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P41043

- GST1_DROME

UniProt

P41043 - GST1_DROME

Protein

Glutathione S-transferase S1

Gene

GstS1

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (27 Jan 2003)
      Previous versions | rss
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    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

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

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

    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.

    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.

    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 – 589
    Helixi59 – 613
    Helixi62 – 7110
    Beta strandi76 – 805
    Turni82 – 843
    Helixi85 – 884
    Helixi89 – 913
    Helixi93 – 953
    Beta strandi99 – 1024
    Beta strandi105 – 1084
    Helixi110 – 12112
    Helixi128 – 15225
    Helixi157 – 16913
    Helixi171 – 18515
    Beta strandi188 – 1914
    Helixi197 – 21317
    Turni217 – 2204
    Helixi222 – 23211
    Helixi235 – 2439

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MADEAQAPPA EGAPPAEGEA PPPAEGAEGA VEGGEAAPPA EPAEPIKHSY    50
    TLFYFNVKAL AEPLRYLFAY GNQEYEDVRV TRDEWPALKP TMPMGQMPVL 100
    EVDGKRVHQS ISMARFLAKT VGLCGATPWE DLQIDIVVDT INDFRLKIAV 150
    VSYEPEDEIK EKKLVTLNAE VIPFYLEKLE QTVKDNDGHL ALGKLTWADV 200
    YFAGITDYMN YMVKRDLLEP YPALRGVVDA VNALEPIKAW IEKRPVTEV 249
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M95198 mRNA. Translation: AAA28596.1 .
    AE013599 Genomic DNA. Translation: AAF57901.1 .
    AY118328 mRNA. Translation: AAM48357.1 .
    PIRi A48982.
    RefSeqi NP_523767.2. NM_079043.3.
    NP_725653.1. NM_166216.2.
    NP_725654.1. NM_166217.3.
    UniGenei Dm.19945.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M0U X-ray 1.75 A/B 1-249 [» ]
    ProteinModelPortali P41043.
    SMRi P41043. Positions 47-249.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 62625. 28 interactions.
    DIPi DIP-21396N.
    IntActi P41043. 1 interaction.
    MINTi MINT-1625589.

    Proteomic databases

    PaxDbi P41043.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0087005 ; FBpp0086156 ; FBgn0010226 .
    FBtr0087006 ; FBpp0086157 ; FBgn0010226 .
    FBtr0100258 ; FBpp0099646 ; FBgn0010226 .
    GeneIDi 36927.
    KEGGi dme:Dmel_CG8938.

    Organism-specific databases

    CTDi 36927.
    FlyBasei FBgn0010226. GstS1.

    Phylogenomic databases

    eggNOGi NOG122057.
    GeneTreei ENSGT00670000097856.
    InParanoidi P41043.
    KOi K00799.
    OrthoDBi EOG78WKT1.
    PhylomeDBi P41043.

    Enzyme and pathway databases

    Reactomei REACT_207120. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
    REACT_209269. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    ChiTaRSi GstS1. drosophila.
    EvolutionaryTracei P41043.
    GenomeRNAii 36927.
    NextBioi 801072.

    Gene expression databases

    Bgeei P41043.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 113 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