Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P56598

- GST29_FASHE

UniProt

P56598 - GST29_FASHE

Protein

Glutathione S-transferase class-mu 26 kDa isozyme 1

Gene
N/A
Organism
Fasciola hepatica (Liver fluke)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei110 – 1101SubstrateBy 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 1 (EC:2.5.1.18)
    Short name:
    GST1
    Alternative name(s):
    Fh1
    OrganismiFasciola hepatica (Liver fluke)
    Taxonomic identifieri6192 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaEchinostomidaEchinostomataEchinostomatoideaFasciolidaeFasciola

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 221220Glutathione S-transferase class-mu 26 kDa isozyme 1PRO_0000185810Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    221
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 119
    Turni12 – 143
    Helixi15 – 239
    Beta strandi27 – 326
    Helixi37 – 437
    Turni44 – 463
    Beta strandi54 – 585
    Beta strandi63 – 664
    Helixi67 – 7711
    Helixi85 – 10925
    Helixi114 – 13623
    Beta strandi144 – 1463
    Helixi149 – 16416
    Turni166 – 1716
    Helixi173 – 18311
    Helixi186 – 1927
    Beta strandi194 – 1963
    Beta strandi208 – 2103
    Beta strandi212 – 2143

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2FHEX-ray2.30A/B2-216[»]
    ProteinModelPortaliP56598.
    SMRiP56598. Positions 2-216.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP56598.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8281GST N-terminalAdd
    BLAST
    Domaini84 – 202119GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 82Glutathione binding
    Regioni40 – 445Glutathione binding
    Regioni53 – 542Glutathione binding
    Regioni66 – 672Glutathione 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.
    IPR003081. GST_mu.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PRINTSiPR01267. GSTRNSFRASEM.
    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.

    P56598-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAKLGYWKI RGLQQPVRLL LEYGEKYEEQ IYERDDGEKW FSKKFELGLD    50
    LPNLPYYIDD KCKLTQSLAI LRYIADKHGM IGSTPEERAR VSMIEGAAVD 100
    LRQGLSRISY DPKFEQLKEG YLKDLPTTMK MWSDFLGKNP YLRGTSVSHV 150
    DFMVYEALDA IRYLEPHCLD HFPNLQQFMS RIEALPSIKA YMESNRFIKW 200
    PLNGWHAQFG GGDAPPSHEK K 221
    Length:221
    Mass (Da):25,730
    Last modified:January 23, 2007 - v2
    Checksum:i17EAF460F750895F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231Y → V in CAA00118. 1 PublicationCurated
    Sequence conflicti111 – 1122DP → VS in CAA00118. 1 PublicationCurated
    Sequence conflicti190 – 1901A → P in CAA00118. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    A00993 Unassigned RNA. Translation: CAA00118.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    A00993 Unassigned RNA. Translation: CAA00118.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FHE X-ray 2.30 A/B 2-216 [» ]
    ProteinModelPortali P56598.
    SMRi P56598. Positions 2-216.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P56598.

    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.
    IPR003081. GST_mu.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01267. GSTRNSFRASEM.
    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 23-221.
    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 (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT.

    Entry informationi

    Entry nameiGST29_FASHE
    AccessioniPrimary (citable) accession number: P56598
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 72 of the entry and version 2 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