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Q6FRV2

- GSHR_CANGA

UniProt

Q6FRV2 - GSHR_CANGA

Protein

Glutathione reductase

Gene

GLR1

Organism
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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      Entry version 72 (01 Oct 2014)
      Sequence version 1 (19 Jul 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 sitei465 – 4651Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi46 – 549FADBy 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:CAGL0H05665g
    OrganismiCandida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata)
    Taxonomic identifieri284593 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeNakaseomycesmitosporic Nakaseomyces
    ProteomesiUP000002428: Chromosome H

    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 – 476476Glutathione reductasePRO_0000067966Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 59Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliQ6FRV2.
    SMRiQ6FRV2. Positions 15-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    HOGENOMiHOG000276712.
    KOiK00383.
    OMAiGTNSDGF.
    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.

    Q6FRV2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIVKRLFRTM APVAKHFDYL VIGGGSGGVA SSRRAASYGA KTLLIEGKAL    50
    GGTCVNVGCV PKKVMWYASD LATRLTHAHE YGLAQNVPLS KESITFNWPE 100
    FKKKRDAYIH RLNGIYENNL KKEGVEVVFG WAKFNKDGNV EVTKHDNTTE 150
    VYSADRILVA TGGKPVYPEK VPGFELGTDS DGFFRLEEQP KKVVVVGAGY 200
    IGIELAGVFH GLGSDSHLVI RGKTVLRKFD EIIQNTVTDY YVEEGINVHK 250
    ETNVDKVEKD EKTGKLSVHL TNGQVLEDVD ELIWTMGRRS LLGIGLENVG 300
    VKLNDKEQII TDEYQNTNVP NIYSLGDVSG RVELTPVAIA AGRKLSNRLF 350
    GPEQYRNDKL DYTNVPSVVF SHPEAGSIGL TEDEAIKQYG KDNIKVYTSK 400
    FTAMYYAMLE HKSPTRYKII CEGPNEKVVG LHIVGDSSAE ILQGFGVAIK 450
    MGATKADFDN CVAIHPTSAE ELVTMR 476
    Length:476
    Mass (Da):52,499
    Last modified:July 19, 2004 - v1
    Checksum:iBA4793D0F077D14D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR380954 Genomic DNA. Translation: CAG59975.1.
    RefSeqiXP_447042.1. XM_447042.1.

    Genome annotation databases

    GeneIDi2888553.
    KEGGicgr:CAGL0H05665g.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR380954 Genomic DNA. Translation: CAG59975.1 .
    RefSeqi XP_447042.1. XM_447042.1.

    3D structure databases

    ProteinModelPortali Q6FRV2.
    SMRi Q6FRV2. Positions 15-476.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2888553.
    KEGGi cgr:CAGL0H05665g.

    Phylogenomic databases

    HOGENOMi HOG000276712.
    KOi K00383.
    OMAi GTNSDGF.
    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_CANGA
    AccessioniPrimary (citable) accession number: Q6FRV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 72 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