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P46417

- GSTX3_SOYBN

UniProt

P46417 - GSTX3_SOYBN

Protein

Glutathione S-transferase 3

Gene

GST3

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      Previous versions | rss
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    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Involved in the detoxification of certain herbicides.

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei13 – 131GlutathioneBy similarity
    Binding sitei54 – 541Glutathione; via amide nitrogen and carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase 3 (EC:2.5.1.18)
    Gene namesi
    Name:GST3
    OrganismiGlycine max (Soybean) (Glycine hispida)
    Taxonomic identifieri3847 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaePhaseoleaeGlycineSoja
    ProteomesiUP000008827: Chromosome 15

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 219219Glutathione S-transferase 3PRO_0000185873Add
    BLAST

    Proteomic databases

    PRIDEiP46417.

    Expressioni

    Gene expression databases

    GenevestigatoriP46417.

    Interactioni

    Subunit structurei

    Homodimer. degradation; (R)-lactate from methylglyoxal: step 1/2.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliP46417.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 8280GST N-terminalAdd
    BLAST
    Domaini88 – 216129GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni66 – 672Glutathione bindingBy similarity

    Sequence similaritiesi

    Belongs to the GST superfamily. HSP26 family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    KOiK00799.
    OMAiRCMERET.

    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.
    PF13417. GST_N_3. 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.

    P46417-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDEVVLLDT WASMYGMRAR IALAEKGVRY EYKEENLMNR SPLLLQMNPI    50
    HKKIPVLIHN GKPICESAII VQYIDEVWND KSPLMPSDPY KRSQARFWVD 100
    YIDKKIYDTW KKMWLSKGEE HEEGKKELIS IFKQLEETLT DKPFYGDDTF 150
    GFVDLCLITF SSWFYTYETY GNFKMEEECP KLMAWVKRCM ERETVSNTLP 200
    DAKKVYGLIV ELQKTLESK 219
    Length:219
    Mass (Da):25,901
    Last modified:November 1, 1995 - v1
    Checksum:i6A2E46B759476A8C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68819 mRNA. Translation: CAA48717.1.
    PIRiS47177.
    RefSeqiNP_001236181.1. NM_001249252.2.
    UniGeneiGma.1560.

    Genome annotation databases

    EnsemblPlantsiGLYMA15G40290.1; GLYMA15G40290.1; GLYMA15G40290.
    GeneIDi547925.
    KEGGigmx:547925.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68819 mRNA. Translation: CAA48717.1 .
    PIRi S47177.
    RefSeqi NP_001236181.1. NM_001249252.2.
    UniGenei Gma.1560.

    3D structure databases

    ProteinModelPortali P46417.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P46417.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi GLYMA15G40290.1 ; GLYMA15G40290.1 ; GLYMA15G40290 .
    GeneIDi 547925.
    KEGGi gmx:547925.

    Phylogenomic databases

    KOi K00799.
    OMAi RCMERET.

    Gene expression databases

    Genevestigatori P46417.

    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.
    PF13417. GST_N_3. 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. Koellner B., Finkelnburg B., Mayerbacher R., Paulus C., Springer B.
      Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leaf.
    2. Cited for: CATALYTIC ACTIVITY, SUBUNIT.

    Entry informationi

    Entry nameiGSTX3_SOYBN
    AccessioniPrimary (citable) accession number: P46417
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally (PubMed:10666306) thought to be a glyoxalase I.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3