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    deoD purine nucleoside phosphorylase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945654, updated on 3-Dec-2024

    Summary

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    Official Symbol
    deoD
    Official Full Name
    purine nucleoside phosphorylase
    Primary source
    ECOCYC:EG10222
    Locus tag
    b4384
    See related
    ASAP:ABE-0014379
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK4376; pup
    Summary
    DeoD has reversible purine nucleoside phosphorylase (PNP) activity with broad substrate specificity; however, it does not act on xanthosine or pyrimidine nucleosides . [More information is available at EcoCyc: EG10222].
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    Genomic context

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    Sequence:
    NC_000913.3 (4620883..4621602)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene thymidine phosphorylase Neighboring gene phosphopentomutase Neighboring gene toxin YjjJ Neighboring gene lipoate--protein ligase A

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Properties of a mutant of Escherichia coli lacking purine nucleoside phosphorylase. Ahmad SI, et al. Biochim Biophys Acta, 1968 Jul 23. PMID 4875425
    2. Designer gene therapy using an Escherichia coli purine nucleoside phosphorylase/prodrug system. Bennett EM, et al. Chem Biol, 2003 Dec. PMID 14700625
    3. Limited thymidine uptake in Escherichia coli due to an inducible thymidine phosphorylase. RACHMELER M, et al. Biochim Biophys Acta, 1961 Apr 29. PMID 13738908
    4. Structural basis for substrate specificity of Escherichia coli purine nucleoside phosphorylase. Bennett EM, et al. J Biol Chem, 2003 Nov 21. PMID 12937174
    5. Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism. Koellner G, et al. J Mol Biol, 2002 Jan 18. PMID 11786017

    See all (63) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. These studies also indicate an important role of the phenyl ring of Phe159 for FRET in the wild-type purine nucleoside phosphorylase, which does not exist in the Ala159 mutant, and for the effective association of PNP with formycin A .
      Title: A QM-MD simulation approach to the analysis of FRET processes in (bio)molecular systems. A case study: complexes of E. coli purine nucleoside phosphorylase and its mutants with formycin A.
    2. Data suggest that in active sites of purine nucleoside phosphorylase complexed with phosphate and formycin A, recombinant enzyme exhibits unexpected binding site for phosphate and exhibits stoichiometry of two phosphate molecules per enzyme subunit.
      Title: New phosphate binding sites in the crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with phosphate and formycin A.
    3. The deoD gene was cloned from Escherichia coli MG1665 & overexpressed in E. coli BL 21(DE3).
      Title: Cloning and characterization of purine nucleoside phosphorylase in Escherichia coli and subsequent ribavirin biosynthesis using immobilized recombinant cells.
    4. Role of ionization of the phosphate cosubstrate on phosphorolysis by purine nucleoside phosphorylase (PNP)
      Title: Role of ionization of the phosphate cosubstrate on phosphorolysis by purine nucleoside phosphorylase (PNP) of bacterial (E. coli) and mammalian (human) origin.
    5. N-terminus verified by Edman degradation on mature peptide
      Title: The biosynthesis of molybdopterin in Escherichia coli. Purification and characterization of the converting factor.
    6. in solution similar to the crystal, E. coli PNP is a hexameric molecule and previous suggestions for coexistence of two oligomeric forms are incorrect.
      Title: Molecular architecture of E. coli purine nucleoside phosphorylase studied by analytical ultracentrifugation and CD spectroscopy.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables glycosyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables guanosine phosphorylase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables pentosyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables purine-nucleoside phosphorylase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables purine-nucleoside phosphorylase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables purine-nucleoside phosphorylase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    acts_upstream_of_or_within DNA damage response IEP
    Inferred from Expression Pattern
    more info
    		 PubMed 
    involved_in nucleoside catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in nucleoside metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in purine nucleoside catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within purine nucleoside catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within purine nucleoside interconversion IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in purine nucleoside metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol HDA PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane HDA PubMed 

    General protein information

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    Preferred Names
    purine nucleoside phosphorylase
    NP_418801.1

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      4620883..4621602
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418801.1 purine nucleoside phosphorylase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418801.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A418GHN3
      Conserved Domains (1) summary
      PRK05819
      Location:2 → 236
      deoD; DeoD-type purine-nucleoside phosphorylase
    Nucleotide Protein
    Heading Accession and Version

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