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Q60151

- GSHR_STRTR

UniProt

Q60151 - GSHR_STRTR

Protein

Glutathione reductase

Gene

gor

Organism
Streptococcus thermophilus
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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 sitei439 – 4391Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi34 – 429FADBy 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:gor
    OrganismiStreptococcus thermophilus
    Taxonomic identifieri1308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 450450Glutathione reductasePRO_0000067979Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi42 ↔ 47Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ60151.
    SMRiQ60151. Positions 3-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    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.

    Q60151-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKEYDYIVI GGGSGGIASA NRAAMHGAKV ILFEGKEVGG TCVNVGCVPK    50
    KVMWYGAQVA ETLHRYAGEY GFDVTINNFD FATLKANRQA YIDRIHGSFE 100
    RGFDSNGVER VYEYARFVDP HTVEVAGELY TAPHILIATG GHPLYPNIPG 150
    SEYGITSDGF FELDEVPKRT AVIGAGYIAV EVAGVLNALG SDTHLFVRKD 200
    RPLRTFDKDI IDVLVDEMAK SGPTLHMHAN ATEVVKNADD SLTISFDNEE 250
    TITVDCLIWA VGRAANTSGF GLEKTGVELT ERGNIYSDEF ENTSVPGIYA 300
    LGDVTGKLDL TPVAVKAGRQ LSERLFNNKV DAKLDYTDVA TVVFSHPAIG 350
    AIGLTEEKAI AKYGAENIKV YKSSFTPMYT ALGDNRQLST MKLVTLGEDE 400
    KIIGLHGIGY GVDEMIQGFS VAIKMGATKA DFDNTVAIHP TGSEEFVTMR 450
    Length:450
    Mass (Da):48,712
    Last modified:November 1, 1996 - v1
    Checksum:i6A0DA46BEA828804
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27672 Genomic DNA. Translation: AAB00353.1.
    Z29494 Genomic DNA. Translation: CAA82630.1.
    PIRiS41386.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27672 Genomic DNA. Translation: AAB00353.1 .
    Z29494 Genomic DNA. Translation: CAA82630.1 .
    PIRi S41386.

    3D structure databases

    ProteinModelPortali Q60151.
    SMRi Q60151. Positions 3-450.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "Characterization of the gor gene of the lactic acid bacterium Streptococcus thermophilus CNRZ368."
      Pebay M., Holl A.-C., Simonet J.-M., Decaris B.
      Res. Microbiol. 146:371-383(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CNRZ 368.

    Entry informationi

    Entry nameiGSHR_STRTR
    AccessioniPrimary (citable) accession number: Q60151
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 91 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond.

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3