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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
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