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P12653

- GSTF1_MAIZE

UniProt

P12653 - GSTF1_MAIZE

Protein

Glutathione S-transferase 1

Gene

GST1

Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 4 (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.

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei12 – 121GlutathioneBy similarity

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    SABIO-RKP12653.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase 1 (EC:2.5.1.18)
    Alternative name(s):
    GST class-phi member 1
    GST-29
    GST-I
    Gene namesi
    Name:GST1
    OrganismiZea mays (Maize)
    Taxonomic identifieri4577 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

    Organism-specific databases

    GrameneiP12653.
    MaizeGDBi65344.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 214213Glutathione S-transferase 1PRO_0000185841Add
    BLAST

    Proteomic databases

    PRIDEiP12653.

    Expressioni

    Tissue specificityi

    Expressed in the stem and leaves, lower levels are seen in the pollen and endosperm.

    Interactioni

    Subunit structurei

    Homodimer or heterodimer of GST-I and GST-IV (=GST-II).2 Publications

    Structurei

    Secondary structure

    1
    214
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 85
    Beta strandi10 – 145
    Helixi15 – 2511
    Beta strandi29 – 324
    Turni36 – 394
    Helixi40 – 423
    Helixi44 – 474
    Beta strandi57 – 604
    Beta strandi63 – 675
    Helixi68 – 7912
    Helixi81 – 844
    Turni85 – 873
    Helixi89 – 10416
    Helixi106 – 11712
    Helixi119 – 1224
    Helixi129 – 15224
    Beta strandi154 – 1607
    Helixi163 – 1664
    Helixi169 – 1757
    Helixi179 – 1868
    Helixi188 – 19912
    Helixi201 – 2099

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AXDX-ray2.50A/B2-210[»]
    1BYEX-ray2.80A/B/C/D2-214[»]
    ProteinModelPortaliP12653.
    SMRiP12653. Positions 2-214.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12653.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8382GST N-terminalAdd
    BLAST
    Domaini88 – 214127GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni41 – 422Glutathione binding
    Regioni54 – 552Glutathione binding
    Regioni67 – 682Glutathione binding

    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.

    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.

    P12653-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPMKLYGAV MSWNLTRCAT ALEEAGSDYE IVPINFATAE HKSPEHLVRN    50
    PFGQVPALQD GDLYLFESRA ICKYAARKNK PELLREGNLE EAAMVDVWIE 100
    VEANQYTAAL NPILFQVLIS PMLGGTTDQK VVDENLEKLK KVLEVYEARL 150
    TKCKYLAGDF LSLADLNHVS VTLCLFATPY ASVLDAYPHV KAWWSGLMER 200
    PSVQKVAALM KPSA 214
    Length:214
    Mass (Da):23,822
    Last modified:January 23, 2007 - v4
    Checksum:i97DA6337ADF03CB1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151L → V in AAA33470. 1 PublicationCurated
    Sequence conflicti15 – 151L → V in AAA33469. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06754 mRNA. Translation: CAA29928.1.
    M16901 mRNA. Translation: AAA33470.1.
    M16902, M16900 Genomic DNA. Translation: AAA33469.1.
    PIRiS03726. XUZM1.
    RefSeqiNP_001105412.1. NM_001111942.1.
    UniGeneiZm.9.

    Genome annotation databases

    GeneIDi542366.
    KEGGizma:542366.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X06754 mRNA. Translation: CAA29928.1 .
    M16901 mRNA. Translation: AAA33470.1 .
    M16902 , M16900 Genomic DNA. Translation: AAA33469.1 .
    PIRi S03726. XUZM1.
    RefSeqi NP_001105412.1. NM_001111942.1.
    UniGenei Zm.9.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AXD X-ray 2.50 A/B 2-210 [» ]
    1BYE X-ray 2.80 A/B/C/D 2-214 [» ]
    ProteinModelPortali P12653.
    SMRi P12653. Positions 2-214.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P12653.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 542366.
    KEGGi zma:542366.

    Organism-specific databases

    Gramenei P12653.
    MaizeGDBi 65344.

    Phylogenomic databases

    HOGENOMi HOG000125746.
    KOi K00799.

    Enzyme and pathway databases

    SABIO-RK P12653.

    Miscellaneous databases

    EvolutionaryTracei P12653.

    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. "Characterization and heterospecific expression of cDNA clones of genes in the maize GSH S-transferase multigene family."
      Grove G., Zarlengo R.P., Timmerman K.P., Li N.-Q., Tam M.F., Tu C.-P.D.
      Nucleic Acids Res. 16:425-438(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Structural analysis of a maize gene coding for glutathione-S-transferase involved in herbicide detoxification."
      Shah D.M., Hironaka C.M., Wiegand R.C., Harding E.I., Krivi G.G., Tiemeier D.C.
      Plant Mol. Biol. 6:203-211(1986)
      [AGRICOLA] [Europe PMC]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Messenger RNA encoding a glutathione-S-transferase responsible for herbicide tolerance in maize is induced in response to safener treatment."
      Wiegand R.C., Shah D.M., Mozer T.J., Harding E.I., Diaz-Collier J., Saunders C., Jaworski E.G., Tiemeier D.C.
      Plant Mol. Biol. 7:235-243(1986)
      [AGRICOLA] [Europe PMC]
      Cited for: PROTEIN SEQUENCE OF 2-16.
    4. "Crystal structure of herbicide-detoxifying maize glutathione S-transferase-I in complex with lactoylglutathione: evidence for an induced-fit mechanism."
      Neuefeind T., Huber R., Dasenbrock H., Prade L., Bieseler B.
      J. Mol. Biol. 274:446-453(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH LACTOYLGLUTATHIONE, SUBUNIT.
    5. "Structures of herbicides in complex with their detoxifying enzyme glutathione S-transferase -- explanations for the selectivity of the enzyme in plants."
      Prade L., Huber R., Bieseler B.
      Structure 6:1445-1452(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH ATRAZINE-GLUTATHIONE CONJUGATE.

    Entry informationi

    Entry nameiGSTF1_MAIZE
    AccessioniPrimary (citable) accession number: P12653
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 101 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3