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P41921

- GSHR_YEAST

UniProt

P41921 - GSHR_YEAST

Protein

Glutathione reductase

Gene

GLR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei472 – 4721Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi53 – 619FADBy similarity

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. glutathione-disulfide reductase activity Source: SGD
    3. NADP binding Source: InterPro

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. cellular response to oxidative stress Source: SGD
    3. glutathione metabolic process Source: InterPro
    4. protein glutathionylation Source: SGD

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    BioCyciYEAST:YPL091W-MONOMER.
    ReactomeiREACT_191152. Detoxification of Reactive Oxygen Species.

    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:YPL091W
    ORF Names:LPG17W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XVI

    Organism-specific databases

    CYGDiYPL091w.
    SGDiS000006012. GLR1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 483483Glutathione reductasePRO_0000067972Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Disulfide bondi61 ↔ 66Redox-activeBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP41921.
    PaxDbiP41921.
    PeptideAtlasiP41921.

    2D gel databases

    COMPLUYEAST-2DPAGEP41921.

    Expressioni

    Gene expression databases

    GenevestigatoriP41921.

    Interactioni

    Protein-protein interaction databases

    BioGridi36090. 61 interactions.
    DIPiDIP-4020N.
    IntActiP41921. 3 interactions.
    MINTiMINT-484403.
    STRINGi4932.YPL091W.

    Structurei

    Secondary structure

    1
    483
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi23 – 297
    Helixi33 – 4412
    Beta strandi49 – 557
    Helixi59 – 646
    Helixi66 – 8217
    Turni83 – 897
    Helixi98 – 1003
    Helixi105 – 12925
    Beta strandi132 – 14110
    Beta strandi147 – 1548
    Beta strandi157 – 16610
    Beta strandi170 – 1723
    Helixi181 – 1833
    Helixi187 – 1926
    Beta strandi198 – 2036
    Helixi207 – 21812
    Beta strandi222 – 2265
    Beta strandi228 – 2325
    Helixi238 – 25114
    Beta strandi254 – 2563
    Beta strandi261 – 2666
    Beta strandi273 – 2775
    Beta strandi282 – 29110
    Beta strandi295 – 2973
    Helixi303 – 3064
    Beta strandi329 – 3313
    Helixi333 – 3353
    Helixi342 – 35716
    Helixi360 – 3623
    Beta strandi374 – 3763
    Beta strandi382 – 3865
    Helixi389 – 3968
    Helixi398 – 4003
    Beta strandi401 – 4088
    Helixi411 – 4155
    Beta strandi422 – 4298
    Turni430 – 4334
    Beta strandi434 – 4429
    Helixi445 – 45713
    Helixi462 – 4665
    Helixi476 – 4805

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HQMX-ray2.40A/B17-483[»]
    ProteinModelPortaliP41921.
    SMRiP41921. Positions 22-483.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP41921.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.
    GeneTreeiENSGT00390000007578.
    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.

    P41921-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLSATKQTFR SLQIRTMSTN TKHYDYLVIG GGSGGVASAR RAASYGAKTL    50
    LVEAKALGGT CVNVGCVPKK VMWYASDLAT RVSHANEYGL YQNLPLDKEH 100
    LTFNWPEFKQ KRDAYVHRLN GIYQKNLEKE KVDVVFGWAR FNKDGNVEVQ 150
    KRDNTTEVYS ANHILVATGG KAIFPENIPG FELGTDSDGF FRLEEQPKKV 200
    VVVGAGYIGI ELAGVFHGLG SETHLVIRGE TVLRKFDECI QNTITDHYVK 250
    EGINVHKLSK IVKVEKNVET DKLKIHMNDS KSIDDVDELI WTIGRKSHLG 300
    MGSENVGIKL NSHDQIIADE YQNTNVPNIY SLGDVVGKVE LTPVAIAAGR 350
    KLSNRLFGPE KFRNDKLDYE NVPSVIFSHP EAGSIGISEK EAIEKYGKEN 400
    IKVYNSKFTA MYYAMLSEKS PTRYKIVCAG PNEKVVGLHI VGDSSAEILQ 450
    GFGVAIKMGA TKADFDNCVA IHPTSAEELV TMR 483
    Length:483
    Mass (Da):53,441
    Last modified:October 1, 1996 - v2
    Checksum:i203BBB770120504A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti315 – 3151Q → E in BAA07109. 1 PublicationCurated
    Sequence conflicti428 – 4281C → G in BAA07109. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35342 Genomic DNA. Translation: AAA92575.1.
    U43281 Genomic DNA. Translation: AAB68208.1.
    D37871 mRNA. Translation: BAA07109.1.
    BK006949 Genomic DNA. Translation: DAA11342.1.
    PIRiS61975.
    RefSeqiNP_015234.1. NM_001183905.1.

    Genome annotation databases

    EnsemblFungiiYPL091W; YPL091W; YPL091W.
    GeneIDi856014.
    KEGGisce:YPL091W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L35342 Genomic DNA. Translation: AAA92575.1 .
    U43281 Genomic DNA. Translation: AAB68208.1 .
    D37871 mRNA. Translation: BAA07109.1 .
    BK006949 Genomic DNA. Translation: DAA11342.1 .
    PIRi S61975.
    RefSeqi NP_015234.1. NM_001183905.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HQM X-ray 2.40 A/B 17-483 [» ]
    ProteinModelPortali P41921.
    SMRi P41921. Positions 22-483.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36090. 61 interactions.
    DIPi DIP-4020N.
    IntActi P41921. 3 interactions.
    MINTi MINT-484403.
    STRINGi 4932.YPL091W.

    Chemistry

    BindingDBi P41921.
    ChEMBLi CHEMBL4119.

    2D gel databases

    COMPLUYEAST-2DPAGE P41921.

    Proteomic databases

    MaxQBi P41921.
    PaxDbi P41921.
    PeptideAtlasi P41921.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YPL091W ; YPL091W ; YPL091W .
    GeneIDi 856014.
    KEGGi sce:YPL091W.

    Organism-specific databases

    CYGDi YPL091w.
    SGDi S000006012. GLR1.

    Phylogenomic databases

    eggNOGi COG1249.
    GeneTreei ENSGT00390000007578.
    HOGENOMi HOG000276712.
    KOi K00383.
    OMAi GTNSDGF.
    OrthoDBi EOG79W9F2.

    Enzyme and pathway databases

    BioCyci YEAST:YPL091W-MONOMER.
    Reactomei REACT_191152. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    EvolutionaryTracei P41921.
    NextBioi 980908.
    PROi P41921.

    Gene expression databases

    Genevestigatori P41921.

    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...

    Publicationsi

    1. "Isolation, characterization and overexpression of the yeast gene, GLR1, encoding glutathione reductase."
      Collinson L.P., Dawes I.W.
      Gene 156:123-127(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 17-483.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
      , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
      Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Aono M., Nakajima N.
      Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE OF 20-483.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiGSHR_YEAST
    AccessioniPrimary (citable) accession number: P41921
    Secondary accession number(s): D6W3S6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 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.
    Present with 7600 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    External Data

    Dasty 3