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P26624

- GST28_SCHJA

UniProt

P26624 - GST28_SCHJA

Protein

Glutathione S-transferase class-mu 28 kDa isozyme

Gene
N/A
Organism
Schistosoma japonicum (Blood fluke)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      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 sitei5 – 51GlutathioneBy similarity
    Binding sitei11 – 111GlutathioneBy similarity
    Binding sitei48 – 481Glutathione; via amide nitrogen and carbonyl oxygen

    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 28 kDa isozyme (EC:2.5.1.18)
    Short name:
    GST 28
    Alternative name(s):
    Sj28 antigen
    Sj28GST
    OrganismiSchistosoma japonicum (Blood fluke)
    Taxonomic identifieri6182 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 206›206Glutathione S-transferase class-mu 28 kDa isozymePRO_0000185814Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi6182.P26624.

    Structurei

    3D structure databases

    ProteinModelPortaliP26624.
    SMRiP26624. Positions 1-206.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini‹1 – 81›81GST N-terminalAdd
    BLAST
    Domaini83 – 206124GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni36 – 405Glutathione bindingBy similarity
    Regioni65 – 662Glutathione 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

    Phylogenomic databases

    eggNOGiNOG122057.

    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: Fragment.

    P26624-1 [UniParc]FASTAAdd to Basket

    « Hide

    VKLIYFNGRG RAEPIRMILV AAGVEFEDER IEFQDWPKIK PTIPGGRLPI    50
    VKITDKRGDV KTMSESLAIA RFIARKHNMM GDTDDEYYII EKMIGQVEDV 100
    ESEYHKTLIK PPEEKEKISK EILNGKVPIL LQAICETLKE STGNLTVGDK 150
    VTLADVVLIA SIDHITDLDK EFLTGKYPEI HKHRKHLLAT SPKLAKYLSE 200
    RHATAF 206
    Length:206
    Mass (Da):23,393
    Last modified:August 1, 1992 - v1
    Checksum:iD1AD3707EDEABAA7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26914 mRNA. Translation: AAA29890.1.
    PIRiB44941.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M26914 mRNA. Translation: AAA29890.1 .
    PIRi B44941.

    3D structure databases

    ProteinModelPortali P26624.
    SMRi P26624. Positions 1-206.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 6182.P26624.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG122057.

    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. "Comparison of the cloned genes of the 26- and 28-kilodalton glutathione S-transferases of Schistosoma japonicum and Schistosoma mansoni."
      Henkle K.J., Davern K.M., Wright M.D., Ramos A.J., Mitchell G.F.
      Mol. Biochem. Parasitol. 40:23-34(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sorsogon / Philippines.

    Entry informationi

    Entry nameiGST28_SCHJA
    AccessioniPrimary (citable) accession number: P26624
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

    There are at least two isoenzymes of GST in S.japonicum.

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3