Dihydroneopterin triphosphate pyrophosphatase (P0AFC0)

Identification
Name:Dihydroneopterin triphosphate pyrophosphatase
Synonyms:
  • dATP pyrophosphohydrolase
Gene Name:nudB
Enzyme Class:Not Available
Biological Properties
General Function:Involved in dATP pyrophosphohydrolase activity
Specific Function:Catalyzes the hydrolysis of dihydroneopterin triphosphate to dihydroneopterin monophosphate and pyrophosphate. Required for efficient folate biosynthesis. Can also hydrolyze nucleoside triphosphates with a preference for dATP
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Pyrophosphate+1.0Thumb+1.0Thumb
1.07,8-dihydroneopterin 3'-triphosphate + 1.0Water → 1.0Pyrophosphate + 1.0Hydrogen ion + 1.0Dihydroneopterin monophosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Dihydroneopterin triphosphate + 1.0Water → 1.0Dihydroneopterin monophosphate + 1.0Hydrogen ion + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0dATP + 1.0Water → 1.0Deoxyadenosine monophosphate + 1.0Hydrogen ion + 1.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB242457,8-dihydroneopterin 3'-triphosphateMetaboCard
ECMDB01532dATPMetaboCard
ECMDB00905Deoxyadenosine monophosphateMetaboCard
ECMDB21206Dihydroneopterin monophosphateMetaboCard
ECMDB21452Dihydroneopterin phosphateMetaboCard
ECMDB01144Dihydroneopterin triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
dATP pyrophosphohydrolase activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
nucleoside-triphosphate diphosphatase activity
pyrophosphatase activity
Process
cellular macromolecule metabolic process
DNA metabolic process
DNA repair
macromolecule metabolic process
metabolic process
Gene Properties
Blattner:b1865
Gene OrientationCounterclockwise
Centisome Percentage:41.95
Left Sequence End1946204
Right Sequence End1946656
Gene Sequence:
>453 bp
ATGAATAACATACAAATAAGAAACTATCAGCCTGGCGATTTTCAGCAACTATGCGCTATT
TTCATTAGAGCGGTTACGATGACCGCCAGTCAGCATTATTCACCACAACAAATTTCCGCC
TGGGCGCAGATTGACGAATCTCGCTGGAAGGAGAAACTCGCGAAATCACAAGTGTGGGTT
GCGATCATTAATGCACAACCGGTTGGTTTTATTTCCCGCATTGAACATTATATCGATATG
TTATTTGTTGACCCTGAATACACCCGCCGTGGGGTTGCCAGCGCTTTGTTAAAACCTTTG
ATTAAGTCTGAATCCGAACTTACGGTGGACGCAAGCATAACCGCAAAACCCTTTTTTGAA
CGTTATGGTTTTCAGACAGTTAAGCAGCAGCGCGTTGAATGCCGGGGAGCGTGGTTTACT
AATTTTTATATGCGATATAAACCGCAACATTAA
Protein Properties
Pfam Domain Function:
Protein Residues:150
Protein Molecular Weight:17306
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Dihydroneopterin triphosphate pyrophosphatase
MKDKVYKRPVSILVVIYAQDTKRVLMLQRRDDPDFWQSVTGSVEEGETAPQAAMREVKEE
VTIDVVAEQLTLIDCQRTVEFEIFSHLRHRYAPGVTRNTESWFCLALPHERQIVFTEHLA
YKWLDAPAAAALTKSWSNRQAIEQFVINAA
References
External Links:
ResourceLink
Uniprot ID:P0AFC0
Uniprot Name:NUDB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4902969
Ecogene ID:EG11138
Ecocyc:EG11138
ColiBase:b1865
Kegg Gene:b1865
EchoBASE ID:EB1128
CCDB:NUDB_ECOLI
BacMap:16129818
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Bullions, L. C., Mejean, V., Claverys, J. P., Bessman, M. J. (1994). "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." J Biol Chem 269:12339-12344. Pubmed: 8163538
  • Gabelli, S. B., Bianchet, M. A., Xu, W., Dunn, C. A., Niu, Z. D., Amzel, L. M., Bessman, M. J. (2007). "Structure and function of the E. coli dihydroneopterin triphosphate pyrophosphatase: a Nudix enzyme involved in folate biosynthesis." Structure 15:1014-1022. Pubmed: 17698004
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • O'Handley, S. F., Frick, D. N., Bullions, L. C., Mildvan, A. S., Bessman, M. J. (1996). "Escherichia coli orf17 codes for a nucleoside triphosphate pyrophosphohydrolase member of the MutT family of proteins. Cloning, purification, and characterization of the enzyme." J Biol Chem 271:24649-24654. Pubmed: 8798731
  • Sharples, G. J., Lloyd, R. G. (1991). "Resolution of Holliday junctions in Escherichia coli: identification of the ruvC gene product as a 19-kilodalton protein." J Bacteriol 173:7711-7715. Pubmed: 1657895
  • Takahagi, M., Iwasaki, H., Nakata, A., Shinagawa, H. (1991). "Molecular analysis of the Escherichia coli ruvC gene, which encodes a Holliday junction-specific endonuclease." J Bacteriol 173:5747-5753. Pubmed: 1885548