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P78965

- GSHR_SCHPO

UniProt

P78965 - GSHR_SCHPO

Protein

Glutathione reductase

Gene

pgr1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 2 (11 Jan 2001)
      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 sitei453 – 4531Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi37 – 4610FADBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. cellular response to menadione Source: PomBase
    3. cellular response to oxidative stress Source: PomBase
    4. glutathione metabolic process Source: PomBase

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    ReactomeiREACT_210617. Synthesis and interconversion of nucleotide di- and triphosphates.
    REACT_219607. 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:pgr1
    ORF Names:pi039, SPBC17A3.07
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC17A3.07.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. mitochondrion Source: PomBase

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 464464Glutathione reductasePRO_0000067970Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 51Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiP78965.
    PaxDbiP78965.

    Interactioni

    Protein-protein interaction databases

    BioGridi276692. 1 interaction.
    MINTiMINT-4691707.
    STRINGi4896.SPBC17A3.07-1.

    Structurei

    3D structure databases

    ProteinModelPortaliP78965.
    SMRiP78965. Positions 6-463.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.
    HOGENOMiHOG000276712.
    KOiK00383.
    OMAiLMRFKRT.
    OrthoDBiEOG79W9F2.
    PhylomeDBiP78965.

    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.

    P78965-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPISKVFDY LVIGGGSGGL ASARRAAKHG AKVALIEASG RLGGTCVNYG    50
    CVPKKIMWNI ADLVAKMKTA KQNGFPNSQL GSFDWGMIKR KRDAYIGRLN 100
    GIYERNVNKD GVAYISGHAS FVSPTEVAVD MNDGSGTQVF SAKYILIAVG 150
    GHPIWPSHIP GAEYGIDSDG FFELESQPKR VAIVGAGYIA VELAGVFAAL 200
    GTETHMFIRQ SKFLRKFDPI ISDGIMDHFQ HIGINVHTNS LEFKKVEKLP 250
    SGELCIHQQD GSTFNVDTLL WAIGRAPKIQ GLRLEKAGVK TLPNGIIIAD 300
    TYQRTNVPTV LSLGDVCGKL ELTPVAIAAG RRLSDRLFGG IKDAHLDYEE 350
    VPSVVFAHPE AGTIGLTEQE AIDKYGESQI KVYNTKFNGL NYSMVEQEDK 400
    VPTTYKLVCA GPLQKVVGLH LVGDFSAEIL QGFGVAIKMG ATKSDFDSCV 450
    AIHPTSAEEL VTLV 464
    Length:464
    Mass (Da):49,999
    Last modified:January 11, 2001 - v2
    Checksum:i2BFFEFD363A3F173
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti184 – 1841V → VV in AAC49809. (PubMed:9287302)Curated
    Sequence conflicti419 – 4246LHLVGD → PTFSWR in AAC49809. (PubMed:9287302)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63845 Genomic DNA. Translation: AAC49809.1.
    AB004537 Genomic DNA. Translation: BAA21419.1.
    CU329671 Genomic DNA. Translation: CAB51766.1.
    PIRiT39699.
    RefSeqiNP_595589.1. NM_001021485.2.

    Genome annotation databases

    EnsemblFungiiSPBC17A3.07.1; SPBC17A3.07.1:pep; SPBC17A3.07.
    GeneIDi2540156.
    KEGGispo:SPBC17A3.07.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U63845 Genomic DNA. Translation: AAC49809.1 .
    AB004537 Genomic DNA. Translation: BAA21419.1 .
    CU329671 Genomic DNA. Translation: CAB51766.1 .
    PIRi T39699.
    RefSeqi NP_595589.1. NM_001021485.2.

    3D structure databases

    ProteinModelPortali P78965.
    SMRi P78965. Positions 6-463.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 276692. 1 interaction.
    MINTi MINT-4691707.
    STRINGi 4896.SPBC17A3.07-1.

    Proteomic databases

    MaxQBi P78965.
    PaxDbi P78965.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC17A3.07.1 ; SPBC17A3.07.1:pep ; SPBC17A3.07 .
    GeneIDi 2540156.
    KEGGi spo:SPBC17A3.07.

    Organism-specific databases

    PomBasei SPBC17A3.07.

    Phylogenomic databases

    eggNOGi COG1249.
    HOGENOMi HOG000276712.
    KOi K00383.
    OMAi LMRFKRT.
    OrthoDBi EOG79W9F2.
    PhylomeDBi P78965.

    Enzyme and pathway databases

    Reactomei REACT_210617. Synthesis and interconversion of nucleotide di- and triphosphates.
    REACT_219607. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    NextBioi 20801291.
    PROi P78965.

    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, expression, and regulation of the pgr1(+) gene encoding glutathione reductase absolutely required for the growth of Schizosaccharomyces pombe."
      Lee J., Dawes I.W., Roe J.-H.
      J. Biol. Chem. 272:23042-23049(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    2. "A 38 kb segment containing the cdc2 gene from the left arm of fission yeast chromosome II: sequence analysis and characterization of the genomic DNA and cDNAs encoded on the segment."
      Machida M., Yamazaki S., Kunihiro S., Tanaka T., Kushida N., Jinno K., Haikawa Y., Yamazaki J., Yamamoto S., Sekine M., Oguchi A., Nagai Y., Sakai M., Aoki K., Ogura K., Kudoh Y., Kikuchi H., Zhang M.Q., Yanagida M.
      Yeast 16:71-80(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.
    3. "The genome sequence of Schizosaccharomyces pombe."
      Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
      , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
      Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 972 / ATCC 24843.

    Entry informationi

    Entry nameiGSHR_SCHPO
    AccessioniPrimary (citable) accession number: P78965
    Secondary accession number(s): O13631
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2001
    Last sequence update: January 11, 2001
    Last modified: October 1, 2014
    This is version 130 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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Schizosaccharomyces pombe
      Schizosaccharomyces pombe: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3