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P31670

- GST27_FASHE

UniProt

P31670 - GST27_FASHE

Protein

Glutathione S-transferase class-mu 26 kDa isozyme 47

Gene
N/A
Organism
Fasciola hepatica (Liver fluke)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
    GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei111 – 1111SubstrateBy similarity

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase class-mu 26 kDa isozyme 47 (EC:2.5.1.18)
    Short name:
    GST47
    Alternative name(s):
    Fh47
    OrganismiFasciola hepatica (Liver fluke)
    Taxonomic identifieri6192 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaEchinostomidaEchinostomataEchinostomatoideaFasciolidaeFasciola

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 218217Glutathione S-transferase class-mu 26 kDa isozyme 47PRO_0000185808Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    218
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107
    Turni12 – 143
    Helixi15 – 239
    Beta strandi29 – 335
    Helixi39 – 424
    Turni43 – 475
    Beta strandi55 – 595
    Beta strandi64 – 674
    Helixi70 – 778
    Turni78 – 803
    Helixi86 – 10722
    Beta strandi110 – 1123
    Helixi115 – 1228
    Turni123 – 1253
    Helixi126 – 13712
    Beta strandi145 – 1473
    Helixi150 – 16213
    Turni163 – 1653
    Helixi167 – 1704
    Helixi174 – 18512
    Helixi187 – 1926
    Beta strandi206 – 2116

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1FHEX-ray3.00A2-218[»]
    ProteinModelPortaliP31670.
    SMRiP31670. Positions 2-215.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP31670.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8382GST N-terminalAdd
    BLAST
    Domaini85 – 203119GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 82Glutathione binding
    Regioni41 – 455Glutathione binding
    Regioni54 – 552Glutathione binding
    Regioni67 – 682Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Mu 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.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P31670-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAKLGYWKL RGLAQPVRLF LEYLGEEYEE HLYGRDDREK WMSEKFNMGL    50
    DLPNLPYYID DKCKLTQSVA IMRYIADKHG MLGTTPEERA RISMIEGAAM 100
    DLRIGFGRVC YNPKFEEVKE EYVKELPKTL KMWSDFLGDR HYLTGSSVSH 150
    VDFMLYETLD SIRYLAPHCL DEFPKLKEFK SRIEALPKIK AYMESKRFIK 200
    WPLNGWAASF GAGDAPPS 218
    Length:218
    Mass (Da):25,412
    Last modified:January 23, 2007 - v3
    Checksum:i3FF8B667232663B3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti66 – 661T → I in CAA00121. 1 PublicationCurated
    Sequence conflicti103 – 1064RIGF → FEEL1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77681 mRNA. Translation: AAA29140.1.
    A00996 Unassigned RNA. Translation: CAA00121.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77681 mRNA. Translation: AAA29140.1 .
    A00996 Unassigned RNA. Translation: CAA00121.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1FHE X-ray 3.00 A 2-218 [» ]
    ProteinModelPortali P31670.
    SMRi P31670. Positions 2-215.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P31670.

    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. "Molecular characterization of cDNA sequences encoding glutathione S-transferases of Fasciola hepatica."
      Panaccio M., Wilson L.R., Crameri S.L., Wijffels G.L., Spithill T.W.
      Exp. Parasitol. 74:232-237(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE OF 8-106.
    3. "Crystallization, structural determination and analysis of a novel parasite vaccine candidate: Fasciola hepatica glutathione S-transferase."
      Rossjohn J., Feil S.C., Wilce M.C.J., Sexton J.L., Spithill T.W., Parker M.W.
      J. Mol. Biol. 273:857-872(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.

    Entry informationi

    Entry nameiGST27_FASHE
    AccessioniPrimary (citable) accession number: P31670
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 80 of the entry and version 3 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