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    nudB dihydroneopterin triphosphate diphosphatase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946383, updated on 17-Dec-2024

    Summary

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    Official Symbol
    nudB
    Official Full Name
    dihydroneopterin triphosphate diphosphatase
    Primary source
    ECOCYC:EG11138
    Locus tag
    b1865
    See related
    ASAP:ABE-0006223
    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
    ECK1866; ntpA; yebD
    Summary
    A nudB mutant has reduced folate synthesis (Gabelli, 2007). [More information is available at EcoGene: EG11138]. Dihydroneopterin triphosphate pyrophosphohydrolase (DHNTPase) catalyzes the hydrolytic removal of pyrophosphate from dihydroneopterin triphosphate (DHNTP) to yield dihydroneopterin phosphate as a product. [More information is available at EcoCyc: EG11138].
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    Genomic context

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    Sequence:
    NC_000913.3 (1948180..1948632, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene crossover junction endodeoxyribonuclease RuvC Neighboring gene putative transcriptional regulator YebC Neighboring gene aspartate--tRNA ligase Neighboring gene isochorismatase family protein YecD Neighboring gene DUF72 domain-containing protein YecE

    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. Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis. Gabelli SB, et al. Structure, 2007 Aug. PMID 17698004
    2. Metal ion coordination in the E. coli Nudix hydrolase dihydroneopterin triphosphate pyrophosphatase: New clues into catalytic mechanism. Hill SE, et al. PLoS One, 2017. PMID 28742822, Free PMC Article
    3. Purification of the MutX protein of Streptococcus pneumoniae, a homologue of Escherichia coli MutT. Identification of a novel catalytic domain for nucleoside triphosphate pyrophosphohydrolase activity. Bullions LC, et al. J Biol Chem, 1994 Apr 22. PMID 8163538
    4. Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme. O'Handley SF, et al. J Biol Chem, 1996 Oct 4. PMID 8798731
    5. Dual hydrolysis of diphosphate and triphosphate derivatives of oxidized deoxyadenosine by Orf17 (NtpA), a MutT-type enzyme. Hori M, et al. DNA Repair (Amst), 2005 Jan 2. PMID 15533835

    See all (19) citations in PubMed

    GeneRIFs: Gene References Into Functions

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables dATP diphosphatase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables dATP diphosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables dihydroneopterin triphosphate pyrophosphohydrolase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables dihydroneopterin triphosphate pyrophosphohydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in folic acid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in folic acid biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in tetrahydrofolate biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    dihydroneopterin triphosphate diphosphatase
    NP_416379.1

    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
      1948180..1948632 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416379.1 dihydroneopterin triphosphate diphosphatase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416379.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A061YJ43, A0A0H3MJX1, A0A192C832, A0AA36KY21, F4T0J5
      Conserved Domains (1) summary
      PRK09438
      Location:4 → 150
      nudB; dihydroneopterin triphosphate pyrophosphatase; Provisional
    Nucleotide Protein
    Heading Accession and Version

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