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P23189

- GSHR_PSEAE

UniProt

P23189 - GSHR_PSEAE

Protein

Glutathione reductase

Gene

gor

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Nov 1991)
      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 sitei436 – 4361Proton 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

    GO - Biological processi

    1. cell redox homeostasis 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
    Ordered Locus Names:PA2025
    OrganismiPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
    Taxonomic identifieri208964 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
    ProteomesiUP000002438: Chromosome

    Organism-specific databases

    PseudoCAPiPA2025.

    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 – 451451Glutathione reductasePRO_0000067977Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi208964.PA2025.

    Structurei

    3D structure databases

    ProteinModelPortaliP23189.
    SMRiP23189. Positions 2-450.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.
    HOGENOMiHOG000276712.
    KOiK00383.
    OMAiHRQPCKM.
    OrthoDBiEOG6QCD6D.
    PhylomeDBiP23189.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    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.
    PROSITEiPS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P23189-1 [UniParc]FASTAAdd to Basket

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    MSFDFDLFVI GAGSGGVRAA RFAAGFGARV AVAESRYLGG TCVNVGCVPK    50
    KLLVYGAHFS EDFEQARAYG WSAGEAQFDW ATLIGNKNRE IQRLNGIYRN 100
    LLVNSGVTLL EGHARLLDAH SVEVDGQRFS AKHILVATGG WPQVPDIPGK 150
    EHAITSNEAF FLERLPRRVL VVGGGYIAVE FASIFNGLGA ETTLLYRRDL 200
    FLRGFDRSVR EHLRDELGKK GLDLQFNSDI ARIDKQADGS LAATLKDGRV 250
    LEADCVFYAT GRRPMLDDLG LENTAVKLTD KGFIAVDEHY QTSEPSILAL 300
    GDVIGRVQLT PVALAEGMAV ARRLFKPEEY RPVDYKLIPT AVFSLPNIGT 350
    VGLTEEEALS AGHKVKIFES RFRPMKLTLT DDQEKTLMKL VVDAHDDRVL 400
    GCHMVGAEAG EILQGIAVAM KAGATKQAFD ETIGIHPTAA EEFVTLRTPT 450
    R 451
    Length:451
    Mass (Da):49,237
    Last modified:November 1, 1991 - v1
    Checksum:i2924599996DB98EA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54201 Genomic DNA. Translation: CAA38122.1.
    AE004091 Genomic DNA. Translation: AAG05413.1.
    PIRiS15236.
    RefSeqiNP_250715.1. NC_002516.2.

    Genome annotation databases

    EnsemblBacteriaiAAG05413; AAG05413; PA2025.
    GeneIDi878570.
    KEGGipae:PA2025.
    PATRICi19838459. VBIPseAer58763_2110.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54201 Genomic DNA. Translation: CAA38122.1 .
    AE004091 Genomic DNA. Translation: AAG05413.1 .
    PIRi S15236.
    RefSeqi NP_250715.1. NC_002516.2.

    3D structure databases

    ProteinModelPortali P23189.
    SMRi P23189. Positions 2-450.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 208964.PA2025.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAG05413 ; AAG05413 ; PA2025 .
    GeneIDi 878570.
    KEGGi pae:PA2025.
    PATRICi 19838459. VBIPseAer58763_2110.

    Organism-specific databases

    PseudoCAPi PA2025.

    Phylogenomic databases

    eggNOGi COG1249.
    HOGENOMi HOG000276712.
    KOi K00383.
    OMAi HRQPCKM.
    OrthoDBi EOG6QCD6D.
    PhylomeDBi P23189.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    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.
    PROSITEi PS00076. PYRIDINE_REDOX_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of the gor gene encoding glutathione reductase from Pseudomonas aeruginosa: determinants of substrate specificity among pyridine nucleotide-disulphide oxidoreductases."
      Perry A.C.F., Ni Bhriain N., Brown N.L., Rouch D.A.
      Mol. Microbiol. 5:163-171(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: PAO8.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

    Entry informationi

    Entry nameiGSHR_PSEAE
    AccessioniPrimary (citable) accession number: P23189
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 117 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.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3