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Information on EC 3.6.1.23 - dUTP diphosphatase and Organism(s) Mycolicibacterium smegmatis and UniProt Accession A0QW08

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EC Tree
     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.1 In phosphorus-containing anhydrides
                3.6.1.23 dUTP diphosphatase
IUBMB Comments
The enzyme catalyses the Mg2+-dependent hydrolysis of dUTP to dUMP, providing the substrate for EC 2.1.1.45, thymidylate synthase, leading to production of thymidine nucleotides. By reducing the effective ratio of dUTP to TTP, the enzyme also reduces the possibility of dUTP incorporation into DNA.
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This record set is specific for:
Mycolicibacterium smegmatis
UNIPROT: A0QW08
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Word Map
The taxonomic range for the selected organisms is: Mycolicibacterium smegmatis
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
dutpase, deoxyuridine triphosphatase, deoxyuridine triphosphate nucleotidohydrolase, deoxyuridine 5'-triphosphate nucleotidohydrolase, dut-n, deoxyuridine 5'-triphosphate, dutp pyrophosphatase, dutp nucleotidohydrolase, orf 54, dcd-dut, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
deoxyuridine 5’-triphosphate nucleotidohydrolase
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desoxyuridine 5'-triphosphatase
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desoxyuridine 5'-triphosphate nucleotidohydrolase
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desoxyuridine-triphosphatase
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-
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dUTP pyrophosphatase
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dUTPase
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-
-
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P18
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-
-
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PIP4
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
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-
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PATHWAY SOURCE
PATHWAYS
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-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
dUTP nucleotidohydrolase
The enzyme catalyses the Mg2+-dependent hydrolysis of dUTP to dUMP, providing the substrate for EC 2.1.1.45, thymidylate synthase, leading to production of thymidine nucleotides. By reducing the effective ratio of dUTP to TTP, the enzyme also reduces the possibility of dUTP incorporation into DNA.
CAS REGISTRY NUMBER
COMMENTARY hide
37289-34-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
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-
-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dUTP + H2O
dUMP + diphosphate
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
dUTPase knock-out results in lethality
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
dUTPase is a target for antitubercular drugs
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Pecsi, I.; Hirmondo, R.; Brown, A.C.; Lopata, A.; Parish, T.; Vertessy, B.G.; Toth, J.
The dUTPase enzyme is essential in Mycobacterium smegmatis
PLoS ONE
7
e37461
2012
Mycolicibacterium smegmatis (A0QW08), Mycolicibacterium smegmatis, Mycobacterium tuberculosis (P9WNS5), Mycobacterium tuberculosis, Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 (A0QW08), Mycobacterium tuberculosis H37Rv (P9WNS5)
Manually annotated by BRENDA team