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P81989

- PUNA_CELSP

UniProt

P81989 - PUNA_CELSP

Protein

Purine nucleoside phosphorylase

Gene

punA

Organism
Cellulomonas sp.
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Jun 2000)
      Previous versions | rss
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    Functioni

    The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine and inosine.1 Publication

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei204 – 2041Sequence Analysis

    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

    BRENDAi2.4.2.1. 1235.
    UniPathwayiUPA00606.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Purine nucleoside phosphorylase (EC:2.4.2.1)
    Short name:
    PNP
    Alternative name(s):
    Inosine phosphorylase
    Inosine-guanosine phosphorylase
    Gene namesi
    Name:punA
    OrganismiCellulomonas sp.
    Taxonomic identifieri40001 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 282282Purine nucleoside phosphorylasePRO_0000184541Add
    BLAST

    Interactioni

    Subunit structurei

    Homotrimer.

    Structurei

    Secondary structure

    1
    282
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi18 – 3316
    Beta strandi39 – 435
    Turni49 – 546
    Beta strandi57 – 637
    Helixi64 – 663
    Beta strandi81 – 888
    Beta strandi94 – 996
    Helixi106 – 1083
    Helixi112 – 1154
    Helixi117 – 1248
    Beta strandi129 – 13810
    Beta strandi148 – 1569
    Helixi177 – 18610
    Beta strandi192 – 1976
    Helixi206 – 21510
    Beta strandi218 – 2247
    Helixi225 – 2339
    Beta strandi237 – 24711
    Turni249 – 2513
    Beta strandi252 – 2543
    Helixi258 – 28023

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C3XX-ray2.40A/B/C9-282[»]
    1QE5X-ray2.20A/B/C9-282[»]
    ProteinModelPortaliP81989.
    SMRiP81989. Positions 9-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81989.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1 – 44Poly-Thr

    Sequence similaritiesi

    Belongs to the PNP/MTAP phosphorylase family.Curated

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    InterProiIPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR011269. PUNP.
    IPR011268. Purine_phosphorylase.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view]
    PANTHERiPTHR11904. PTHR11904. 1 hit.
    PTHR11904:SF9. PTHR11904:SF9. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000477. PurNPase. 1 hit.
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01697. PNPH-PUNA-XAPA. 1 hit.
    TIGR01698. PUNP. 1 hit.
    PROSITEiPS01240. PNP_MTAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P81989-1 [UniParc]FASTAAdd to Basket

    « Hide

    TTTTPPSTPP LDDPATDPFL VARAAADHIA QATGVEGHDM ALVLGSGWGG    50
    AAELLGEVVA EVPTHEIPGF SAPAVAGHLS VTRSIRVERA DGSVRHALVL 100
    GSRTHLYEGK GVRAVVHGVR TAAATGAETL ILTNGCGGLN QEWGAGTPVL 150
    LSDHINLTAR SPLEGPTFVD LTDVYSPRLR ELAHRVDPTL PEGVYAQFPG 200
    PHYETPAEVR MAGILGADLV GMSTTLEAIA ARHCGLEVLG VSLVTNLAAG 250
    ISPTPLSHAE VIEAGQAAGP RISALLADIA KR 282
    Length:282
    Mass (Da):29,021
    Last modified:June 1, 2000 - v1
    Checksum:i65F468DACC43D360
    GO

    Cross-referencesi

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C3X X-ray 2.40 A/B/C 9-282 [» ]
    1QE5 X-ray 2.20 A/B/C 9-282 [» ]
    ProteinModelPortali P81989.
    SMRi P81989. Positions 9-282.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00606 .
    BRENDAi 2.4.2.1. 1235.

    Miscellaneous databases

    EvolutionaryTracei P81989.

    Family and domain databases

    Gene3Di 3.40.50.1580. 1 hit.
    InterProi IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR011269. PUNP.
    IPR011268. Purine_phosphorylase.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view ]
    PANTHERi PTHR11904. PTHR11904. 1 hit.
    PTHR11904:SF9. PTHR11904:SF9. 1 hit.
    Pfami PF01048. PNP_UDP_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000477. PurNPase. 1 hit.
    SUPFAMi SSF53167. SSF53167. 1 hit.
    TIGRFAMsi TIGR01697. PNPH-PUNA-XAPA. 1 hit.
    TIGR01698. PUNP. 1 hit.
    PROSITEi PS01240. PNP_MTAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Crystal structure of the purine nucleoside phosphorylase (PNP) from Cellulomonas sp. and its implication for the mechanism of trimeric PNPs."
      Tebbe J., Bzowska A., Wielgus-Kutrowska B., Schroeder W., Kazimierczuk Z., Shugar D., Saenger W., Koellner G.
      J. Mol. Biol. 294:1239-1255(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION.

    Entry informationi

    Entry nameiPUNA_CELSP
    AccessioniPrimary (citable) accession number: P81989
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: June 1, 2000
    Last modified: October 1, 2014
    This is version 68 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, Direct protein sequencing

    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