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P46420

- GSTF4_MAIZE

UniProt

P46420 - GSTF4_MAIZE

Protein

Glutathione S-transferase 4

Gene

GST4

Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 87 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      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. Most active with substrates possessing a chloroacetamide structure. Trans-cinnamic acid and 1-chloro-2,4-dinitrobenzene are not effective substrates. May play an important role in the benoxacor-mediated protection of maize from metolachlor injury.

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 7.5-8. Active from pH 6 to 9.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei14 – 141GlutathioneBy similarity

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase 4 (EC:2.5.1.18)
    Alternative name(s):
    GST class-phi member 4
    GST-27
    GST-IV
    Gene namesi
    Name:GST4
    OrganismiZea mays (Maize)
    Taxonomic identifieri4577 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

    Organism-specific databases

    GrameneiP46420.
    MaizeGDBi113242.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 223222Glutathione S-transferase 4PRO_0000185843Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21Blocked amino end (Ala)

    Proteomic databases

    PRIDEiP46420.

    Expressioni

    Tissue specificityi

    Seedling roots.

    Inductioni

    By herbicides.

    Interactioni

    Subunit structurei

    Homodimer or heterodimer of GST-I and GST-IV (=GST-II).

    Structurei

    3D structure databases

    ProteinModelPortaliP46420.
    SMRiP46420. Positions 6-212.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 8582GST N-terminalAdd
    BLAST
    Domaini90 – 223134GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni43 – 442Glutathione bindingBy similarity
    Regioni56 – 572Glutathione bindingBy similarity
    Regioni69 – 702Glutathione bindingBy similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    HOGENOMiHOG000125746.
    KOiK00799.
    OMAiDAIYEAY.

    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.

    P46420-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATPAVKVYG WAISPFVSRA LLALEEAGVD YELVPMSRQD GDHRRPEHLA    50
    RNPFGKVPVL EDGDLTLFES RAIARHVLRK HKPELLGGGR LEQTAMVDVW 100
    LEVEAHQLSP PAIAIVVECV FAPFLGRERN QAVVDENVEK LKKVLEVYEA 150
    RLATCTYLAG DFLSLADLSP FTIMHCLMAT EYAALVHALP HVSAWWQGLA 200
    ARPAANKVAQ FMPVGAGAPK EQE 223
    Length:223
    Mass (Da):24,570
    Last modified:January 23, 2007 - v2
    Checksum:i24235245AFB4A403
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79515 mRNA. Translation: CAA56047.1.
    U12679 mRNA. Translation: AAA20585.1.
    PIRiS52037.
    RefSeqiNP_001105366.1. NM_001111896.1.
    UniGeneiZm.17839.

    Genome annotation databases

    GeneIDi542311.
    KEGGizma:542311.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79515 mRNA. Translation: CAA56047.1 .
    U12679 mRNA. Translation: AAA20585.1 .
    PIRi S52037.
    RefSeqi NP_001105366.1. NM_001111896.1.
    UniGenei Zm.17839.

    3D structure databases

    ProteinModelPortali P46420.
    SMRi P46420. Positions 6-212.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P46420.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 542311.
    KEGGi zma:542311.

    Organism-specific databases

    Gramenei P46420.
    MaizeGDBi 113242.

    Phylogenomic databases

    HOGENOMi HOG000125746.
    KOi K00799.
    OMAi DAIYEAY.

    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. "Cloning and characterization of maize herbicide safener-induced cDNAs encoding subunits of glutathione S-transferase isoforms I, II and IV."
      Jepson I., Lay V.J., Holt D.C., Bright S.W.J., Greenland A.J.
      Plant Mol. Biol. 26:1855-1866(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. UE95.
      Tissue: Seedling root.
    2. "A cDNA clone encoding the 27-kilodalton subunits of glutathione S-transferase IV from Zea mays."
      Irzyk G.P., Potter S., Ward E., Fuerst E.P.
      Plant Physiol. 107:311-312(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Pioneer hybrid 3906.
    3. "Purification and characterization of a glutathione S-transferase from benoxacor-treated maize (Zea mays)."
      Irzyk G.P., Fuerst E.P.
      Plant Physiol. 102:803-810(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.

    Entry informationi

    Entry nameiGSTF4_MAIZE
    AccessioniPrimary (citable) accession number: P46420
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 87 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3