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Q94655

- GSHR_PLAFK

UniProt

Q94655 - GSHR_PLAFK

Protein

Glutathione reductase

Gene

GR2

Organism
Plasmodium falciparum (isolate K1 / Thailand)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      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: 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:GR2
    OrganismiPlasmodium falciparum (isolate K1 / Thailand)
    Taxonomic identifieri5839 [NCBI]
    Taxonomic lineageiEukaryotaAlveolataApicomplexaAconoidasidaHaemosporidaPlasmodiumPlasmodium (Laverania)

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 500499Glutathione reductasePRO_0000067959Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    500
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 86
    Helixi12 – 2312
    Beta strandi28 – 358
    Helixi38 – 425
    Helixi45 – 6319
    Helixi64 – 674
    Helixi77 – 10125
    Beta strandi105 – 1095
    Beta strandi142 – 1476
    Helixi161 – 1633
    Helixi167 – 1704
    Beta strandi177 – 1826
    Helixi186 – 19611
    Turni197 – 1993
    Beta strandi201 – 2055
    Beta strandi207 – 2115
    Helixi217 – 22913
    Beta strandi233 – 2353
    Beta strandi240 – 2478
    Beta strandi251 – 2555
    Beta strandi260 – 26910
    Turni276 – 2794
    Turni283 – 2864
    Beta strandi289 – 2924
    Beta strandi294 – 2963
    Beta strandi303 – 3097
    Beta strandi314 – 3163
    Helixi354 – 36916
    Beta strandi383 – 3853
    Beta strandi391 – 3955
    Helixi398 – 4047
    Helixi407 – 4093
    Beta strandi410 – 4178
    Helixi420 – 4223
    Helixi429 – 4313
    Beta strandi435 – 4428
    Turni443 – 4464
    Beta strandi447 – 4559
    Helixi458 – 47013
    Helixi475 – 4795
    Helixi491 – 4944

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ONFX-ray2.60A1-500[»]
    ProteinModelPortaliQ94655.
    SMRiQ94655. Positions 2-496.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ94655.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG1249.

    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.

    Q94655-1 [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 KLEKLNVETN NNYIVVDENQ 300
    RTSVNNIYAV GDCCMVKKSK EIEDLNLLKL YNEERYLNKK ENVTEDIFYN 350
    VQLTPVAINA GRLLADRLFL KKTRKTNYKL IPTVIFSHPP IGTIGLSEEA 400
    AIQIYGKENV KIYESKFTNL FFSVYDIEPE LKEKTYLKLV CVGKDELIKG 450
    LHIIGLNADE IVQGFAVALK MNATKKDFDE TIPIHPTAAE EFLTLQPWMK 500
    Length:500
    Mass (Da):56,561
    Last modified:January 23, 2007 - v3
    Checksum:iAB2299144002FCD3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X93462 Genomic DNA. Translation: CAA63747.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X93462 Genomic DNA. Translation: CAA63747.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ONF X-ray 2.60 A 1-500 [» ]
    ProteinModelPortali Q94655.
    SMRi Q94655. Positions 2-496.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL1741261.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG1249.

    Miscellaneous databases

    EvolutionaryTracei Q94655.

    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 cloning and characterization of a putative glutathione reductase gene, the PfGR2 gene, from Plasmodium falciparum."
      Faerber P.M., Becker K., Mueller S.
      Eur. J. Biochem. 239:655-661(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Glutathione reductase and glutamate dehydrogenase of Plasmodium falciparum, the causative agent of tropical malaria."
      Krauth-Siegel R.L., Muller J.G., Lottspeich F., Schirmer R.H.
      Eur. J. Biochem. 235:345-350(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-16, CHARACTERIZATION.

    Entry informationi

    Entry nameiGSHR_PLAFK
    AccessioniPrimary (citable) accession number: Q94655
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 93 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

    The active site is a redox-active disulfide bond.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3