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P30113

- GST28_SCHBO

UniProt

P30113 - GST28_SCHBO

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Protein
Glutathione S-transferase class-mu 28 kDa isozyme
Gene
N/A
Organism
Schistosoma bovis (Blood fluke)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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 sitei10 – 101Glutathione
Binding sitei16 – 161Glutathione
Binding sitei53 – 531Glutathione; via amide nitrogen and carbonyl oxygen

GO - Molecular functioni

  1. glutathione transferase activity Source: UniProtKB-EC
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase class-mu 28 kDa isozyme (EC:2.5.1.18)
    Short name:
    GST 28
    Alternative name(s):
    Sb28GST
    OrganismiSchistosoma bovis (Blood fluke)
    Taxonomic identifieri6184 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101Y → F: Loss of enzyme activity. 1 Publication
    Mutagenesisi21 – 211R → L: Reduces catalytic activity 12-fold. 1 Publication
    Mutagenesisi21 – 211R → Q: Reduces catalytic activity 120-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 211211Glutathione S-transferase class-mu 28 kDa isozyme
    PRO_0000185812Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 117
    Turni13 – 175
    Helixi18 – 2710
    Beta strandi32 – 354
    Turni38 – 403
    Turni42 – 443
    Helixi45 – 473
    Beta strandi53 – 597
    Beta strandi65 – 695
    Helixi71 – 8111
    Helixi89 – 11022
    Helixi117 – 12913
    Helixi131 – 14414
    Beta strandi147 – 1526
    Helixi158 – 17316
    Helixi183 – 19513
    Helixi197 – 2037

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C80X-ray2.30A/B1-211[»]
    2C8UX-ray2.00A/B1-211[»]
    2CA8X-ray2.49A1-211[»]
    2CAIX-ray2.26A/B1-211[»]
    2CAQX-ray2.00A1-211[»]
    2F8FX-ray2.10A/B1-211[»]
    ProteinModelPortaliP30113.
    SMRiP30113. Positions 4-211.

    Miscellaneous databases

    EvolutionaryTraceiP30113.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 8683GST N-terminal
    Add
    BLAST
    Domaini88 – 211124GST C-terminal
    Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni41 – 455Glutathione binding
    Regioni70 – 712Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Mu family.

    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.

    P30113-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTGDHIKVIY FNGRGRAESI RMTLVAAGVN YEDERISFQD WPKIKPTIPG    50
    GRLPAVKITD NHGHVKWMVE SLAIARYMAK KHHMMGGTEE EYYNVEKLIG 100
    QAEDLEHEYY KTLMKPEEEK QKIIKEILNG KVPVLLDIIC ESLKASTGKL 150
    AVGDKVTLAD LVLIAVIDHV TDLDKEFLTG KYPEIHKHRE NLLASSPRLA 200
    KYLSDRAATP F 211
    Length:211
    Mass (Da):23,898
    Last modified:June 1, 1994 - v2
    Checksum:i9B9F1358710D3C76
    GO

    Sequence cautioni

    The sequence AAA29892.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87799 Genomic DNA. Translation: AAA29892.1. Different initiation.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M87799 Genomic DNA. Translation: AAA29892.1 . Different initiation.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C80 X-ray 2.30 A/B 1-211 [» ]
    2C8U X-ray 2.00 A/B 1-211 [» ]
    2CA8 X-ray 2.49 A 1-211 [» ]
    2CAI X-ray 2.26 A/B 1-211 [» ]
    2CAQ X-ray 2.00 A 1-211 [» ]
    2F8F X-ray 2.10 A/B 1-211 [» ]
    ProteinModelPortali P30113.
    SMRi P30113. Positions 4-211.
    ModBasei Search...

    Chemistry

    DrugBanki DB00143. Glutathione.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P30113.

    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. "Inter-species variation of schistosome 28-kDa glutathione S-transferases."
      Trottein F., Goding G., Sellin B., Gorillot I., Samaio M., Lecocq J.-P., Capron A.
      Mol. Biochem. Parasitol. 54:63-72(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Probing the mechanism of GSH activation in Schistosoma haematobium glutathione-S-transferase by site-directed mutagenesis and X-ray crystallography."
      Baiocco P., Gourlay L.J., Angelucci F., Fontaine J., Herve M., Miele A.E., Trottein F., Brunori M., Bellelli A.
      J. Mol. Biol. 360:678-689(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, SUBUNIT, MUTAGENESIS OF TYR-10 AND ARG-21.

    Entry informationi

    Entry nameiGST28_SCHBO
    AccessioniPrimary (citable) accession number: P30113
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: June 1, 1994
    Last modified: April 16, 2014
    This is version 80 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

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