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)

P30112

- GST26_FASHE

UniProt

P30112 - GST26_FASHE

Protein

Glutathione S-transferase class-mu 26 kDa isozyme 51

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 73 (01 Oct 2014)
      Sequence version 3 (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 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 51 (EC:2.5.1.18)
    Short name:
    GST51
    Alternative name(s):
    Fh51
    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 – 11RemovedBy similarity
    Chaini2 – 218217Glutathione S-transferase class-mu 26 kDa isozyme 51PRO_0000185807Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    218
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 119
    Turni12 – 143
    Helixi15 – 2410
    Beta strandi29 – 335
    Helixi38 – 447
    Beta strandi55 – 606
    Beta strandi63 – 675
    Helixi68 – 7811
    Helixi86 – 11025
    Helixi115 – 13723
    Beta strandi145 – 1473
    Helixi150 – 16213
    Turni163 – 1653
    Turni167 – 1726
    Helixi174 – 18411
    Helixi187 – 1948
    Beta strandi208 – 2114

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2WRTX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L1-218[»]
    ProteinModelPortaliP30112.
    SMRiP30112. Positions 2-215.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30112.

    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 bindingBy similarity
    Regioni41 – 455Glutathione bindingBy similarity
    Regioni54 – 552Glutathione bindingBy similarity
    Regioni67 – 682Glutathione bindingBy similarity

    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.

    P30112-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAKLGYWKI RGLQQPVRLL LEYLGEEYEE HLYGRDDREK WFGDKFNMGL    50
    DLPNLPYYID DKCKLTQSVA IMRYIADKHG MLGTTPEERA RISMIEGAAM 100
    DLRMGFVRVC YNPKFEEVKG DYLKELPTTL KMWSNFLGDR HYLTGSPVSH 150
    VDFMVYEALD CIRYLAPQCL EDFPKLKEFK SRIEDLPKIK AYMESEKFIK 200
    WPLNSWIASF GGGDAAPA 218
    Length:218
    Mass (Da):25,373
    Last modified:January 23, 2007 - v3
    Checksum:iDF8A826E056A2196
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti84 – 841T → S(PubMed:7682383)Curated
    Sequence conflicti135 – 1351N → D(PubMed:7682383)Curated
    Sequence conflicti147 – 1471P → T(PubMed:7682383)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77682 mRNA. Translation: AAA29141.1.
    PIRiA48388.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77682 mRNA. Translation: AAA29141.1 .
    PIRi A48388.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2WRT X-ray 2.40 A/B/C/D/E/F/G/H/I/J/K/L 1-218 [» ]
    ProteinModelPortali P30112.
    SMRi P30112. Positions 2-215.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P30112.

    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. "Sequence analysis of a Fasciola hepatica glutathione S-transferase cDNA clone."
      Muro A., Rodriguez-Medina J.R., Hillyer G.V.
      Am. J. Trop. Med. Hyg. 48:457-463(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-218.

    Entry informationi

    Entry nameiGST26_FASHE
    AccessioniPrimary (citable) accession number: P30112
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 73 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