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Protein

Purine nucleoside phosphorylase

Gene

SSO2706

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. Cleaves inosine, guanosine, and adenosine with a better efficiency than MTA.2 Publications

Catalytic activityi

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.
Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate.
Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate.

Kineticsi

  1. KM=154 µM for S-methyl-5'-thioadenosine1 Publication
  2. KM=25.4 µM for adenosine1 Publication
  3. KM=84 µM for inosine1 Publication
  4. KM=113.6 µM for guanosine1 Publication

    Temperature dependencei

    Optimum temperature is 120 degrees Celsius. Highly thermostable.1 Publication

    Pathway:ipurine nucleoside salvage

    This protein is involved in the pathway purine nucleoside salvage, which is part of Purine metabolism.
    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 sitei5 – 51Substrate; shared with dimeric partner
    Binding sitei21 – 211Phosphate; via amide nitrogen
    Binding sitei25 – 251Phosphate
    Binding sitei43 – 431Phosphate; shared with dimeric partner
    Binding sitei163 – 1631Substrate

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciSSOL273057:GCH2-2504-MONOMER.
    BRENDAi2.4.2.28. 6163.
    UniPathwayiUPA00606.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Purine nucleoside phosphorylase (EC:2.4.2.1)
    Short name:
    PNP
    Alternative name(s):
    5'-methylthioadenosine phosphorylase I
    Short name:
    MTA phosphorylase I
    Short name:
    MTAPI
    Gene namesi
    Ordered Locus Names:SSO2706
    OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
    Taxonomic identifieri273057 [NCBI]
    Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
    ProteomesiUP000001974 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 236236Purine nucleoside phosphorylasePRO_0000063195Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi125 – 125Interchain

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Homohexamer; disulfide-linked. Trimer of homodimers, with three symmetric intersubunit disulfide bonds linking the dimers to one another.2 Publications

    Protein-protein interaction databases

    STRINGi273057.SSO2706.

    Structurei

    Secondary structure

    1
    236
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63Combined sources
    Beta strandi15 – 217Combined sources
    Helixi23 – 297Combined sources
    Helixi30 – 323Combined sources
    Beta strandi33 – 408Combined sources
    Helixi42 – 443Combined sources
    Beta strandi47 – 526Combined sources
    Beta strandi55 – 617Combined sources
    Helixi66 – 7813Combined sources
    Beta strandi83 – 9210Combined sources
    Beta strandi102 – 1109Combined sources
    Helixi114 – 1207Combined sources
    Helixi132 – 14413Combined sources
    Beta strandi149 – 1568Combined sources
    Helixi160 – 1623Combined sources
    Helixi167 – 1726Combined sources
    Turni173 – 1753Combined sources
    Beta strandi176 – 1827Combined sources
    Helixi183 – 19311Combined sources
    Beta strandi196 – 20611Combined sources
    Helixi218 – 23417Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JDSX-ray1.80A/B/C/D/E/F1-236[»]
    1JDTX-ray2.00A/B/C1-236[»]
    1JDUX-ray2.50A/B/C1-236[»]
    1JDVX-ray2.00A/B/C/D/E/F1-236[»]
    1JDZX-ray2.00A/B/C1-236[»]
    1JE0X-ray1.60A/B/C1-236[»]
    1JE1X-ray1.80A/B/C/D/E/F1-236[»]
    1JP7X-ray1.80A/B/C1-236[»]
    1JPVX-ray1.80A/B/C1-236[»]
    ProteinModelPortaliP50389.
    SMRiP50389. Positions 2-236.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50389.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni86 – 894Phosphate binding
    Regioni180 – 1823Substrate binding
    Regioni204 – 2052Substrate binding

    Sequence similaritiesi

    Belongs to the PNP/UDP phosphorylase family.Curated

    Phylogenomic databases

    eggNOGiCOG2820.
    HOGENOMiHOG000274897.
    InParanoidiP50389.
    KOiK00772.
    OMAiECYNEVR.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    InterProiIPR018017. Nucleoside_phosphorylase.
    IPR018016. Nucleoside_phosphorylase_CS.
    IPR000845. Nucleoside_phosphorylase_d.
    [Graphical view]
    PANTHERiPTHR21234. PTHR21234. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    PROSITEiPS01232. PNP_UDP_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P50389-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MNPVHILAKK GEVAERVLVV GDPGRARLLS TLLQNPKLTN ENRGFLVYTG
    60 70 80 90 100
    KYNGETVSIA THGIGGPSIA IVLEELAMLG ANVFIRYGTT GALVPYINLG
    110 120 130 140 150
    EYIIVTGASY NQGGLFYQYL RDNACVASTP DFELTNKLVT SFSKRNLKYY
    160 170 180 190 200
    VGNVFSSDAF YAEDEEFVKK WSSRGNIAVE MECATLFTLS KVKGWKSATV
    210 220 230
    LVVSDNLAKG GIWITKEELE KSVMDGAKAV LDTLTS
    Length:236
    Mass (Da):25,738
    Last modified:October 1, 1996 - v1
    Checksum:iF1570ECE8AA3D51B
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z50181 Genomic DNA. Translation: CAA90560.1.
    AE006641 Genomic DNA. Translation: AAK42818.1.
    PIRiS58291.
    RefSeqiNP_344028.1. NC_002754.1.
    WP_009988635.1. NC_002754.1.

    Genome annotation databases

    EnsemblBacteriaiAAK42818; AAK42818; SSO2706.
    GeneIDi1452737.
    KEGGisso:SSO2706.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    Z50181 Genomic DNA. Translation: CAA90560.1.
    AE006641 Genomic DNA. Translation: AAK42818.1.
    PIRiS58291.
    RefSeqiNP_344028.1. NC_002754.1.
    WP_009988635.1. NC_002754.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JDSX-ray1.80A/B/C/D/E/F1-236[»]
    1JDTX-ray2.00A/B/C1-236[»]
    1JDUX-ray2.50A/B/C1-236[»]
    1JDVX-ray2.00A/B/C/D/E/F1-236[»]
    1JDZX-ray2.00A/B/C1-236[»]
    1JE0X-ray1.60A/B/C1-236[»]
    1JE1X-ray1.80A/B/C/D/E/F1-236[»]
    1JP7X-ray1.80A/B/C1-236[»]
    1JPVX-ray1.80A/B/C1-236[»]
    ProteinModelPortaliP50389.
    SMRiP50389. Positions 2-236.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi273057.SSO2706.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAK42818; AAK42818; SSO2706.
    GeneIDi1452737.
    KEGGisso:SSO2706.

    Phylogenomic databases

    eggNOGiCOG2820.
    HOGENOMiHOG000274897.
    InParanoidiP50389.
    KOiK00772.
    OMAiECYNEVR.

    Enzyme and pathway databases

    UniPathwayiUPA00606.
    BioCyciSSOL273057:GCH2-2504-MONOMER.
    BRENDAi2.4.2.28. 6163.

    Miscellaneous databases

    EvolutionaryTraceiP50389.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    InterProiIPR018017. Nucleoside_phosphorylase.
    IPR018016. Nucleoside_phosphorylase_CS.
    IPR000845. Nucleoside_phosphorylase_d.
    [Graphical view]
    PANTHERiPTHR21234. PTHR21234. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    PROSITEiPS01232. PNP_UDP_1. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Gene cloning and amino acid sequence determination."
      Cacciapuoti G., Porcelli M., Bertoldo C., Fusco S., De Rosa M., Zappia V.
      Eur. J. Biochem. 239:632-637(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
    3. "Purification and characterization of extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and evidence for intersubunit disulfide bonds."
      Cacciapuoti G., Porcelli M., Bertoldo C., de Rosa M., Zappia V.
      J. Biol. Chem. 269:24762-24769(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-26, FUNCTION, SUBUNIT.
    4. "A novel hyperthermostable 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus."
      Cacciapuoti G., Forte S., Moretti M.A., Brio A., Zappia V., Porcelli M.
      FEBS J. 272:1886-1899(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    5. "Three-dimensional structure of a hyperthermophilic 5'-deoxy-5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus."
      Appleby T.C., Mathews I.I., Porcelli M., Cacciapuoti G., Ealick S.E.
      J. Biol. Chem. 276:39232-39242(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH SUBSTRATES AND SUBSTRATE ANALOGS.

    Entry informationi

    Entry nameiPNPH_SULSO
    AccessioniPrimary (citable) accession number: P50389
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: January 7, 2015
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. 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.