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Q6C5H4

- GSHR_YARLI

UniProt

Q6C5H4 - GSHR_YARLI

Protein

Glutathione reductase

Gene

GLR1

Organism
Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (16 Aug 2004)
      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 sitei459 – 4591Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi36 – 449FADBy 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 (EC:1.8.1.7)
    Short name:
    GR
    Short name:
    GRase
    Gene namesi
    Name:GLR1
    Ordered Locus Names:YALI0E18029g
    OrganismiYarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica)
    Taxonomic identifieri284591 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesDipodascaceaeYarrowia
    ProteomesiUP000001300: 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 – 470470Glutathione reductasePRO_0000067971Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi44 ↔ 49Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    STRINGi4952.Q6C5H4.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6C5H4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.
    HOGENOMiHOG000276712.
    KOiK00383.
    OMAiLMRFKRT.
    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.

    Q6C5H4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASIPHYDYL VIGGGSGGVA SARRAASYGA KTLLIEGKAL GGTCVNVGCV    50
    PKKVMWNASD LAGRIRQAKE YGFPDVDPKY ADNFDWSGFK AKRDAYVKRL 100
    NGIYERNLQK EGVEYVFGWA TLYKQEGQEF PLVHVKSDDG NTKLYSAKKI 150
    MIATGGKPRL PDVPGAEYGI DSDGFFALET QPKRVAVVGG GYIGVELAGV 200
    FHGLNSETTL FCRGQTVLRA FDIMIQDTIT DYYVKEGINV LKGSGVKKIV 250
    KKDNGELLVT YEQDGAEKDI TLDSLIWTIG REPLKDTLNL GEFGIKTNKR 300
    GYIEVDEYQR SSVDNIYSLG DVCGKVELTP MAIAAGRKLS NRLFGPTEFK 350
    NQKQDYTDVP SAVFSHPEVG SIGITEAAAK EQYGEENVKV YTSKFVAMYY 400
    AMLEEKAPTA YKLVCAGKDE KVVGLHIVGA DSAEILQGFG VAIRMGATKA 450
    DFDNVVAIHP TSAEELVTMR 470
    Length:470
    Mass (Da):51,302
    Last modified:August 16, 2004 - v1
    Checksum:iB9E4760F181DD143
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382131 Genomic DNA. Translation: CAG79681.1.
    RefSeqiXP_504088.1. XM_504088.1.

    Genome annotation databases

    EnsemblFungiiCAG79681; CAG79681; YALI0_E18029g.
    GeneIDi2911696.
    KEGGiyli:YALI0E18029g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR382131 Genomic DNA. Translation: CAG79681.1 .
    RefSeqi XP_504088.1. XM_504088.1.

    3D structure databases

    ProteinModelPortali Q6C5H4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 4952.Q6C5H4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CAG79681 ; CAG79681 ; YALI0_E18029g .
    GeneIDi 2911696.
    KEGGi yli:YALI0E18029g.

    Phylogenomic databases

    eggNOGi COG1249.
    HOGENOMi HOG000276712.
    KOi K00383.
    OMAi LMRFKRT.
    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_YARLI
    AccessioniPrimary (citable) accession number: Q6C5H4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 77 of the entry and version 1 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