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
- FunctionsdUTP diphosphatase activity / magnesium ion bindingProcessesdUMP biosynthetic process / dUTP catabolic processComponentscytoplasm / 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
- dUTPase (PF00692)
- 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
Resource Link UniProtKB ID P06968 UniProtKB Entry Name DUT_ECOLI GenBank Protein ID 41297 GenBank Gene ID X01714 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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 ID Name Drug group Pharmacological action? Actions Details DB01965 2'-Deoxyuridine 5'-alpha,beta-imido-triphosphate experimental unknown Details DB02333 Deoxyuridine-5'-Triphosphate experimental unknown Details DB03413 Deoxyuridine-5'-Diphosphate experimental unknown Details DB03800 Deoxyuridine monophosphate experimental unknown Details