Length:249
Mass (Da):27,614
Last modified:January 27, 2003 - v2
Checksum:i11AB417F550859BD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 7010AEPLRYLFAY → PSPCATCSD in AAA28596 (PubMed:1445191).Curated
Sequence conflicti79 – 857RVTRDEW → AHPRRV in AAA28596 (PubMed:1445191).Curated
Sequence conflicti224 – 2241L → V in AAA28596 (PubMed:1445191).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95198 mRNA. Translation: AAA28596.1.
AE013599 Genomic DNA. Translation: AAF57901.1.
AY118328 mRNA. Translation: AAM48357.1.
PIRiA48982.
RefSeqiNP_523767.2. NM_079043.3.
NP_725653.1. NM_166216.2.
NP_725654.1. NM_166217.3.
UniGeneiDm.19945.

Genome annotation databases

EnsemblMetazoaiFBtr0087005; FBpp0086156; FBgn0010226.
FBtr0087006; FBpp0086157; FBgn0010226.
FBtr0100258; FBpp0099646; FBgn0010226.
GeneIDi36927.
KEGGidme:Dmel_CG8938.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M95198 mRNA. Translation: AAA28596.1.
AE013599 Genomic DNA. Translation: AAF57901.1.
AY118328 mRNA. Translation: AAM48357.1.
PIRiA48982.
RefSeqiNP_523767.2. NM_079043.3.
NP_725653.1. NM_166216.2.
NP_725654.1. NM_166217.3.
UniGeneiDm.19945.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1M0UX-ray1.75A/B1-249[»]
ProteinModelPortaliP41043.
SMRiP41043. Positions 47-249.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62625. 28 interactions.
DIPiDIP-21396N.
IntActiP41043. 1 interaction.
MINTiMINT-1625589.

Proteomic databases

PaxDbiP41043.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0087005; FBpp0086156; FBgn0010226.
FBtr0087006; FBpp0086157; FBgn0010226.
FBtr0100258; FBpp0099646; FBgn0010226.
GeneIDi36927.
KEGGidme:Dmel_CG8938.

Organism-specific databases

CTDi36927.
FlyBaseiFBgn0010226. GstS1.

Phylogenomic databases

eggNOGiNOG122057.
GeneTreeiENSGT00670000097856.
InParanoidiP41043.
KOiK00799.
OrthoDBiEOG78WKT1.
PhylomeDBiP41043.

Enzyme and pathway databases

ReactomeiREACT_207120. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_209269. Detoxification of Reactive Oxygen Species.
REACT_257622. Glutathione conjugation.

Miscellaneous databases

ChiTaRSiGstS1. fly.
EvolutionaryTraceiP41043.
GenomeRNAii36927.
NextBioi801072.

Gene expression databases

BgeeiP41043.
ExpressionAtlasiP41043. differential.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of a Drosophila gene encoding glutathione S-transferase."
    Beall C., Fyrberg C., Song S., Fyrberg E.
    Biochem. Genet. 30:515-527(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Drosophila melanogaster."
    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.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. "Structure of a Drosophila sigma class glutathione S-transferase reveals a novel active site topography suited for lipid peroxidation products."
    Agianian B., Tucker P.A., Schouten A., Leonard K., Bullard B., Gros P.
    J. Mol. Biol. 326:151-165(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiGST1_DROME
AccessioniPrimary (citable) accession number: P41043
Secondary accession number(s): Q0E945, Q9V7Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 27, 2003
Last modified: February 4, 2015
This is version 117 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.