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P11804

- GSHR_SPISP

UniProt

P11804 - GSHR_SPISP

Protein

Glutathione reductase

Gene
N/A
Organism
Spirulina sp.
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Maintains high levels of reduced glutathione in the cytosol.

    Catalytic activityi

    2 glutathione + NADP+ = glutathione disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi5 – 139FADBy similarity

    GO - Molecular functioni

    1. glutathione-disulfide reductase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione reductase (EC:1.8.1.7)
    Short name:
    GR
    Short name:
    GRase
    OrganismiSpirulina sp.
    Taxonomic identifieri1157 [NCBI]
    Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesSpirulina

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – ›58›58Glutathione reductasePRO_0000067978Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi13 ↔ 18Redox-active1 Publication

    Keywords - PTMi

    Disulfide bond

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Family and domain databases

    InterProiIPR012999. Pyr_OxRdtase_I_AS.
    [Graphical view]
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragments.

    P11804-1 [UniParc]FASTAAdd to Basket

    « Hide

    VAIAENSVVG GTCVIRGCVP KLTLTGDDTE PLIVDALLCA TGRTTQSNIF   50
    AVGDCTDR 58
    Length:58
    Mass (Da):5,952
    Last modified:October 1, 1989 - v1
    Checksum:iB2C2A050EF55B5EF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11
    Non-adjacent residuesi21 – 222Curated
    Non-adjacent residuesi43 – 442Curated
    Non-terminal residuei58 – 581

    Sequence databases

    PIRiPX0017.

    Cross-referencesi

    Sequence databases

    PIRi PX0017.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR012999. Pyr_OxRdtase_I_AS.
    [Graphical view ]
    PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequence studies of cysteinyl peptides from Spirulina glutathione reductase: comparison of active site cysteine peptides with those of other flavoprotein disulfide oxidoreductases."
      Cui J.-Y., Wakabayashi S., Wada K., Fukuyama K., Matsubara H.
      J. Biochem. 105:390-394(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, DISULFIDE BOND.

    Entry informationi

    Entry nameiGSHR_SPISP
    AccessioniPrimary (citable) accession number: P11804
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 61 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond.

    Keywords - Technical termi

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3