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Q873E8

- GSHR_NEUCR

UniProt

Q873E8 - GSHR_NEUCR

Protein

Glutathione reductase

Gene

gtr-1

Organism
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 81 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      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 sitei457 – 4571Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi38 – 469FADBy 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. cellular response to oxidative stress Source: EnsemblFungi
    3. glutathione metabolic process Source: InterPro
    4. protein glutathionylation Source: EnsemblFungi

    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:gtr-1
    Synonyms:glr1
    ORF Names:B10C3.130, NCU03339
    OrganismiNeurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
    Taxonomic identifieri367110 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesSordariaceaeNeurospora
    ProteomesiUP000001805: Chromosome 6, Linkage Group II

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. mitochondrion Source: EnsemblFungi
    2. nucleus Source: EnsemblFungi

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 468468Glutathione reductasePRO_0000067969Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    STRINGi5141.NCU03339.1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ873E8.
    SMRiQ873E8. Positions 6-468.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.
    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.

    Q873E8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPISRETDF LVIGGGSGGI ATARAAAGKY GIKSMVVEGK RLGGTCVNVG    50
    CVPKKVTFYA ALVAETIHQA KDYGFSVEQT APFDWPTFKQ KRDAYVARLN 100
    GIYERNLAND KVEYVHGWAK LLSPNSVEVT LDDGTKSVVN AKKILIAVGG 150
    NPTIPPHIPG SEYGTNSDGF FDIDTLPKKV ALVGAGYIAV EFAGMLNALG 200
    VETHLFIRHD TFLRSFDPMI QQVSVKEYER IGVKVHKKSQ LTSVQKDAAG 250
    KLAINFKEGE GEQSISDVDH LIWAVGRTPA VEGLGLDKAG VKTNEKGYIE 300
    VDEYQNTSTE NIYAVGDVCG QVELTPVAIA AGRKLAARLF GPEEFRTLKL 350
    NYDNVPSVVF AHPEIGSIGL TEPEAVAKYG AENLKIYKSS FTAMYYAMMK 400
    PEDKAPTAYK LICAGPEEKV VGLHIIGLGS GEILQGFGVA VNMGATKADF 450
    DNCVAIHPTS AEELVTLK 468
    Length:468
    Mass (Da):50,313
    Last modified:June 1, 2003 - v1
    Checksum:iA3802C1A7DC0B479
    GO

    Sequence cautioni

    The sequence ESA43520.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence ESA43521.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX284749 Genomic DNA. Translation: CAD70360.1.
    CM002237 Genomic DNA. Translation: ESA43520.1. Different initiation.
    CM002237 Genomic DNA. Translation: ESA43521.1. Different initiation.
    RefSeqiXP_956448.1. XM_951355.1.
    UniGeneiNcr.16209.

    Genome annotation databases

    EnsemblFungiiEFNCRT00000002546; EFNCRP00000002546; EFNCRG00000002543.
    GeneIDi3872613.
    KEGGincr:NCU03339.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX284749 Genomic DNA. Translation: CAD70360.1 .
    CM002237 Genomic DNA. Translation: ESA43520.1 . Different initiation.
    CM002237 Genomic DNA. Translation: ESA43521.1 . Different initiation.
    RefSeqi XP_956448.1. XM_951355.1.
    UniGenei Ncr.16209.

    3D structure databases

    ProteinModelPortali Q873E8.
    SMRi Q873E8. Positions 6-468.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5141.NCU03339.1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii EFNCRT00000002546 ; EFNCRP00000002546 ; EFNCRG00000002543 .
    GeneIDi 3872613.
    KEGGi ncr:NCU03339.

    Phylogenomic databases

    eggNOGi COG1249.
    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...

    Publicationsi

    1. "What's in the genome of a filamentous fungus? Analysis of the Neurospora genome sequence."
      Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D., Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.
      Nucleic Acids Res. 31:1944-1954(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.
    2. "The genome sequence of the filamentous fungus Neurospora crassa."
      Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B., Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.
      , Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D., Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D., Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A., DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R., Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R., Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.
      Nature 422:859-868(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987.

    Entry informationi

    Entry nameiGSHR_NEUCR
    AccessioniPrimary (citable) accession number: Q873E8
    Secondary accession number(s): Q1K529, V5IP83
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 81 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