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P30102

- GSTY2_ISSOR

UniProt

P30102 - GSTY2_ISSOR

Protein

Glutathione S-transferase Y-2

Gene

GSTY2

Organism
Issatchenkia orientalis (Yeast) (Candida krusei)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    • Comment

    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

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase Y-2 (EC:2.5.1.18)
    Gene namesi
    Name:GSTY2
    OrganismiIssatchenkia orientalis (Yeast) (Candida krusei)
    Taxonomic identifieri4909 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesPichiaceaePichia

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 191190Glutathione S-transferase Y-2PRO_0000185983Add
    BLAST

    Expressioni

    Inductioni

    By O-dinitrobenzene.

    Structurei

    3D structure databases

    ProteinModelPortaliP30102.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8079GST N-terminalAdd
    BLAST
    Domaini85 – 191107GST C-terminalAdd
    BLAST

    Sequence similaritiesi

    Belongs to the GST superfamily.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.

    P30102-1 [UniParc]FASTAAdd to Basket

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    MTFATVYIKP HTPRGDWLAS LGQYVGLEIK TVDYKSAEAS KFEELFPLKR    50
    VPALVTPNGF QLTELIAIVE YIVAKGSKPE LSGKTTEERA TNTRWLSFFN 100
    SDFVQAAGGY FMGPNDEIKQ QSLQTMLSLL EYIDKHLSQS KYFTNNTILT 150
    ADIFAFQIFA MAKQFGVDFT HYPNVERFTG EVSQHPIIKN M 191
    Length:191
    Mass (Da):21,652
    Last modified:January 23, 2007 - v2
    Checksum:i3BD1849C2C91363D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57957 mRNA. Translation: CAA41025.1.
    PIRiS16178.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57957 mRNA. Translation: CAA41025.1 .
    PIRi S16178.

    3D structure databases

    ProteinModelPortali P30102.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Nucleotide sequence of the yeast glutathione S-transferase cDNA."
      Tamaki H., Kumagai H., Tochikura T.
      Biochim. Biophys. Acta 1089:276-279(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Glutathione S-transferase in yeast: induction of mRNA, cDNA cloning and expression in Escherichia coli."
      Tamaki H., Kumagai H., Tochikura T.
      Biochem. Biophys. Res. Commun. 172:669-675(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-16 AND 164-189.

    Entry informationi

    Entry nameiGSTY2_ISSOR
    AccessioniPrimary (citable) accession number: P30102
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 65 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3