Deoxyuridine 5'-triphosphate nucleotidohydrolase

Details

Name
Deoxyuridine 5'-triphosphate nucleotidohydrolase
Synonyms
  • 3.6.1.23
  • dUTP pyrophosphatase
  • dUTPase
Gene Name
dut
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Amino acid sequence
>lcl|BSEQ0051205|Deoxyuridine 5'-triphosphate nucleotidohydrolase
MSTTLAIVRLDPGLPLPSRAHDGDAGVDLYSAEDVELAPGRRALVRTGVAVAVPFGMVGL
VHPRSGLATRVGLSIVNSPGTIDAGYRGEIKVALINLDPAAPIVVHRGDRIAQLLVQRVE
LVELVEVSSFDEAGLASTSRGDGGHGSSGGHASL
Number of residues
154
Molecular Weight
15802.815
Theoretical pI
Not Available
GO Classification
Functions
dUTP diphosphatase activity / magnesium ion binding
Processes
dUMP biosynthetic process / dUTP catabolic process / dUTP metabolic process / growth
General 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.
Specific Function
Dutp diphosphatase activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0051206|Deoxyuridine 5'-triphosphate nucleotidohydrolase (dut)
GTGTCGACCACTCTGGCGATCGTCCGCCTCGACCCCGGGCTCCCGCTGCCCAGCCGCGCT
CACGACGGCGACGCCGGCGTTGATCTCTACAGCGCCGAAGACGTCGAGCTGGCACCTGGG
CGCCGCGCCCTGGTACGGACGGGTGTTGCGGTCGCCGTCCCGTTCGGCATGGTCGGGCTG
GTCCATCCGCGCTCCGGGTTGGCCACGCGGGTGGGGCTTTCGATCGTCAACAGTCCGGGC
ACCATCGACGCGGGTTATCGTGGGGAGATCAAGGTGGCCCTGATCAACTTGGACCCAGCC
GCGCCCATCGTGGTACATCGCGGTGACCGAATCGCCCAGTTGCTAGTGCAACGGGTTGAG
TTGGTCGAGCTGGTCGAGGTCTCGTCGTTCGACGAGGCCGGGCTGGCCTCGACATCCCGC
GGCGACGGTGGCCACGGTTCCTCCGGCGGACATGCGAGTTTGTGA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP9WNS5
UniProtKB Entry NameDUT_MYCTU
General References
  1. Cole ST, Brosch R, Parkhill J, Garnier T, Churcher C, Harris D, Gordon SV, Eiglmeier K, Gas S, Barry CE 3rd, Tekaia F, Badcock K, Basham D, Brown D, Chillingworth T, Connor R, Davies R, Devlin K, Feltwell T, Gentles S, Hamlin N, Holroyd S, Hornsby T, Jagels K, Krogh A, McLean J, Moule S, Murphy L, Oliver K, Osborne J, Quail MA, Rajandream MA, Rogers J, Rutter S, Seeger K, Skelton J, Squares R, Squares S, Sulston JE, Taylor K, Whitehead S, Barrell BG: Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature. 1998 Jun 11;393(6685):537-44. [Article]
  2. Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A: Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3. [Article]
  3. Chan S, Segelke B, Lekin T, Krupka H, Cho US, Kim MY, So M, Kim CY, Naranjo CM, Rogers YC, Park MS, Waldo GS, Pashkov I, Cascio D, Perry JL, Sawaya MR: Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into the catalytic mechanism. J Mol Biol. 2004 Aug 6;341(2):503-17. [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