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P20432

- GSTT1_DROME

UniProt

P20432 - GSTT1_DROME

Protein

Glutathione S-transferase 1-1

Gene

GstD1

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 127 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Has DDT dehydrochlorinase activity.1 Publication

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.1 Publication
    1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101Glutathione1 Publication

    GO - Molecular functioni

    1. DDT-dehydrochlorinase activity Source: FlyBase
    2. glutathione transferase activity Source: FlyBase

    GO - Biological processi

    1. glutathione metabolic process Source: FlyBase

    Keywords - Molecular functioni

    Lyase, Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase 1-1 (EC:2.5.1.18, EC:4.5.1.1)
    Alternative name(s):
    DDT-dehydrochlorinase
    GST class-theta
    Gene namesi
    Name:GstD1
    Synonyms:GST, Gst1
    ORF Names:CG10045
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0001149. GstD1.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 209209Glutathione S-transferase 1-1PRO_0000185947Add
    BLAST

    Proteomic databases

    PaxDbiP20432.
    PRIDEiP20432.

    Expressioni

    Gene expression databases

    BgeeiP20432.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi66612. 15 interactions.
    DIPiDIP-17237N.
    IntActiP20432. 2 interactions.
    MINTiMINT-323021.

    Structurei

    Secondary structure

    1
    209
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64
    Helixi11 – 2313
    Beta strandi28 – 314
    Helixi34 – 363
    Helixi38 – 403
    Helixi42 – 454
    Beta strandi55 – 584
    Beta strandi61 – 644
    Helixi66 – 7712
    Beta strandi79 – 813
    Helixi88 – 10316
    Helixi105 – 11915
    Helixi125 – 14117
    Turni142 – 1443
    Beta strandi146 – 1527
    Helixi155 – 16915
    Helixi174 – 1763
    Helixi178 – 19013
    Helixi194 – 20411
    Helixi205 – 2073

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EINX-ray1.13A1-209[»]
    3MAKX-ray1.80A1-209[»]
    ProteinModelPortaliP20432.
    SMRiP20432. Positions 2-208.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20432.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8181GST N-terminalAdd
    BLAST
    Domaini87 – 208122GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni51 – 533Glutathione binding
    Regioni65 – 673Glutathione binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0625.
    GeneTreeiENSGT00540000069741.
    InParanoidiP20432.
    KOiK00799.
    OMAiYTRLAHE.
    OrthoDBiEOG7V1FRJ.
    PhylomeDBiP20432.

    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.

    P20432-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDFYYLPGS SPCRSVIMTA KAVGVELNKK LLNLQAGEHL KPEFLKINPQ    50
    HTIPTLVDNG FALWESRAIQ VYLVEKYGKT DSLYPKCPKK RAVINQRLYF 100
    DMGTLYQSFA NYYYPQVFAK APADPEAFKK IEAAFEFLNT FLEGQDYAAG 150
    DSLTVADIAL VATVSTFEVA KFEISKYANV NRWYENAKKV TPGWEENWAG 200
    CLEFKKYFE 209
    Length:209
    Mass (Da):23,866
    Last modified:February 1, 1991 - v1
    Checksum:i4AD8E237CCF804F2
    GO

    Sequence cautioni

    The sequence AAM52032.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14233 mRNA. Translation: CAA32449.1.
    S51044 mRNA. Translation: AAA04220.1.
    M97702 Genomic DNA. No translation available.
    AE014297 Genomic DNA. Translation: AAF54786.1.
    AE014297 Genomic DNA. Translation: ABC66168.1.
    AY121705 mRNA. Translation: AAM52032.1. Different initiation.
    PIRiA34798. XUFF11.
    RefSeqiNP_001034042.1. NM_001038953.1.
    NP_524326.1. NM_079602.4.
    UniGeneiDm.2439.

    Genome annotation databases

    EnsemblMetazoaiFBtr0082607; FBpp0082077; FBgn0001149.
    FBtr0100410; FBpp0099824; FBgn0001149.
    GeneIDi41503.
    KEGGidme:Dmel_CG10045.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X14233 mRNA. Translation: CAA32449.1 .
    S51044 mRNA. Translation: AAA04220.1 .
    M97702 Genomic DNA. No translation available.
    AE014297 Genomic DNA. Translation: AAF54786.1 .
    AE014297 Genomic DNA. Translation: ABC66168.1 .
    AY121705 mRNA. Translation: AAM52032.1 . Different initiation.
    PIRi A34798. XUFF11.
    RefSeqi NP_001034042.1. NM_001038953.1.
    NP_524326.1. NM_079602.4.
    UniGenei Dm.2439.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EIN X-ray 1.13 A 1-209 [» ]
    3MAK X-ray 1.80 A 1-209 [» ]
    ProteinModelPortali P20432.
    SMRi P20432. Positions 2-208.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 66612. 15 interactions.
    DIPi DIP-17237N.
    IntActi P20432. 2 interactions.
    MINTi MINT-323021.

    Proteomic databases

    PaxDbi P20432.
    PRIDEi P20432.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0082607 ; FBpp0082077 ; FBgn0001149 .
    FBtr0100410 ; FBpp0099824 ; FBgn0001149 .
    GeneIDi 41503.
    KEGGi dme:Dmel_CG10045.

    Organism-specific databases

    CTDi 41503.
    FlyBasei FBgn0001149. GstD1.

    Phylogenomic databases

    eggNOGi COG0625.
    GeneTreei ENSGT00540000069741.
    InParanoidi P20432.
    KOi K00799.
    OMAi YTRLAHE.
    OrthoDBi EOG7V1FRJ.
    PhylomeDBi P20432.

    Miscellaneous databases

    EvolutionaryTracei P20432.
    GenomeRNAii 41503.
    NextBioi 824191.

    Gene expression databases

    Bgeei P20432.

    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. "Drosophila glutathione S-transferase 1-1 shares a region of sequence homology with the maize glutathione S-transferase III."
      Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.
      Proc. Natl. Acad. Sci. U.S.A. 87:31-35(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-20.
      Strain: Oregon-R.
    2. "The Drosophila glutathione S-transferase 1-1 is encoded by an intronless gene at 87B."
      Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.
      Biochem. Biophys. Res. Commun. 178:1205-1211(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    3. "The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster."
      Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.
      J. Biol. Chem. 268:9737-9746(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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.
    5. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Head.
    7. "Recognition and detoxification of the insecticide DDT by Drosophila melanogaster glutathione S-transferase D1."
      Low W.Y., Feil S.C., Ng H.L., Gorman M.A., Morton C.J., Pyke J., McConville M.J., Bieri M., Mok Y.F., Robin C., Gooley P.R., Parker M.W., Batterham P.
      J. Mol. Biol. 399:358-366(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.13 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, FUNCTION AS DDT DEHYDROCHLORINASE, CATALYTIC ACTIVITY, SUBUNIT.

    Entry informationi

    Entry nameiGSTT1_DROME
    AccessioniPrimary (citable) accession number: P20432
    Secondary accession number(s): Q4JFI6
    , Q8MR98, Q9TX88, Q9VG99
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Miscellaneous

    Has a specific activity toward 1-chloro-2,4-dinitrobenzene comparable to that for the mammalian glutathione S-transferases but did not have as broad a substrate specificity pattern. Has no GSH peroxidase activity.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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