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P48429

- GST2_ASCSU

UniProt

P48429 - GST2_ASCSU

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Protein
Glutathione S-transferase 2
Gene
GST2
Organism
Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Status
Reviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

Catalytic activityi

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

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 2 (EC:2.5.1.18)
    Alternative name(s):
    GST class-sigma
    Gene namesi
    Name:GST2
    OrganismiAscaris suum (Pig roundworm) (Ascaris lumbricoides)
    Taxonomic identifieri6253 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaAscarididaAscaridoideaAscarididaeAscaris

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – ›20›20Glutathione S-transferase 2
    PRO_0000185924Add
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – ›20›20GST N-terminal
    Add
    BLAST

    Sequence similaritiesi

    Belongs to the GST superfamily. Sigma family.

    Family and domain databases

    Gene3Di3.40.30.10. 1 hit.
    InterProiIPR012336. Thioredoxin-like_fold.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    P48429-1 [UniParc]FASTAAdd to Basket

    « Hide

    GYKVTYFAIR GLAEPIXLLL                                    20
    Length:20
    Mass (Da):2,249
    Last modified:February 1, 1996 - v1
    Checksum:iA506D5F2B144FB20
    GO

    Non-terminal residue

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei20 – 201

    Cross-referencesi

    3D structure databases

    ModBasei Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.40.30.10. 1 hit.
    InterProi IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of a cDNA encoding glutathione S-transferase from Ascaris suum."
      Liebau E., Schoenberger O.L., Walter R.D., Henkle-Duehrsen K.J.
      Mol. Biochem. Parasitol. 63:167-170(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiGST2_ASCSU
    AccessioniPrimary (citable) accession number: P48429
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: April 16, 2014
    This is version 35 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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