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Protein

Probable 6-oxopurine nucleoside phosphorylase

Gene

PF0853

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Purine nucleoside phosphorylase which is highly specific for 6-oxopurine nucleosides. Cleaves guanosine or inosine to respective bases and sugar-1-phosphate molecules. Involved in purine salvage.UniRule annotation2 Publications

Miscellaneous

Although this enzyme belongs to the family of MTA phosphorylases based on sequence homology, it has been shown that conserved amino acid substitutions in the substrate binding pocket convert the substrate specificity of this enzyme from 6-aminopurines to 6-oxopurines. It seems that P.furiosus has developed a specific enzyme (PF0853) for the metabolism of 6-oxo-purines, next to the canonical MTA phosphorylase PF0016.

Catalytic activityi

Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate.UniRule annotation

Kineticsi

  1. KM=322 µM for inosine
  2. KM=122 µM for guanosine
  3. KM=1454 µM for adenosine

    pH dependencei

    Optimum pH is 7.4. Active from pH 5 to 10.

    Temperature dependencei

    Optimum temperature is 120 degrees Celsius. Thermostable up to 133 degrees Celsius.

    Pathwayi: purine nucleoside salvage

    This protein is involved in the pathway purine nucleoside salvage, which is part of Purine metabolism.UniRule annotation
    View all proteins of this organism that are known to be involved in the pathway purine nucleoside salvage and in Purine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei10PhosphateUniRule annotation1
    Sitei169Important for substrate specificityUniRule annotation1
    Binding sitei187Substrate; via amide nitrogenUniRule annotation1
    Binding sitei188PhosphateUniRule annotation1
    Sitei223Important for substrate specificityUniRule annotation1

    GO - Molecular functioni

    GO - Biological processi

    Keywordsi

    Molecular functionGlycosyltransferase, Transferase
    Biological processPurine salvage

    Enzyme and pathway databases

    BRENDAi2.4.2.1 5243
    UniPathwayiUPA00606

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Probable 6-oxopurine nucleoside phosphorylaseUniRule annotation (EC:2.4.2.1UniRule annotation)
    Alternative name(s):
    Purine nucleoside phosphorylaseUniRule annotation
    Short name:
    PNPUniRule annotation
    Short name:
    PfPNP
    Gene namesi
    Ordered Locus Names:PF0853
    OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
    Taxonomic identifieri186497 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
    Proteomesi

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi169E → S: Decreases catalytic activity for insosine and allows the enzyme to phosphorolytically cleave MTA with a catalytic efficiency about 4-fold higher than for inosine; when associated with D-211, D-213 and A-223. 1 Publication1
    Mutagenesisi211N → D: Decreases catalytic activity for insosine and allows the enzyme to phosphorolytically cleave MTA with a catalytic efficiency about 4-fold higher than for inosine; when associated with S-169, D-213 and A-223. 1 Publication1
    Mutagenesisi213A → D: Decreases catalytic activity for insosine and allows the enzyme to phosphorolytically cleave MTA with a catalytic efficiency about 4-fold higher than for inosine; when associated with S-169, D-211 and A-223. 1 Publication1
    Mutagenesisi223H → A: Decreases catalytic activity for insosine and allows the enzyme to phosphorolytically cleave MTA with a catalytic efficiency about 4-fold higher than for inosine; when associated with S-169, D-211, and D-213. 1 Publication1
    Mutagenesisi254C → S: Fully active, but reduces thermodynamic and kinetic stability of the enzyme; when associated with S-256. 1
    Mutagenesisi256C → S: Fully active, but reduces thermodynamic and kinetic stability of the enzyme; when associated with S-254. 1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemoved
    ChainiPRO_00004150862 – 265Probable 6-oxopurine nucleoside phosphorylaseAdd BLAST264

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi136 ↔ 2021 Publication
    Disulfide bondi162 ↔ 1901 Publication
    Disulfide bondi254 ↔ 2561 Publication

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PRIDEiQ8U2I1

    Interactioni

    Subunit structurei

    Homohexamer. Dimer of a homotrimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi186497.PF0853

    Structurei

    3D structure databases

    ProteinModelPortaliQ8U2I1
    SMRiQ8U2I1
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni49 – 50Phosphate bindingUniRule annotation2
    Regioni82 – 83Phosphate bindingUniRule annotation2
    Regioni211 – 213Substrate bindingUniRule annotation3

    Sequence similaritiesi

    Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiarCOG01327 Archaea
    COG0005 LUCA
    HOGENOMiHOG000228987
    KOiK00772
    OMAiCTPFGKP
    OrthoDBiPOG093Z08FG

    Family and domain databases

    HAMAPiMF_01963 MTAP, 1 hit
    InterProiView protein in InterPro
    IPR010044 MTAP
    IPR000845 Nucleoside_phosphorylase_d
    IPR035994 Nucleoside_phosphorylase_sf
    IPR018099 Purine_phosphorylase-2_CS
    PANTHERiPTHR42679 PTHR42679, 1 hit
    PfamiView protein in Pfam
    PF01048 PNP_UDP_1, 1 hit
    SUPFAMiSSF53167 SSF53167, 1 hit
    TIGRFAMsiTIGR01694 MTAP, 1 hit
    PROSITEiView protein in PROSITE
    PS01240 PNP_MTAP_2, 1 hit

    Sequencei

    Sequence statusi: Complete.

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

    Q8U2I1-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPRIAIVGGS GVYDFPAENK REETVKTPYG EVKITVGVVG DEEVAFLARH
    60 70 80 90 100
    GKGHSIPPHK INYRANIWAL YELGVERIIA TSAVGSMNPE MKPGDFVILD
    110 120 130 140 150
    QIIDFTVSRP RTFYDGEESP HERKFVAHVD FTEPYCPEIR KALITAARNL
    160 170 180 190 200
    GLPYHPRGTY VCTEGPRFET AAEIRAYRIL GGDVVGMTQC PEAILARELE
    210 220 230 240 250
    MCYATVAIVT NYAAGMSGKK LTHSEVVELM QKKSEDIVKL ILAAIPLIPK
    260
    ERRCGCKDAL KGATG
    Length:265
    Mass (Da):29,208
    Last modified:June 1, 2002 - v1
    Checksum:i19BF1EBBB2FEDBB8
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009950 Genomic DNA Translation: AAL80977.1
    RefSeqiWP_011011984.1, NC_003413.1

    Genome annotation databases

    EnsemblBacteriaiAAL80977; AAL80977; PF0853
    GeneIDi1468711
    KEGGipfu:PF0853
    PATRICifig|186497.12.peg.903

    Entry informationi

    Entry nameiPNPH_PYRFU
    AccessioniPrimary (citable) accession number: Q8U2I1
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: June 1, 2002
    Last modified: May 23, 2018
    This is version 84 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

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