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Q43154

- GSHRP_SPIOL

UniProt

Q43154 - GSHRP_SPIOL

Protein

Glutathione reductase, chloroplastic

Gene
N/A
Organism
Spinacia oleracea (Spinach)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 88 (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 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 sitei224 – 2241NADPBy similarity
    Binding sitei230 – 2301NADPBy similarity
    Active sitei462 – 4621Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi54 – 6310FADBy 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 (EC:1.8.1.7)
    Short name:
    GR
    Short name:
    GRase
    OrganismiSpinacia oleracea (Spinach)
    Taxonomic identifieri3562 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeCaryophyllalesAmaranthaceaeChenopodioideaeAnserineaeSpinacia

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei‹1 – 2›2ChloroplastSequence Analysis
    Chaini3 – 489487Glutathione reductase, chloroplasticPRO_0000030283Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi63 ↔ 68Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliQ43154.
    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: Fragment.

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

    Q43154-1 [UniParc]FASTAAdd to Basket

    « Hide

    EDNHSTVEDD AANYDFDLFV IGAGSGGVRA ARFSANLGAK VGICELPFHP    50
    ISSEVIGGVG GTCVIRGCVP KKILVYGASF GGELEDAKNY GWELNEKIDF 100
    NWKKLLQKKT DEIIRLNNIY KRLLSNAGVK LYEGEGKIVG PNEVQVTQLD 150
    GTKLSYSAKH ILIATGSRAQ RPNIPGQELA ITSDEALSLE EFPKRVVILG 200
    GGYISVEFAS IWRGMGADVN LCFRKELPLR GFDDEMRAAV ARNLEGRGVN 250
    VHPRTTLTEL VKTDGGVVAR TDHGEEIEAD VVLFATGRSP NTKRLNLEAL 300
    GVELDRTGAV KVDEYSRTSV PSIWAIGDVT NRMNLTPVAL MEGTCFAKTV 350
    FGGQNSKPDY SNIACAVFSI PPLAVVGLSE EQAIEQASGD ILVFTSSFNP 400
    MKNTISGRQE KTIMKLVVDA ETDKVLGASM CGPDAAEIMQ GIAIALKFGA 450
    TKAQFDSTVG IHPSAAEEFV TMREPSRRVP GAGKPKTNL 489
    Length:489
    Mass (Da):52,611
    Last modified:November 1, 1997 - v1
    Checksum:i970FC5B079A72CCD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D37870 mRNA. Translation: BAA07108.1.
    PIRiT09151.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D37870 mRNA. Translation: BAA07108.1 .
    PIRi T09151.

    3D structure databases

    ProteinModelPortali Q43154.
    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. Aono M., Fujiyama K., Sano T., Tanaka K.
      Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. New Asia.
      Tissue: Leaf.

    Entry informationi

    Entry nameiGSHRP_SPIOL
    AccessioniPrimary (citable) accession number: Q43154
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 88 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