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Q43621

- GSHRC_PEA

UniProt

Q43621 - GSHRC_PEA

Protein

Glutathione reductase, cytosolic

Gene
N/A
Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Maintains high levels of reduced glutathione in the cytosol. May play a role in the restoration of the post-stress redox state of the cytosolic glutathione pool.

    Catalytic activityi

    2 glutathione + NADP+ = glutathione disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei233 – 2331NADPBy similarity
    Binding sitei239 – 2391NADPBy similarity
    Active sitei471 – 4711Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi63 – 7210FADBy similarity

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. glutathione-disulfide reductase activity Source: UniProtKB-EC
    3. NADP binding Source: InterPro

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. glutathione metabolic process Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione reductase, cytosolic (EC:1.8.1.7)
    Short name:
    GR
    Short name:
    GRase
    Alternative name(s):
    GOR2
    OrganismiPisum sativum (Garden pea)
    Taxonomic identifieri3888 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 498498Glutathione reductase, cytosolicPRO_0000067964Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi72 ↔ 77Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiQ43621.

    Expressioni

    Inductioni

    Increased expression in the recovery (post-stress) phases of both drought and chilling.

    Structurei

    3D structure databases

    ProteinModelPortaliQ43621.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006324. Glut-diS_reduct.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    [Graphical view]
    PfamiPF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    SUPFAMiSSF55424. SSF55424. 1 hit.
    TIGRFAMsiTIGR01424. gluta_reduc_2. 1 hit.
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q43621-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARKMLNDGE PDLKKGEEQG KVYDFDLFII GAGSGGVRAA RFSSNFGAKV    50
    GICELPFHPI SSETIGGVGG TCVIRGCVPK KILVYGASYG GELQDARNFG 100
    WELNENVDFN WKKLLQKKTD EINRLNGIYK RLLSNAGVKL FEGEGKIASP 150
    NEVEVTQLDG TKLSYSAKHI LIATGSRAQR PNIPGQELGI TSDEALSLEE 200
    FPKRAVILGG GYIAVEFASI WRGMGSSVNL VFRKELPLRG FDDEMRAVVA 250
    RNLEGRGINL HPRTNLAQLI KTEDGIKVIT DHGEELIADV VLFATGRSPN 300
    SKRLNLEKVG VEFDKAGAIV VDEYSRTNIP SIWAVGDVTN RLNLTPVALM 350
    EASLFAKTVF GGQASKPDYN DIPYAVFCIP PLSVVGLSEE QAVEQTKGDV 400
    LIFTSTFNPM KNTISGRQEK TVMKLVVDAQ TDKVLGASMC GPDAPEIVQG 450
    IAIAIKCGAT KAQFDSTVGI HPSSAEEFVT MRSETRRVTG GVKPKTNL 498
    Length:498
    Mass (Da):53,897
    Last modified:November 1, 1997 - v1
    Checksum:i19AD08959764C6D0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98274 mRNA. Translation: CAA66924.1.
    PIRiT06442.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98274 mRNA. Translation: CAA66924.1 .
    PIRi T06442.

    3D structure databases

    ProteinModelPortali Q43621.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q43621.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006324. Glut-diS_reduct.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR012999. Pyr_OxRdtase_I_AS.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    [Graphical view ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    SUPFAMi SSF55424. SSF55424. 1 hit.
    TIGRFAMsi TIGR01424. gluta_reduc_2. 1 hit.
    PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterisation of a cytosolic glutathione reductase cDNA from pea (Pisum sativum L.) and its expression in response to stress."
      Stevens R.G., Greissen G.P., Mullineaux P.M.
      Plant Mol. Biol. 35:641-654(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Birte.
      Tissue: Leaf.

    Entry informationi

    Entry nameiGSHRC_PEA
    AccessioniPrimary (citable) accession number: Q43621
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 89 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond.

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3