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P46427

- GSTP_ONCVO

UniProt

P46427 - GSTP_ONCVO

Protein

Glutathione S-transferase 2

Gene

GST2

Organism
Onchocerca volvulus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Appears to play a central role in the parasite detoxification system.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei7 – 71Glutathione
    Binding sitei42 – 421GlutathioneBy similarity

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase 2 (EC:2.5.1.18)
    Alternative name(s):
    GST class-pi
    Gene namesi
    Name:GST2
    OrganismiOnchocerca volvulus
    Taxonomic identifieri6282 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaSpiruridaFilarioideaOnchocercidaeOnchocerca

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 208208Glutathione S-transferase 2PRO_0000185914Add
    BLAST

    Expressioni

    Tissue specificityi

    Hypodermis, wall of the seminal receptacle and spermatozoa of adult worms.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    208
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 119
    Helixi12 – 143
    Helixi15 – 239
    Beta strandi29 – 335
    Helixi35 – 373
    Turni39 – 413
    Helixi42 – 443
    Beta strandi52 – 554
    Beta strandi58 – 625
    Helixi63 – 7311
    Helixi81 – 10727
    Helixi109 – 11911
    Helixi121 – 13212
    Turni133 – 1353
    Helixi136 – 1383
    Beta strandi139 – 1413
    Beta strandi144 – 1463
    Helixi149 – 16416
    Turni166 – 1716
    Helixi173 – 18311
    Helixi186 – 19712

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1TU7X-ray1.50A/B1-208[»]
    1TU8X-ray1.80A/B/C/D1-208[»]
    ProteinModelPortaliP46427.
    SMRiP46427. Positions 1-208.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46427.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 7878GST N-terminalAdd
    BLAST
    Domaini80 – 200121GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 502Glutathione binding
    Regioni62 – 632Glutathione binding

    Sequence similaritiesi

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

    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.
    IPR003082. GST_pi.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PRINTSiPR01268. GSTRNSFRASEP.
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P46427-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSYKLTYFSI RGLAEPIRLF LVDQDIKFID DRIAKDDFSS IKSQFQFGQL    50
    PCLYDGDQQI VQSGAILRHL ARKYNLNGEN EMETTYIDMF CEGVRDLHVK 100
    YTRMIYMAYE TEKDPYIKSI LPGELAKFEK LLATRGNGRN LILGDKISYA 150
    DYALFEELDV HQILDPHCLD KFPLLKAFHQ RMKDRPKLKE YCEKRDAAKV 200
    PVNGNGKQ 208
    Length:208
    Mass (Da):24,232
    Last modified:November 1, 1995 - v1
    Checksum:iD3A76450AE7A1321
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L28771 mRNA. Translation: AAA53575.1.
    X77393 mRNA. Translation: CAA54568.1.
    PIRiS41933.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L28771 mRNA. Translation: AAA53575.1 .
    X77393 mRNA. Translation: CAA54568.1 .
    PIRi S41933.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1TU7 X-ray 1.50 A/B 1-208 [» ]
    1TU8 X-ray 1.80 A/B/C/D 1-208 [» ]
    ProteinModelPortali P46427.
    SMRi P46427. Positions 1-208.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P46427.

    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.
    IPR003082. GST_pi.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01268. GSTRNSFRASEP.
    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. "Molecular characterisation and localisation of an Onchocerca volvulus pi-class glutathione S-transferase."
      Salinas G., Braun G., Taylor D.W.
      Mol. Biochem. Parasitol. 66:1-9(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Guatemala.
    2. "Onchocerca volvulus: isolation and sequence of a second glutathione S-transferase cDNA."
      Liebau E., Walter R.D., Henkle-Duehrsen K.
      Exp. Parasitol. 79:68-71(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Structure of the major cytosolic glutathione S-transferase from the parasitic nematode Onchocerca volvulus."
      Perbandt M., Hoppner J., Betzel C., Walter R.D., Liebau E.
      J. Biol. Chem. 280:12630-12636(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE, SUBUNIT.

    Entry informationi

    Entry nameiGSTP_ONCVO
    AccessioniPrimary (citable) accession number: P46427
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 66 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3