Deoxyuridine 5'-triphosphate nucleotidohydrolase (P06968)

Identification
Name:Deoxyuridine 5'-triphosphate nucleotidohydrolase
Synonyms:
  • dUTPase
  • dUTP pyrophosphatase
Gene Name:dut
Enzyme Class:
Biological Properties
General Function:Involved in hydrolase activity
Specific Function:This enzyme is involved in nucleotide metabolism:it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Deoxyuridine triphosphate + 1.0Water ↔ 1.0dUMP + 1.0Hydrogen ion + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Deoxyuridine triphosphate + 1.0Water ↔ 1.0dUMP + 1.0Pyrophosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Deoxyuridine triphosphate + 1.0Water → 1.0Phosphate + 1.0Hydrogen ion + 1.0dUMP
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Deoxyuridine triphosphate + 1.0Water ↔ 1.0dUMP + 1.0Hydrogen ion + 1.0Pyrophosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Deoxyuridine triphosphate + 1.0Water → 1.0dUMP + 1.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01191Deoxyuridine triphosphateMetaboCard
ECMDB01409dUMPMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
dUTP diphosphatase 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 nitrogen compound metabolic process
dUTP metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
pyrimidine deoxyribonucleoside triphosphate metabolic process
pyrimidine nucleoside triphosphate metabolic process
pyrimidine nucleotide metabolic process
Gene Properties
Blattner:b3640
Gene OrientationClockwise
Centisome Percentage:82.16
Left Sequence End3811955
Right Sequence End3812410
Gene Sequence:
>456 bp
TTGACTACTAACACTCATACTCTGCAGATTGAAGAGATTTTAGAACTTCTGCCGCACCGT
TTCCCGTTCTTACTGGTGGATCGCGTGCTGGATTTTGAAGAAGGTCGTTTTCTGCGCGCA
GTAAAAAATGTCTCTGTCAATGAGCCATTCTTCCAGGGCCATTTCCCTGGAAAACCGATT
TTCCCGGGTGTGCTGATTCTGGAAGCAATGGCACAGGCAACAGGTATTCTGGCGTTTAAA
AGCGTAGGAAAACTGGAACCGGGTGAGCTGTACTACTTCGCTGGTATTGACGAAGCGCGC
TTCAAGCGCCCGGTCGTGCCTGGCGATCAAATGATCATGGAAGTCACTTTCGAAAAAACG
CGCCGCGGCCTGACCCGTTTTAAAGGGGTTGCTCTGGTCGATGGTAAAGTAGTTTGCGAA
GCAACGATGATGTGTGCTCGTAGCCGGGAGGCCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:151
Protein Molecular Weight:16155
Protein Theoretical pI:5
PDB File:1EUW
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Deoxyuridine 5'-triphosphate nucleotidohydrolase
MKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLNDAVELAPGDTTLVPTGLAIHIAD
PSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMI
FVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ
References
External Links:
ResourceLink
Uniprot ID:P06968
Uniprot Name:DUT_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4902921
PDB ID:1EUW
Ecogene ID:EG10251
Ecocyc:EG10251
ColiBase:b3640
Kegg Gene:b3640
EchoBASE ID:EB0247
CCDB:DUT_ECOLI
BacMap:16131511
General Reference:
  • Barabas, O., Pongracz, V., Kovari, J., Wilmanns, M., Vertessy, B. G. (2004). "Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase." J Biol Chem 279:42907-42915. Pubmed: 15208312
  • 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
  • Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
  • Cedergren-Zeppezauer, E. S., Larsson, G., Nyman, P. O., Dauter, Z., Wilson, K. S. (1992). "Crystal structure of a dUTPase." Nature 355:740-743. Pubmed: 1311056
  • Dauter, Z., Wilson, K. S., Larsson, G., Nyman, P. O., Cedergren-Zeppezauer, E. S. (1998). "The refined structure of dUTPase from Escherichia coli." Acta Crystallogr D Biol Crystallogr 54:735-749. Pubmed: 9757088
  • Gonzalez, A., Larsson, G., Persson, R., Cedergren-Zeppezauer, E. (2001). "Atomic resolution structure of Escherichia coli dUTPase determined ab initio." Acta Crystallogr D Biol Crystallogr 57:767-774. Pubmed: 11375495
  • 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
  • Larsson, G., Svensson, L. A., Nyman, P. O. (1996). "Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP)." Nat Struct Biol 3:532-538. Pubmed: 8646539
  • Lundberg, L. G., Thoresson, H. O., Karlstrom, O. H., Nyman, P. O. (1983). "Nucleotide sequence of the structural gene for dUTPase of Escherichia coli K-12." EMBO J 2:967-971. Pubmed: 6139280