Deoxyuridine 5'-triphosphate nucleotidohydrolase

Details

Name
Deoxyuridine 5'-triphosphate nucleotidohydrolase
Synonyms
  • 3.6.1.23
  • dnaS
  • dUTP pyrophosphatase
  • dUTPase
  • sof
Gene Name
dut
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0019104|Deoxyuridine 5'-triphosphate nucleotidohydrolase
MKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLNDAVELAPGDTTLVPTGLAIHIAD
PSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMISVWNRGQDSFTIQPGERIAQMI
FVPVVQAEFNLVEDFDATDRGEGGFGHSGRQ
Number of residues
151
Molecular Weight
16155.34
Theoretical pI
4.87
GO Classification
Functions
dUTP diphosphatase activity / magnesium ion binding
Processes
dUMP biosynthetic process / dUTP catabolic process
Components
cytoplasm / cytosol
General Function
Magnesium ion binding
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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasmic
Gene sequence
>lcl|BSEQ0019105|Deoxyuridine 5'-triphosphate nucleotidohydrolase (dut)
ATGAAAAAAATCGACGTTAAGATTCTGGACCCGCGCGTTGGGAAGGAATTTCCGCTCCCG
ACTTATGCCACCTCTGGCTCTGCCGGACTTGACCTGCGTGCCTGTCTCAACGACGCCGTA
GAACTGGCTCCGGGTGACACTACGCTGGTTCCGACCGGGCTGGCGATTCATATTGCCGAT
CCTTCACTGGCGGCAATGATGCTGCCGCGCTCCGGATTGGGACATAAGCACGGTATCGTG
CTTGGTAACCTGGTAGGATTGATCGATTCTGACTATCAGGGCCAGTTGATGATTTCCGTG
TGGAACCGTGGTCAGGACAGCTTCACCATTCAACCTGGCGAACGCATCGCCCAGATGATT
TTTGTTCCGGTAGTACAGGCTGAATTTAATCTGGTGGAAGATTTCGACGCCACCGACCGC
GGTGAAGGCGGCTTTGGTCACTCTGGTCGTCAGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP06968
UniProtKB Entry NameDUT_ECOLI
GenBank Protein ID41297
GenBank Gene IDX01714
General References
  1. Lundberg LG, Thoresson HO, Karlstrom OH, Nyman PO: Nucleotide sequence of the structural gene for dUTPase of Escherichia coli K-12. EMBO J. 1983;2(6):967-71. [Article]
  2. Burland V, Plunkett G 3rd, Daniels DL, Blattner FR: DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication. Genomics. 1993 Jun;16(3):551-61. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  6. Cedergren-Zeppezauer ES, Larsson G, Nyman PO, Dauter Z, Wilson KS: Crystal structure of a dUTPase. Nature. 1992 Feb 20;355(6362):740-3. [Article]
  7. Larsson G, Svensson LA, Nyman PO: Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP). Nat Struct Biol. 1996 Jun;3(6):532-8. [Article]
  8. Dauter Z, Wilson KS, Larsson G, Nyman PO, Cedergren-Zeppezauer ES: The refined structure of dUTPase from Escherichia coli. Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):735-49. [Article]
  9. Gonzalez A, Larsson G, Persson R, Cedergren-Zeppezauer E: Atomic resolution structure of Escherichia coli dUTPase determined ab initio. Acta Crystallogr D Biol Crystallogr. 2001 Jun;57(Pt 6):767-74. Epub 2001 May 25. [Article]
  10. Barabas O, Pongracz V, Kovari J, Wilmanns M, Vertessy BG: Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase. J Biol Chem. 2004 Oct 8;279(41):42907-15. Epub 2004 Jun 17. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB019652'-Deoxyuridine 5'-alpha,beta-imido-triphosphateexperimentalunknownDetails
DB02333Deoxyuridine-5'-TriphosphateexperimentalunknownDetails
DB03413Deoxyuridine-5'-DiphosphateexperimentalunknownDetails
DB03800Deoxyuridine monophosphateexperimentalunknownDetails