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P43783

- GSHR_HAEIN

UniProt

P43783 - GSHR_HAEIN

Protein

Glutathione reductase

Gene

gor

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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 sitei445 – 4451Proton 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
    Ordered Locus Names:HI_0161
    OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
    Taxonomic identifieri71421 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
    ProteomesiUP000000579: Chromosome

    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 – 456456Glutathione reductasePRO_0000067976Add
    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

    Protein-protein interaction databases

    STRINGi71421.HI0161.

    Structurei

    3D structure databases

    ProteinModelPortaliP43783.
    SMRiP43783. Positions 2-456.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.
    KOiK00383.
    OMAiHRQPCKM.
    OrthoDBiEOG6QCD6D.
    PhylomeDBiP43783.

    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.

    P43783-1 [UniParc]FASTAAdd to Basket

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    MTKHYDYIAI GGGSGGIASL NRAASYGKKC AIIEAKHLGG TCVNVGCVPK    50
    KVMFYGAHIA EAINNYAPDY GFDVEVKKFD FSKLIESRQA YISRIHTSYN 100
    NVLAKNNIDV INGFGKFVDA HTIEVTLADG TKEQVTADHI LIATGGRPYR 150
    PNIKGQEYGI DSDGFFALTE LPKRAAVIGA GYIAVELSGV LNSLGVETHL 200
    LVRRHAPMRN QDPLIVETLV EVLAQDGIQL HTNSTPSEIV KNADGSLTVR 250
    CDGQSDVTVD CVIWAAGRVP TTDKIGLENA GVETNEHGYV KVDKYQNTNV 300
    KGIYAVGDII ENGIELTPVA VAAGRRLSER LFNNKPTEYL DYSLVPTVVF 350
    SHPPIGTVGL TEPQAIEQYG AENVKVYKSS FTAMYTAVTQ HRQPCKMKLV 400
    CVGKDEKVVG LHGIGFGVDE MIQGFAVAIK MGATKADFDN TVAIHPTGSE 450
    EFVTMR 456
    Length:456
    Mass (Da):49,329
    Last modified:November 1, 1995 - v1
    Checksum:i846988C215FE949A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20229 Genomic DNA. Translation: AAA62137.1.
    L42023 Genomic DNA. Translation: AAC21833.1.
    PIRiA64052.
    RefSeqiNP_438331.1. NC_000907.1.
    WP_005694117.1. NC_000907.1.

    Genome annotation databases

    EnsemblBacteriaiAAC21833; AAC21833; HI_0161.
    GeneIDi951071.
    KEGGihin:HI0161.
    PATRICi20188821. VBIHaeInf48452_0167.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U20229 Genomic DNA. Translation: AAA62137.1 .
    L42023 Genomic DNA. Translation: AAC21833.1 .
    PIRi A64052.
    RefSeqi NP_438331.1. NC_000907.1.
    WP_005694117.1. NC_000907.1.

    3D structure databases

    ProteinModelPortali P43783.
    SMRi P43783. Positions 2-456.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 71421.HI0161.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC21833 ; AAC21833 ; HI_0161 .
    GeneIDi 951071.
    KEGGi hin:HI0161.
    PATRICi 20188821. VBIHaeInf48452_0167.

    Phylogenomic databases

    eggNOGi COG1249.
    KOi K00383.
    OMAi HRQPCKM.
    OrthoDBi EOG6QCD6D.
    PhylomeDBi P43783.

    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. Barcak G.J., Heimer S.R.
      Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.

    Entry informationi

    Entry nameiGSHR_HAEIN
    AccessioniPrimary (citable) accession number: P43783
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 113 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. Haemophilus influenzae
      Haemophilus influenzae (strain Rd): entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3