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P27456

- GSHRP_PEA

UniProt

P27456 - GSHRP_PEA

Protein

Glutathione reductase, chloroplastic/mitochondrial

Gene

GR

Organism
Pisum sativum (Garden pea)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Maintains high levels of reduced glutathione in the chloroplast.

    Catalytic activityi

    2 glutathione + NADP+ = glutathione disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei277 – 2771NADPBy similarity
    Binding sitei283 – 2831NADPBy similarity
    Active sitei515 – 5151Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi112 – 12110FADBy 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, chloroplastic/mitochondrial (EC:1.8.1.7)
    Short name:
    GR
    Short name:
    GRase
    Alternative name(s):
    GOR1
    Gene namesi
    Name:GR
    Synonyms:GOR1
    OrganismiPisum sativum (Garden pea)
    Taxonomic identifieri3888 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideaeFabeaePisum

    Subcellular locationi

    Plastidchloroplast 1 Publication. Mitochondrion 1 Publication
    Note: The majority of the protein is found in chloroplast, with only 3% in mitochondria.

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell
    2. mitochondrion Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Mitochondrion, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 6060Chloroplast and mitochondrionSequence AnalysisAdd
    BLAST
    Chaini61 – 552492Glutathione reductase, chloroplastic/mitochondrialPRO_0000030281Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi121 ↔ 126Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliP27456.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center, Transit peptide

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P27456-1 [UniParc]FASTAAdd to Basket

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    MNQAMATPLS LSCCSPTLTR STLFFTKTFP FSRSFSTPLP LSTKTLISLS    50
    PPHRTFAVRA ESQNGADPAR QYDFDLFTIG AGSGGVRASR FASNFGASSA 100
    VCELPFSTIS SDTTGGVGGT CVIRGCVPKK LLVYASKFSH EFEESNGFGW 150
    RYDSEPKHDW SSLIANKNAE LQRLTGIYKN TLKNAGVKLI EGRGKIVDAH 200
    TVDVDGKLYS AKHILVSVGG RPFIPDIPGK EYAIDSDAAL DLPSKPQKIA 250
    IVGGGYIALE FAGIFNGLKS EVHVFIRQKK VLRGFDEEIR DFVAENMALR 300
    GIEFHTEESP VAITKAADGS LSLKTNKGTE EGFSHIMFAT GRSPNTKDLG 350
    LESVGVKVAK DGSIEVDEYS QTSVPSIWAI GDATNRVNLT PVALMEGVAL 400
    AKTLFQNEPT KPDYRAIPSA VFSQPPIGGV GLTEEQAAEQ YGDIDVFTAN 450
    FRPMKATLSG LPDRVFMKLI VSAETNVVLG LHMCGEDAAE IAQGFAVGIK 500
    AGLTKADFDA TVGIHPTAAE EFVTMRTPTR KVRKNQASQG KSDSKAKAVA 550
    GS 552
    Length:552
    Mass (Da):59,108
    Last modified:August 1, 1992 - v1
    Checksum:i690D1058AE4168BC
    GO

    Sequence cautioni

    The sequence CAA42921.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60373 mRNA. Translation: CAA42921.1. Different initiation.
    X90996 Genomic DNA. Translation: CAA62482.1.
    PIRiS18973.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60373 mRNA. Translation: CAA42921.1 . Different initiation.
    X90996 Genomic DNA. Translation: CAA62482.1 .
    PIRi S18973.

    3D structure databases

    ProteinModelPortali P27456.
    ModBasei Search...
    MobiDBi Search...

    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. "Molecular characterization of glutathione reductase cDNAs from pea (Pisum sativum L.)."
      Creissen G., Edwards E.A., Enard C., Wellburn A., Mullineaux P.M.
      Plant J. 2:129-131(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leaf.
    2. "Characterisation of a glutathione reductase gene and its genetic locus from pea (Pisum sativum L.)."
      Mullineaux P.M., Enard C., Hellens R., Creissen G.
      Planta 200:186-194(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Birte.
    3. "Simultaneous targeting of pea glutathione reductase and of a bacterial fusion protein to chloroplasts and mitochondria in transgenic tobacco."
      Creissen G.P., Reynolds H., Xue Y., Mullineaux P.M.
      Plant J. 8:167-175(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiGSHRP_PEA
    AccessioniPrimary (citable) accession number: P27456
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 103 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