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P55859

- PNPH_BOVIN

UniProt

P55859 - PNPH_BOVIN

Protein

Purine nucleoside phosphorylase

Gene

PNP

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 3 (05 Feb 2008)
      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.1 Publication

    Catalytic activityi

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

    Pathwayi

    GO - Molecular functioni

    1. purine-nucleoside phosphorylase activity Source: UniProtKB

    GO - Biological processi

    1. nucleoside metabolic process Source: InterPro

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.4.2.1. 908.
    ReactomeiREACT_211472. Purine salvage.
    REACT_214112. Purine catabolism.
    SABIO-RKP55859.
    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:PNP
    Synonyms:NP
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 10

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. cytoskeleton Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 289289Purine nucleoside phosphorylasePRO_0000184535Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP55859.
    PRIDEiP55859.

    Interactioni

    Subunit structurei

    Homotrimer.

    Structurei

    Secondary structure

    1
    289
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 2014
    Beta strandi26 – 316
    Helixi36 – 416
    Beta strandi43 – 497
    Helixi50 – 523
    Beta strandi62 – 643
    Beta strandi67 – 737
    Beta strandi76 – 838
    Helixi87 – 893
    Helixi93 – 964
    Helixi98 – 1069
    Beta strandi110 – 11910
    Beta strandi129 – 1379
    Helixi138 – 1414
    Turni153 – 1553
    Helixi168 – 18114
    Beta strandi188 – 1947
    Helixi203 – 2119
    Beta strandi215 – 2217
    Helixi222 – 2309
    Beta strandi234 – 24411
    Beta strandi248 – 2503
    Helixi257 – 27822
    Helixi279 – 2813
    Beta strandi284 – 2874

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A9OX-ray2.00A1-289[»]
    1A9PX-ray2.40A1-289[»]
    1A9QX-ray2.00A1-282[»]
    1A9RX-ray2.00A1-282[»]
    1A9SX-ray2.00A1-289[»]
    1A9TX-ray2.00A1-284[»]
    1B8NX-ray2.00A1-284[»]
    1B8OX-ray1.50A1-284[»]
    1FXUX-ray2.20A1-289[»]
    1LV8X-ray2.30A/B/C/D/E/F1-289[»]
    1LVUX-ray2.05A/B/C/D/E/F1-289[»]
    1PBNX-ray2.00A1-289[»]
    1V48X-ray2.20A1-289[»]
    1VFNX-ray2.15A4-284[»]
    2AI1X-ray2.00A1-289[»]
    2AI2X-ray1.70A1-289[»]
    2AI3X-ray1.70A1-289[»]
    2QPLX-ray2.10A3-284[»]
    3FUCX-ray1.45A/B/C1-284[»]
    3PNPX-ray1.60A1-289[»]
    4PNPX-ray1.80A1-289[»]
    ProteinModelPortaliP55859.
    SMRiP55859. Positions 3-282.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55859.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PNP/MTAP phosphorylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0005.
    GeneTreeiENSGT00550000074740.
    HOGENOMiHOG000045183.
    HOVERGENiHBG002460.
    InParanoidiP55859.
    OMAiDRTMRQK.
    OrthoDBiEOG73RBBZ.
    TreeFamiTF300049.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    InterProiIPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR011270. Pur_Nuc_Pase_Ino/Guo-sp.
    IPR011268. Purine_phosphorylase.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view]
    PANTHERiPTHR11904. PTHR11904. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000477. PurNPase. 1 hit.
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01700. PNPH. 1 hit.
    TIGR01697. PNPH-PUNA-XAPA. 1 hit.
    PROSITEiPS01240. PNP_MTAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P55859-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANGYTYEDY QDTAKWLLSH TEQRPQVAVI CGSGLGGLVN KLTQAQTFDY    50
    SEIPNFPEST VPGHAGRLVF GILNGRACVM MQGRFHMYEG YPFWKVTFPV 100
    RVFRLLGVET LVVTNAAGGL NPNFEVGDIM LIRDHINLPG FSGENPLRGP 150
    NEERFGVRFP AMSDAYDRDM RQKAHSTWKQ MGEQRELQEG TYVMLGGPNF 200
    ETVAECRLLR NLGADAVGMS TVPEVIVARH CGLRVFGFSL ITNKVIMDYE 250
    SQGKANHEEV LEAGKQAAQK LEQFVSLLMA SIPVSGHTG 289
    Length:289
    Mass (Da):32,037
    Last modified:February 5, 2008 - v3
    Checksum:i7ECF84CCA494DEED
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21A → Q AA sequence (PubMed:7607309)Curated
    Sequence conflicti25 – 251P → S in AAX46392. (PubMed:16305752)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT021545 mRNA. Translation: AAX46392.1.
    BC103291 mRNA. Translation: AAI03292.2.
    PIRiS66203.
    UniGeneiBt.65253.

    Genome annotation databases

    EnsembliENSBTAT00000016346; ENSBTAP00000016346; ENSBTAG00000012317.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BT021545 mRNA. Translation: AAX46392.1 .
    BC103291 mRNA. Translation: AAI03292.2 .
    PIRi S66203.
    UniGenei Bt.65253.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A9O X-ray 2.00 A 1-289 [» ]
    1A9P X-ray 2.40 A 1-289 [» ]
    1A9Q X-ray 2.00 A 1-282 [» ]
    1A9R X-ray 2.00 A 1-282 [» ]
    1A9S X-ray 2.00 A 1-289 [» ]
    1A9T X-ray 2.00 A 1-284 [» ]
    1B8N X-ray 2.00 A 1-284 [» ]
    1B8O X-ray 1.50 A 1-284 [» ]
    1FXU X-ray 2.20 A 1-289 [» ]
    1LV8 X-ray 2.30 A/B/C/D/E/F 1-289 [» ]
    1LVU X-ray 2.05 A/B/C/D/E/F 1-289 [» ]
    1PBN X-ray 2.00 A 1-289 [» ]
    1V48 X-ray 2.20 A 1-289 [» ]
    1VFN X-ray 2.15 A 4-284 [» ]
    2AI1 X-ray 2.00 A 1-289 [» ]
    2AI2 X-ray 1.70 A 1-289 [» ]
    2AI3 X-ray 1.70 A 1-289 [» ]
    2QPL X-ray 2.10 A 3-284 [» ]
    3FUC X-ray 1.45 A/B/C 1-284 [» ]
    3PNP X-ray 1.60 A 1-289 [» ]
    4PNP X-ray 1.80 A 1-289 [» ]
    ProteinModelPortali P55859.
    SMRi P55859. Positions 3-282.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P55859.
    ChEMBLi CHEMBL2935.

    Proteomic databases

    PaxDbi P55859.
    PRIDEi P55859.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000016346 ; ENSBTAP00000016346 ; ENSBTAG00000012317 .

    Phylogenomic databases

    eggNOGi COG0005.
    GeneTreei ENSGT00550000074740.
    HOGENOMi HOG000045183.
    HOVERGENi HBG002460.
    InParanoidi P55859.
    OMAi DRTMRQK.
    OrthoDBi EOG73RBBZ.
    TreeFami TF300049.

    Enzyme and pathway databases

    UniPathwayi UPA00606 .
    BRENDAi 2.4.2.1. 908.
    Reactomei REACT_211472. Purine salvage.
    REACT_214112. Purine catabolism.
    SABIO-RK P55859.

    Miscellaneous databases

    EvolutionaryTracei P55859.

    Family and domain databases

    Gene3Di 3.40.50.1580. 1 hit.
    InterProi IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR011270. Pur_Nuc_Pase_Ino/Guo-sp.
    IPR011268. Purine_phosphorylase.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view ]
    PANTHERi PTHR11904. PTHR11904. 1 hit.
    Pfami PF01048. PNP_UDP_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000477. PurNPase. 1 hit.
    SUPFAMi SSF53167. SSF53167. 1 hit.
    TIGRFAMsi TIGR01700. PNPH. 1 hit.
    TIGR01697. PNPH-PUNA-XAPA. 1 hit.
    PROSITEi PS01240. PNP_MTAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Calf spleen purine nucleoside phosphorylase: purification, sequence and crystal structure of its complex with an N(7)-acycloguanosine inhibitor."
      Bzowska A., Luic M., Schroeder W., Shugar D., Saenger W., Koellner G.
      FEBS Lett. 367:214-218(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION.
      Tissue: Spleen.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Uterus.
    4. "Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15-A resolution."
      Koellner G., Luic M., Shugar D., Saenger W., Bzowska A.
      J. Mol. Biol. 265:202-216(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
      Tissue: Spleen.
    5. Mao C., Zhou M., Ealick S., Federov A.A., Almo S.C.
      Submitted (JUL-1995) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
    6. "Calf spleen purine nucleoside phosphorylase complexed with substrates and substrate analogues."
      Mao C., Cook W.J., Zhou M., Federov A.A., Almo S.C., Ealick S.E.
      Biochemistry 37:7135-7146(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
      Tissue: Spleen.
    7. "The high resolution crystal structure of bovine spleen purine nucleoside phosphorylase in complex forms with phosphate and 9-deazainosine."
      Pugmire M.J., Mao C., Ealick S.E.
      Submitted (MAR-1998) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
      Tissue: Spleen.

    Entry informationi

    Entry nameiPNPH_BOVIN
    AccessioniPrimary (citable) accession number: P55859
    Secondary accession number(s): Q3ZBH6, Q58DQ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 5, 2008
    Last modified: October 1, 2014
    This is version 113 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata 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