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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: Annotation score: 5 out of 5-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

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.

    Pathway:ipurine 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)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101PhosphateUniRule annotation
    Sitei169 – 1691Important for substrate specificityUniRule annotation
    Binding sitei187 – 1871Substrate; via amide nitrogenUniRule annotation
    Binding sitei188 – 1881PhosphateUniRule annotation
    Sitei223 – 2231Important for substrate specificityUniRule annotation

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Purine 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
    ProteomesiUP000001013 Componenti: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi169 – 1691E → 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 Publication
    Mutagenesisi211 – 2111N → 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 Publication
    Mutagenesisi213 – 2131A → 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 Publication
    Mutagenesisi223 – 2231H → 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 Publication
    Mutagenesisi254 – 2541C → S: Fully active, but reduces thermodynamic and kinetic stability of the enzyme; when associated with S-256.
    Mutagenesisi256 – 2561C → S: Fully active, but reduces thermodynamic and kinetic stability of the enzyme; when associated with S-254.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 265264Probable 6-oxopurine nucleoside phosphorylasePRO_0000415086Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni49 – 502Phosphate bindingUniRule annotation
    Regioni82 – 832Phosphate bindingUniRule annotation
    Regioni211 – 2133Substrate bindingUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0005.
    HOGENOMiHOG000228987.
    KOiK00772.
    OMAiGCDIVGM.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    HAMAPiMF_01963. MTAP.
    InterProiIPR010044. MTAP.
    IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view]
    PANTHERiPTHR11904. PTHR11904. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01694. MTAP. 1 hit.
    PROSITEiPS01240. PNP_MTAP_2. 1 hit.
    [Graphical view]

    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.
    RefSeqiNP_578582.1. NC_003413.1.
    WP_011011984.1. NC_003413.1.

    Genome annotation databases

    EnsemblBacteriaiAAL80977; AAL80977; PF0853.
    GeneIDi1468711.
    KEGGipfu:PF0853.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE009950 Genomic DNA. Translation: AAL80977.1.
    RefSeqiNP_578582.1. NC_003413.1.
    WP_011011984.1. NC_003413.1.

    3D structure databases

    ProteinModelPortaliQ8U2I1.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi186497.PF0853.

    Proteomic databases

    PRIDEiQ8U2I1.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAL80977; AAL80977; PF0853.
    GeneIDi1468711.
    KEGGipfu:PF0853.

    Phylogenomic databases

    eggNOGiCOG0005.
    HOGENOMiHOG000228987.
    KOiK00772.
    OMAiGCDIVGM.

    Enzyme and pathway databases

    UniPathwayiUPA00606.
    BRENDAi2.4.2.1. 5243.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    HAMAPiMF_01963. MTAP.
    InterProiIPR010044. MTAP.
    IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view]
    PANTHERiPTHR11904. PTHR11904. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01694. MTAP. 1 hit.
    PROSITEiPS01240. PNP_MTAP_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
      Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
      Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
    2. "Biochemical and structural characterization of mammalian-like purine nucleoside phosphorylase from the Archaeon Pyrococcus furiosus."
      Cacciapuoti G., Gorassini S., Mazzeo M.F., Siciliano R.A., Carbone V., Zappia V., Porcelli M.
      FEBS J. 274:2482-2495(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBUNIT, DISULFIDE BONDS.
    3. "Unraveling the structural and functional differences between purine nucleoside phosphorylase and 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus."
      Cacciapuoti G., Marabotti A., Fuccio F., Porcelli M.
      Biochim. Biophys. Acta 1814:1358-1366(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLU-169; ASN-211; ALA-213 AND HIS-223.

    Entry informationi

    Entry nameiPNPH_PYRFU
    AccessioniPrimary (citable) accession number: Q8U2I1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 25, 2012
    Last sequence update: June 1, 2002
    Last modified: May 27, 2015
    This is version 73 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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.

    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

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.