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P50389

- PNPH_SULSO

UniProt

P50389 - PNPH_SULSO

Protein

Purine nucleoside phosphorylase

Gene

SSO2706

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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

    Pathwayi

    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

    1. purine-nucleoside phosphorylase activity Source: UniProtKB-EC

    GO - Biological processi

    1. nucleoside metabolic process Source: InterPro

    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: 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 – 63
    Beta strandi15 – 217
    Helixi23 – 297
    Helixi30 – 323
    Beta strandi33 – 408
    Helixi42 – 443
    Beta strandi47 – 526
    Beta strandi55 – 617
    Helixi66 – 7813
    Beta strandi83 – 9210
    Beta strandi102 – 1109
    Helixi114 – 1207
    Helixi132 – 14413
    Beta strandi149 – 1568
    Helixi160 – 1623
    Helixi167 – 1726
    Turni173 – 1753
    Beta strandi176 – 1827
    Helixi183 – 19311
    Beta strandi196 – 20611
    Helixi218 – 23417

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK00772.
    OMAiGEPDRAN.

    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

    MNPVHILAKK GEVAERVLVV GDPGRARLLS TLLQNPKLTN ENRGFLVYTG    50
    KYNGETVSIA THGIGGPSIA IVLEELAMLG ANVFIRYGTT GALVPYINLG 100
    EYIIVTGASY NQGGLFYQYL RDNACVASTP DFELTNKLVT SFSKRNLKYY 150
    VGNVFSSDAF YAEDEEFVKK WSSRGNIAVE MECATLFTLS KVKGWKSATV 200
    LVVSDNLAKG GIWITKEELE KSVMDGAKAV LDTLTS 236
    Length:236
    Mass (Da):25,738
    Last modified:October 1, 1996 - v1
    Checksum:iF1570ECE8AA3D51B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z50181 Genomic DNA. Translation: CAA90560.1 .
    AE006641 Genomic DNA. Translation: AAK42818.1 .
    PIRi S58291.
    RefSeqi NP_344028.1. NC_002754.1.
    WP_009988635.1. NC_002754.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JDS X-ray 1.80 A/B/C/D/E/F 1-236 [» ]
    1JDT X-ray 2.00 A/B/C 1-236 [» ]
    1JDU X-ray 2.50 A/B/C 1-236 [» ]
    1JDV X-ray 2.00 A/B/C/D/E/F 1-236 [» ]
    1JDZ X-ray 2.00 A/B/C 1-236 [» ]
    1JE0 X-ray 1.60 A/B/C 1-236 [» ]
    1JE1 X-ray 1.80 A/B/C/D/E/F 1-236 [» ]
    1JP7 X-ray 1.80 A/B/C 1-236 [» ]
    1JPV X-ray 1.80 A/B/C 1-236 [» ]
    ProteinModelPortali P50389.
    SMRi P50389. Positions 2-236.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 273057.SSO2706.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAK42818 ; AAK42818 ; SSO2706 .
    GeneIDi 1452737.
    KEGGi sso:SSO2706.

    Phylogenomic databases

    eggNOGi COG2820.
    HOGENOMi HOG000274897.
    KOi K00772.
    OMAi GEPDRAN.

    Enzyme and pathway databases

    UniPathwayi UPA00606 .
    BioCyci SSOL273057:GCH2-2504-MONOMER.
    BRENDAi 2.4.2.28. 6163.

    Miscellaneous databases

    EvolutionaryTracei P50389.

    Family and domain databases

    Gene3Di 3.40.50.1580. 1 hit.
    InterProi IPR018017. Nucleoside_phosphorylase.
    IPR018016. Nucleoside_phosphorylase_CS.
    IPR000845. Nucleoside_phosphorylase_d.
    [Graphical view ]
    PANTHERi PTHR21234. PTHR21234. 1 hit.
    Pfami PF01048. PNP_UDP_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53167. SSF53167. 1 hit.
    PROSITEi PS01232. PNP_UDP_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 99 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