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O15770

- GSHR_PLAF7

UniProt

O15770 - GSHR_PLAF7

Protein

Glutathione reductase

Gene

GR3

Organism
Plasmodium falciparum (isolate 3D7)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 4 (05 Oct 2010)
      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 sitei485 – 4851Proton acceptorBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi32 – 409FADBy similarity

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. glutathione-disulfide reductase activity Source: GeneDB_Pfalciparum

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. response to oxidative stress Source: GeneDB_Pfalciparum

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NADP

    Enzyme and pathway databases

    ReactomeiREACT_191640. 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:GR3
    ORF Names:PF14_0192
    OrganismiPlasmodium falciparum (isolate 3D7)
    Taxonomic identifieri36329 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)
    ProteomesiUP000001450: Chromosome 14

    Organism-specific databases

    EuPathDBiPlasmoDB:PF3D7_1419800.2.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. apicoplast Source: GeneDB_Pfalciparum
    2. cytoplasm Source: GeneDB_Pfalciparum

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 500499Glutathione reductasePRO_0000067960Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi40 ↔ 45Redox-activeBy similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    STRINGi5833.PF14_0192-1.

    Structurei

    3D structure databases

    ProteinModelPortaliO15770.
    SMRiO15770. Positions 2-496.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    HOGENOMiHOG000276712.
    KOiK00383.
    OMAiGTNSDGF.
    PhylomeDBiO15770.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O15770-1 [UniParc]FASTAAdd to Basket

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    MVYDLIVIGG GSGGMAAARR AARHNAKVAL VEKSRLGGTC VNVGCVPKKI    50
    MFNAASVHDI LENSRHYGFD TKFSFNLPLL VERRDKYIQR LNNIYRQNLS 100
    KDKVDLYEGT ASFLSENRIL IKGTKDNNNK DNGPLNEEIL EGRNILIAVG 150
    NKPVFPPVKG IENTISSDEF FNIKESKKIG IVGSGYIAVE LINVIKRLGI 200
    DSYIFARGNR ILRKFDESVI NVLENDMKKN NINIVTFADV VEIKKVSDKN 250
    LSIHLSDGRI YEHFDHVIYC VGRSPDTENL NLEKLNVETN NNYIVVDENQ 300
    RTSVNNIYAV GDCCMVKKSK EIEDLNLLKL YNEETYLNKK ENVTEDIFYN 350
    VQLTPVAINA GRLLADRLFL KKTRKTNYKL IPTVIFSHPP IGTIGLSEEA 400
    AIQIYGKENV KIYESKFTNL FFSVYDIEPE LKEKTYLKLV CVGKDELIKG 450
    LHIIGLNADE IVQGFAVALK MNATKKDFDE TIPIHPTAAE EFLTLQPWMK 500
    Length:500
    Mass (Da):56,492
    Last modified:October 5, 2010 - v4
    Checksum:iEFFBA1668599EA37
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti283 – 2831E → G in AAB84117. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF027825 mRNA. Translation: AAB84117.1.
    AE014187 Genomic DNA. Translation: AAN36804.1.
    RefSeqiXP_001348365.1. XM_001348329.1.

    Genome annotation databases

    EnsemblProtistsiPF14_0192:mRNA; PF14_0192:pep; PF14_0192.
    GeneIDi811773.
    KEGGipfa:PF14_0192.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF027825 mRNA. Translation: AAB84117.1 .
    AE014187 Genomic DNA. Translation: AAN36804.1 .
    RefSeqi XP_001348365.1. XM_001348329.1.

    3D structure databases

    ProteinModelPortali O15770.
    SMRi O15770. Positions 2-496.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5833.PF14_0192-1.

    Chemistry

    BindingDBi O15770.
    ChEMBLi CHEMBL5061.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblProtistsi PF14_0192:mRNA ; PF14_0192:pep ; PF14_0192 .
    GeneIDi 811773.
    KEGGi pfa:PF14_0192.

    Organism-specific databases

    EuPathDBi PlasmoDB:PF3D7_1419800.2.

    Phylogenomic databases

    HOGENOMi HOG000276712.
    KOi K00383.
    OMAi GTNSDGF.
    PhylomeDBi O15770.

    Enzyme and pathway databases

    Reactomei REACT_191640. Detoxification of Reactive Oxygen Species.

    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. "Glutathione reductase from Plasmodium falciparum."
      Gilberger T.-W., Walter R.D., Mueller S.
      Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Isolate 3D7.

    Entry informationi

    Entry nameiGSHR_PLAF7
    AccessioniPrimary (citable) accession number: O15770
    Secondary accession number(s): Q8ILQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 98 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    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