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P46354

- PUNA_BACSU

UniProt

P46354 - PUNA_BACSU

Protein

Purine nucleoside phosphorylase 1

Gene

punA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Nov 1995)
      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.

    Catalytic activityi

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

    Pathwayi

    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

    BioCyciBSUB:BSU23490-MONOMER.
    RETL1328306-WGS:GSTH-199-MONOMER.
    UniPathwayiUPA00606.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Purine nucleoside phosphorylase 1 (EC:2.4.2.1)
    Short name:
    PNP 1
    Alternative name(s):
    Inosine phosphorylase
    Inosine-guanosine phosphorylase
    Purine nucleoside phosphorylase I
    Short name:
    PNP I
    Short name:
    PU-NPase I
    Gene namesi
    Name:punA
    Synonyms:deoD, pnp, yqkO
    Ordered Locus Names:BSU23490
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU23490. [Micado]

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 271271Purine nucleoside phosphorylase 1PRO_0000184540Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei28 – 281Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP46354.

    PTM databases

    PhosSiteiP0802232.

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU23490.

    Structurei

    3D structure databases

    ProteinModelPortaliP46354.
    SMRiP46354. Positions 1-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PNP/MTAP phosphorylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0005.
    HOGENOMiHOG000045183.
    KOiK03783.
    OMAiDQPLSHD.
    OrthoDBiEOG6423M2.
    PhylomeDBiP46354.

    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.
    PTHR11904:SF9. PTHR11904:SF9. 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.

    P46354-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKDRIERAAA FIKQNLPESP KIGLILGSGL GILADEIENP VKLKYEDIPE    50
    FPVSTVEGHA GQLVLGTLEG VSVIAMQGRF HFYEGYSMEK VTFPVRVMKA 100
    LGVEALIVTN AAGGVNTEFR AGDLMIITDH INFMGTNPLI GPNEADFGAR 150
    FPDMSSAYDK DLSSLAEKIA KDLNIPIQKG VYTAVTGPSY ETPAEVRFLR 200
    TMGSDAVGMS TVPEVIVANH AGMRVLGISC ISNAAAGILD QPLSHDEVME 250
    VTEKVKAGFL KLVKAIVAQY E 271
    Length:271
    Mass (Da):29,127
    Last modified:November 1, 1995 - v1
    Checksum:i420B26E7309D9FC9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti184 – 1841A → D in M85047. (PubMed:1629150)Curated
    Sequence conflicti227 – 2271G → A in M85047. (PubMed:1629150)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U32685 Genomic DNA. Translation: AAA74434.1.
    D84432 Genomic DNA. Translation: BAA12651.1.
    AL009126 Genomic DNA. Translation: CAB14281.1.
    M85047 Genomic DNA. No translation available.
    PIRiD69680.
    RefSeqiNP_390230.1. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB14281; CAB14281; BSU23490.
    GeneIDi938731.
    KEGGibsu:BSU23490.
    PATRICi18976517. VBIBacSub10457_2449.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U32685 Genomic DNA. Translation: AAA74434.1 .
    D84432 Genomic DNA. Translation: BAA12651.1 .
    AL009126 Genomic DNA. Translation: CAB14281.1 .
    M85047 Genomic DNA. No translation available.
    PIRi D69680.
    RefSeqi NP_390230.1. NC_000964.3.

    3D structure databases

    ProteinModelPortali P46354.
    SMRi P46354. Positions 1-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU23490.

    PTM databases

    PhosSitei P0802232.

    Proteomic databases

    PaxDbi P46354.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14281 ; CAB14281 ; BSU23490 .
    GeneIDi 938731.
    KEGGi bsu:BSU23490.
    PATRICi 18976517. VBIBacSub10457_2449.

    Organism-specific databases

    GenoListi BSU23490. [Micado ]

    Phylogenomic databases

    eggNOGi COG0005.
    HOGENOMi HOG000045183.
    KOi K03783.
    OMAi DQPLSHD.
    OrthoDBi EOG6423M2.
    PhylomeDBi P46354.

    Enzyme and pathway databases

    UniPathwayi UPA00606 .
    BioCyci BSUB:BSU23490-MONOMER.
    RETL1328306-WGS:GSTH-199-MONOMER.

    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.
    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 TIGR01700. PNPH. 1 hit.
    TIGR01697. PNPH-PUNA-XAPA. 1 hit.
    PROSITEi PS01240. PNP_MTAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleosides as a carbon source in Bacillus subtilis: characterization of the drm-pupG operon."
      Schuch R., Garibian A., Saxild H.H., Piggot P.J., Nygaard P.
      Microbiology 145:2957-2966(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / BR151.
    2. "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
      Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
      Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / JH642.
    3. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
      Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
      , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
      Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: 168.
    4. "Characterization of a Bacillus subtilis sporulation operon that includes genes for an RNA polymerase sigma factor and for a putative DD-carboxypeptidase."
      Wu J.-J., Schuch R., Piggot P.J.
      J. Bacteriol. 174:4885-4892(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-271.
      Strain: 168 / MB24.
    5. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
      Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
      Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: 168.

    Entry informationi

    Entry nameiPUNA_BACSU
    AccessioniPrimary (citable) accession number: P46354
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1995
    Last modified: October 1, 2014
    This is version 109 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

    Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3