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Information on EC 3.6.1.23 - dUTP diphosphatase and Organism(s) Sulfolobus islandicus rod-shaped virus 1 and UniProt Accession O71028

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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:
Sulfolobus islandicus rod-shaped virus 1
UNIPROT: O71028
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Word Map
The taxonomic range for the selected organisms is: Sulfolobus islandicus rod-shaped virus 1
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
dutpase, deoxyuridine triphosphatase, deoxyuridine triphosphate nucleotidohydrolase, dut-n, deoxyuridine 5'-triphosphate nucleotidohydrolase, deoxyuridine 5'-triphosphate, dutp pyrophosphatase, dutp nucleotidohydrolase, orf 54, dcd-dut, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
desoxyuridine 5'-triphosphatase
-
-
-
-
desoxyuridine 5'-triphosphate nucleotidohydrolase
-
-
-
-
desoxyuridine-triphosphatase
-
-
-
-
dUTP pyrophosphatase
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-
-
-
dUTPase
-
-
-
-
P18
-
-
-
-
PIP4
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphorous acid anhydride hydrolysis
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
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
-
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
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Sulfolobus islandicus rod-shaped virus SIRV
Uniprot
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DUT_SIRV1
158
0
17906
Swiss-Prot
other Location (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Prangishvili, D.; Klenk, H.P.; Jacobs, G.; Schmiechen, A.; Hanselmann, C.; Holz, I.; Zillig, W.
Biochemical and phylogenetic characterization of the dUTPase from the archaeal virus SIRV
J. Biol. Chem.
273
6024-6029
1998
Sulfolobus islandicus rod-shaped virus 1 (O71028), Sulfolobus islandicus rod-shaped virus 1
Manually annotated by BRENDA team