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Q6BPI1

- GSHR_DEBHA

UniProt

Q6BPI1 - GSHR_DEBHA

Protein

Glutathione reductase

Gene

GLR1

Organism
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 73 (01 Oct 2014)
      Sequence version 3 (16 Dec 2008)
      Previous versions | rss
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    Functioni

    Maintains high levels of reduced glutathione in the cytosol.By similarity

    Catalytic activityi

    2 glutathione + NADP+ = glutathione disulfide + NADPH.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei479 – 4791Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi39 – 4911FADBy similarityAdd
    BLAST

    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 (EC:1.8.1.7)
    Short name:
    GR
    Short name:
    GRase
    Gene namesi
    Name:GLR1
    Ordered Locus Names:DEHA2E13442g
    OrganismiDebaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii)
    Taxonomic identifieri284592 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDebaryomycetaceaeDebaryomyces
    ProteomesiUP000000599: Chromosome E

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 490490Glutathione reductasePRO_0000067967Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi49 ↔ 54Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    STRINGi4959.Q6BPI1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6BPI1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.
    HOGENOMiHOG000276712.
    KOiK00383.
    OrthoDBiEOG79W9F2.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006322. Glutathione_Rdtase_euk/bac.
    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.
    TIGRFAMsiTIGR01421. gluta_reduc_1. 1 hit.
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6BPI1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPLQAIRKY DYLVIGGGSG GVASARRAAS YGAKVLLIES KFNKMGGTCV    50
    NVGCVPKKVM WYAGDLAEKR HHLKSYGLST TDDKVKYGDF DWSTFKDKRD 100
    AYVKRLNGIY ERNLKNEGVD YIYGFAHFAN SNGDVEVTLT GDQELSFLEE 150
    GKEFKKDEKL VFAGSKTLIA TGGYAINPPN VEGHELGTTS DGFFELQKQP 200
    KSVAVVGAGY IGVELSGIFK ALGSETHLVI RGDTVLRSFD ESIQNSITDY 250
    YTDKLGVNII KQSGSVSKVE KIDGDRKKIT LGNGQVLEVD ELIWTMGRKS 300
    LINIGLDKVG VTLNDKQQVD VDQFQQTANP NIFSLGDVIG KVELTPVAIA 350
    AGRRLSNRLF SGDKAFENDH LDYSNVPSVI FSHPEAGSIG LSCKEAKEKY 400
    GEDQIKIYKS KFNAMYYAMM EDDSLKSPTS YKVVCAGEDE KVVGLHIVGD 450
    SSAEILQGFG VAIKMGATKK DFDSCVAIHP TSAEELVTMK 490
    Length:490
    Mass (Da):53,520
    Last modified:December 16, 2008 - v3
    Checksum:i1076F6EDB4389EAE
    GO

    Sequence cautioni

    The sequence CAG88130.2 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382137 Genomic DNA. Translation: CAG88130.2. Different initiation.
    RefSeqiXP_459889.2. XM_459889.2.

    Genome annotation databases

    GeneIDi2902393.
    KEGGidha:DEHA2E13442g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382137 Genomic DNA. Translation: CAG88130.2 . Different initiation.
    RefSeqi XP_459889.2. XM_459889.2.

    3D structure databases

    ProteinModelPortali Q6BPI1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 4959.Q6BPI1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2902393.
    KEGGi dha:DEHA2E13442g.

    Phylogenomic databases

    eggNOGi COG1249.
    HOGENOMi HOG000276712.
    KOi K00383.
    OrthoDBi EOG79W9F2.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR006322. Glutathione_Rdtase_euk/bac.
    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 TIGR01421. gluta_reduc_1. 1 hit.
    PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Entry informationi

    Entry nameiGSHR_DEBHA
    AccessioniPrimary (citable) accession number: Q6BPI1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 73 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3