3.2.2.27: uracil-DNA glycosylase
This is an abbreviated version!
For detailed information about uracil-DNA glycosylase, go to the full flat file.
Word Map on EC 3.2.2.27
-
3.2.2.27
-
deamination
-
cytosine
-
glycosylases
-
endonuclease
-
thymine
-
abasic
-
misincorporation
-
ung2
-
uracil-containing
-
duplex
-
hypermutation
-
dump
-
deoxyuridine
-
activation-induced
-
excises
-
mispairs
-
base-excision
-
dutpase
-
8-oxoguanine
-
apyrimidinic
-
5-methylcytosine
-
5-hydroxymethyluracil
-
g-quadruplexes
-
transversions
-
ape1
-
thymine-dna
-
formamidopyrimidine
-
5-hydroxyuracil
-
short-patch
-
xrcc1
-
apurinic
-
class-switching
-
3,n4-ethenocytosine
-
translesion
-
post-replicative
-
ap-endonuclease
-
aid-induced
-
apobec3g
-
drug development
-
molecular biology
-
analysis
-
medicine
- 3.2.2.27
-
deamination
- cytosine
- glycosylases
- endonuclease
- thymine
-
abasic
-
misincorporation
- ung2
-
uracil-containing
- duplex
-
hypermutation
- dump
- deoxyuridine
-
activation-induced
-
excises
- mispairs
-
base-excision
- dutpase
- 8-oxoguanine
-
apyrimidinic
- 5-methylcytosine
- 5-hydroxymethyluracil
-
g-quadruplexes
-
transversions
- ape1
-
thymine-dna
- formamidopyrimidine
- 5-hydroxyuracil
-
short-patch
- xrcc1
-
apurinic
-
class-switching
- 3,n4-ethenocytosine
-
translesion
-
post-replicative
- ap-endonuclease
-
aid-induced
- apobec3g
- drug development
- molecular biology
- analysis
- medicine
Reaction
Hydrolyses single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil =
Synonyms
5-formyluracil-DNA glycosylase, AFUDG, Afung protein, Blr0248, DNA N-glycosylase, dr0689, DR_0968, endonuclease VIII, family 1 uracil N-glycosylase, family 4 UDGa, family 4 uracil-DNA glycosylase, HMUDG, mismatch-specific uracil-DNA glycosylase, MjUDG, More, MtuNei1, MUG, Pa-UDG, PF1385, PfuUDG, single-strand selective monofunctional uracil-DNA glycosylase, single-strand selective uracil DNA glycosylase, single-strand-selective mono-functional uracil-DNA glycosylase, single-strand-selective monofunctional uracil DNA glycosylase, single-strand-selective monofunctional uracil-DNA glycosylase, single-stranded monofunctional uracil DNA N-glycosylase, SMUG1, SMUG1-like glycosylase, STK_22380, Ta0477, TD12-encoded protein, Thd1p, Thp1p, TMUDG, type 1 UDG, UDG, UDG1, UDGa, UdgB, UDGIV, UDGV, UL114, UL2, UNG, UNG-1, Ung-type uracil glycosylase, UNG1, UNG2, Unga, uracil DNA glycosylase, uracil DNA glycosylase 2, uracil DNA-glycosylase, uracil DNA-glycosylase 2, uracil-DNA glycosylase, uracil-DNA glycosylase 2, uracil-DNA glycosylase a, uracil-DNA N-glycosylase, uracil-N-glycosylase 2
ECTree
3.2.2.27 uracil-DNA glycosylaseAdvanced search results
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results (Natural Substrates Products
Natural Substrates Products on EC 3.2.2.27 - uracil-DNA glycosylase
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NATURAL SUBSTRATE 
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
3,N4-ethenocytosine-mismatched single-stranded DNA + H2O
3,N4-ethenocytosine + single-stranded DNA with abasic site
-
-
-
?
5-fluorouracil-mismatched double-stranded DNA + H2O
5-fluorouracil + double-stranded DNA with abasic site
5-formyluracil-mismatched double-stranded DNA + H2O
5-formyluracil + double-stranded DNA with abasic site
5-formyluracil-mismatched single-stranded DNA + H2O
5-formyluracil + single-stranded DNA with abasic site
-
-
-
?
5-hydroxymethyl-uracil-mismatched double-stranded DNA + H2O
5-hydroxymethyl-uracil + double-stranded DNA with abasic site
the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates
-
-
?
5-hydroxymethyl-uracil-mismatched single-stranded DNA + H2O
5-hydroxymethyl-uracil + single-stranded DNA with abasic site
the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates
-
-
?
5-hydroxymethyluracil-mismatched double-stranded DNA + H2O
5-hydroxymethyluracil + double-stranded DNA with abasic site
-
-
-
?
5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
5-hydroxyuracil-mismatched double-stranded DNA + H2O
5-hydroxyuracil + double-stranded DNA with abasic site
-
-
-
?
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
5-methylcytosine-mismatched double-stranded DNA + H2O
5-methylcytosine + double-stranded DNA with abasic site
-
-
-
?
ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
UDGb is active on ethenocytosine-G
-
-
?
hypoxanthine-mismatched double-stranded DNA + H2O
hypoxanthine + double-stranded DNA with abasic site
the UDGb from Pyrobaculum aerophilum, belonging to a fifth UDG family, catalyzes the removal of uracil as well as of hypoxanthine from DNA by cleavage of e.g. hypoxanthine-thymine pairs, possessing an active site, that lacks the polar amino acid residue, see also EC 3.2.2.15, substrate specificity and active site structure, overview
-
-
?
thymine-mismatched double-stranded DNA + H2O
thymine + double-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
-
-
-
?
3,N4-ethenocytosine-mismatched double-stranded DNA + H2O
3,N4-ethenocytosine + double-stranded DNA with abasic site
-
-
-
?
5-fluorouracil-mismatched double-stranded DNA + H2O
5-fluorouracil + double-stranded DNA with abasic site
-
-
-
?
5-fluorouracil-mismatched double-stranded DNA + H2O
5-fluorouracil + double-stranded DNA with abasic site
UDGb is active on 5-fluorouracil-G pairs
-
-
?
5-fluorouracil-mismatched double-stranded DNA + H2O
5-fluorouracil + double-stranded DNA with abasic site
-
-
-
?
5-formyluracil-mismatched double-stranded DNA + H2O
5-formyluracil + double-stranded DNA with abasic site
-
-
-
?
5-formyluracil-mismatched double-stranded DNA + H2O
5-formyluracil + double-stranded DNA with abasic site
-
-
-
-
?
5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
-
-
-
?
5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
-
-
-
?
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
-
-
-
?
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
-
-
-
?
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
isoform UNG1, which in contrast to isoform UNG2 lacks a PCNA-binding motif, may be specialized to act on single stranded DNA (ssDNA) through its ability to bind ssDNA-binding protein RPA
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
isoform UNG1, which in contrast to isoform UNG2 lacks a PCNA-binding motif, may be specialized to act on single stranded DNA (ssDNA) through its ability to bind ssDNA-binding protein RPA
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-containing single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the enzyme removes uracil from DNA, which can occur by misincorporation of dUMP in place of dTMP during DNA synthesis or by deamination of cytosine, resulting in U-A or U-G mispairs
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
family 2 mismatch-specific uracil DNA glycosylase (MUG) is known to exhibit glycosylase activity on three mismatched base pairs, T/U, G/U and C/U. Family 1 uracil N-glycosylase (UNG) is an extremely efficient enzyme that can remove uracil from any uracil-containing base pairs including the A/U base pair
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the enzyme initiates repair of uracil-DNA is achieved in a base-excision pathway
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
cytosine bases can be deaminated spontaneously to uracil, causing DNA damage. Uracil-DNA glycosylase repairs this kind of DNA damage
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
cytosine bases can be deaminated spontaneously to uracil, causing DNA damage. Uracil-DNA glycosylase repairs this kind of DNA damage
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
under physiological conditions of 60 mM NaCl, pH 7.5, increasing amounts of viral UNG cleave both 45mer U-G and PS-U oligonucleotides. Monkeypox virus, which occurs naturally in Africa, can cause a smallpoxlike disease in humans. The DNA repair protein uracil-DNA glycosylase, UNG, is one of the viral enzymes important for poxvirus pathogenesis, thus inhibition of UNG is a therapeutic strategy, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
under physiological conditions of 60 mM NaCl, pH 7.5, increasing amounts of viral UNG cleave both 45mer U-G and PS-U oligonucleotides. Monkeypox virus, which occurs naturally in Africa, can cause a smallpoxlike disease in humans. The DNA repair protein uracil-DNA glycosylase, UNG, is one of the viral enzymes important for poxvirus pathogenesis, thus inhibition of UNG is a therapeutic strategy, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
the highly preferred substrate of UDGa is uracil mispaired with guanine, followed by A-U pairs, no activity with hydroxymethyl-uracil mispaired with guanine, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
the formation of archaeal chromatin is highly repressive to UDG1 activity, mechanistic basis for coupling UDG1 to the replication fork, modelling, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
UDG is a DNA repair enzyme removing uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP, and it is the primary activity in the DNA base excision repair pathway, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
UDG is a DNA repair enzyme removing uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP, and it is the primary activity in the DNA base excision repair pathway, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
Q7WYV4
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q7WYV4
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
the DNA repair protein uracil-DNA glycosylase is one of the viral enzymes important for poxvirus pathogenesis, it is part of the base excision repair pathway, BER
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
UDG catalyzes excision of uracil from DNA. The viral UDG plays an essential role in viral replication as a component of the DNA polymerase processivity factor. It adopts a catalysis-independent role in DNA replication that involves interaction with a viral protein, A20, to form the processivity factor. UDG-A20 association is essential for assembling of the processive DNA polymerase complex, overview
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
family 2 mismatch-specific uracil DNA glycosylase (MUG) is known to exhibit glycosylase activity on three mismatched base pairs, T/U, G/U and C/U. Family 1 uracil N-glycosylase (UNG) is an extremely efficient enzyme that can remove uracil from any uracil-containing base pairs including the A/U base pair
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Monkeypox virus, which occurs naturally in Africa, can cause a smallpox-like disease in humans. The DNA repair protein uracil-DNA glycosylase, UNG, is one of the viral enzymes important for poxvirus pathogenesis, thus inhibition of UNG is a therapeutic strategy, overview
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Monkeypox virus, which occurs naturally in Africa, can cause a smallpox-like disease in humans. The DNA repair protein uracil-DNA glycosylase, UNG, is one of the viral enzymes important for poxvirus pathogenesis, thus inhibition of UNG is a therapeutic strategy, overview
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
UDGs of the four UDG families catalyze the removal of uracil from DNA by flipping it out of the double helix into their binding pockets, where the glycosidic bond is hydrolyzed by a water molecule activated by an aromatic amino acid, while the UDGb from Pyrobaculum aerophilum, belonging to a fifth UDG family, catalyzes the removal of uracil, possessing an active site, that lacks the polar amino acid residue, see also EC 3.2.2.15, substrate specificity and active site structure, overview
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Q7WYV4
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q7WYV4
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
?
uracil-mismatched single-stranded DNA + H2O
uracil + single-stranded DNA with abasic site
-
-
-
-
?
additional information
?
-
-
AtUNG is the major UDG activity in Arabidopsis thaliana AtUNG excises uracil in vivo but generates toxic AP sites when processing abundant U:A pairs in dTTP-depleted cells
-
-
?
additional information
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5-methylcytosine and thymine derivatives are processed with an appreciable efficiency only by the human and the Drosophila enzymes
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additional information
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5-methylcytosine and thymine derivatives are processed with an appreciable efficiency only by the human and the Drosophila enzymes
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additional information
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family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family
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additional information
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uracil-DNA glycosylases are ubiquitously found enzymes that hydrolyze the N-glycosidic bond of deoxyuridine, generating from deamination of cytosine, in DNA, UNG enzymes specifically excise Ura bases from both double-stranded and single-stranded DNA with a slight preference for the latter substrate, and shows no activity against normal DNA bases or against uracil in RNA. As potentially mutagenic and deleterious for cell regulation, uracil must be removed from DNA
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dual role of hSMUG1 as a backup enzyme for UNG and a primary repair enzyme for a subset of oxidized pyrimidines such as 5-formyluracil, 5-hydroxymethyluracil, and 5-hydroxyuracil
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additional information
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dual role of hSMUG1 as a backup enzyme for UNG and a primary repair enzyme for a subset of oxidized pyrimidines such as 5-formyluracil, 5-hydroxymethyluracil, and 5-hydroxyuracil
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additional information
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family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family
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additional information
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hSMUG1 removes uracil from both double- and single-stranded DNA in nuclear chromatin, hSMUG1 has a broad substrate specificity, including 5-hydroxymethyluracil, and 3,N4-ethenocytosine. hSMUG1 acts as a broad specificity backup and is the major 5-hydroxymethyluracil-DNA glycosylase in nuclear cell extracts, overview
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additional information
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hSMUG1 removes uracil from both double- and single-stranded DNA in nuclear chromatin, hSMUG1 has a broad substrate specificity, including 5-hydroxymethyluracil, and 3,N4-ethenocytosine. hSMUG1 acts as a broad specificity backup and is the major 5-hydroxymethyluracil-DNA glycosylase in nuclear cell extracts, overview
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hSMUG1 removes uracil from both double- and single-stranded DNA, including 5-hydroxy-2'-deoxyuridine and 5-carboxy-2'-deoxyuridine, substrate selectivity mechanism, overview
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additional information
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hSMUG1 removes uracil from both double- and single-stranded DNA, including 5-hydroxy-2'-deoxyuridine and 5-carboxy-2'-deoxyuridine, substrate selectivity mechanism, overview
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hUNG2 removes uracil from both double- and single-stranded DNA in nuclear chromatin. hUNG2 in nuclear extracts initiates base excision repair of plasmids containing either U-A and U-G in vitro. hUNG2 is responsible for both prereplicative removal of deaminated cytosine and postreplicative removal of misincorporated uracil at the replication fork, it is the major enzyme for removal of deaminated cytosine outside of replication foci, overview
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additional information
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hUNG2 removes uracil from both double- and single-stranded DNA in nuclear chromatin. hUNG2 in nuclear extracts initiates base excision repair of plasmids containing either U-A and U-G in vitro. hUNG2 is responsible for both prereplicative removal of deaminated cytosine and postreplicative removal of misincorporated uracil at the replication fork, it is the major enzyme for removal of deaminated cytosine outside of replication foci, overview
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additional information
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UDG initiates DNA base excision repair, BER, by hydrolyzing the uracil base from the deoxyribose. BER repairs a wide range of base lesions through the use of many different DNA glycosylases specific for distinct types of DNA damage, UDG activity is cell-cycle dependent and generally higher in proliferating cells than in non-cycling cells, overview
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UNG2 is an important enzyme in the base excision repair pathway, interaction with Ugene is involved in the phenotype of colon cancer, Ugene interacts with the base excision repair pathway, overview
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additional information
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uracil DNA glycosylase acts in removing uracil from the sugar backbone of DNA, leaving abasic sites and initiating the uracil base-excision-repair pathway, BER. The human UNG2 enzyme, but not UNG1, is packaged and incorporated into HIV-1 virions via specific interaction with the integrase domain of the Gag-Pol precursor, the virally Vpr protein might also able to mediate the incorporation of UNG2, packaged UNG2 can process uracil from DNA, indicating that HIV-1 has the ability to control dUTP misincorporation in viral DNA, the enzyme is essential to the HIV-1 life cycle. HIV-1 RT and UNG2 recombinant proteins can process uracil from primer-template substrate, molecular mechanism
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additional information
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hSMUG1 shows excision activity for 5-formyluracil, a major thymine lesion formed by ionizing radiation, opposite all normal bases in DNA
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additional information
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UNG2 of the human host is required by HIV-1 strain R5, but not by X4HIV, during the early stage of infection
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additional information
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uracil DNA glycosylase does not show any activity on G:IU, i.e. iodouridine, or A:IU mispairs
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additional information
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uracil in single-stranded DNA, resulting from incorporation of dUMP during replication and from spontaneous or enzymatic deamination of cytosine, causing U:A pairs or U:G mismatches, respectively, has to be removed by the enzyme. Nuclear UNG2 is apparently the sole contributor to the post-replicative repair of U:A lesions and to the removal of uracil from U:G contexts in immunoglobulin genes as part of somatic hypermutation and class-switch recombination processes in adaptive immunity. UNG2 and SMUG1 contribute to U:G repair. UNG2 is highly specific for uracil, SMUG1 also efficiently removes 5-hydroxymethyluracil
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additional information
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uracil-DNA glycosylases are ubiquitously found enzymes that hydrolyze the N-glycosidic bond of deoxyuridine, generating from deamination of cytosine, in DNA, UNG enzymes specifically excise Ura bases from both double-stranded and single-stranded DNA with a slight preference for the latter substrate, and shows no activity against normal DNA bases or against uracil in RNA. As potentially mutagenic and deleterious for cell regulation, uracil must be removed from DNA
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additional information
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family-1 enzymes are active against uracil in ssDNA and dsDNA, and recognise uracil explicitly in an extrahelical conformation via a combination of protein and bound-water interactions. Extrahelical recognition requires an efficient process of substrate location by base-sampling probably by hopping or gliding along the DNA. Family-2 enzymes are mismatch specific and explicitly recognise the widowed guanine on the complementary strand rather than the extrahelical scissile pyrimidine. Although structures are not yet available for family-3/SMUG and family-4 enzymes, sequence analysis suggests similar overall folds, and identifies common active site motifs but with a surprising lack of conservation of catalytic residues between members of the super-family
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additional information
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viral uracil DNA glycosylase, UL2, in conjunction with the HSV-1 DNA polymerase catalytic subunit, UL30, cellular AP endonuclease and DNA ligase IIIalpha/XRCC1, perform uracil-initiated base excision repair. UL30 exhibits apurinic/apyrimidinic and 5'-deoxyribose phosphate lyase activities. UL2 and UL30 co-localize to viral prereplicative sites. The interaction between HSV-1 proteins UL2 and Pol occurs in HSV-1 infected cells
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UL114 and DNA polymerase catalytic subunit UL54 act in concert during base excision repair of the viral genome
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additional information
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DNA uracil repair occurs ubiquitously throughout all existant life forms. Base excision repair is triggered by a uracil DNA glycosylase, UDG. The organism uniquely initiates DNA repair by direct strand incision next to the DNA-U residue, a reaction catalyzed by the DNA uridine endonuclease Mth212, detailed mechanism, overview
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additional information
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DNA uracil repair occurs ubiquitously throughout all existant life forms. Base excision repair is triggered by a uracil DNA glycosylase, UDG. The organism uniquely initiates DNA repair by direct strand incision next to the DNA-U residue, a reaction catalyzed by the DNA uridine endonuclease Mth212, detailed mechanism, overview
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SMUG1 is specialized for antimutational uracil excision in mammalian cells. Ung knockout mice display no increase in mutation frequency due to the second UDG activity, SMUG1
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deamination of cytosine in DNA leads to formation of uracil, which is removed by uracil DNA glycosylase, UNG. The N-terminus of UNG is required for class switch recombination activity, overview
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additional information
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uracil in single-stranded DNA, resulting from incorporation of dUMP during replication and from spontaneous or enzymatic deamination of cytosine, causing U:A pairs or U:G mismatches, respectively, has to be removed by the enzyme. Nuclear UNG2 is apparently the sole contributor to the post-replicative repair of U:A lesions and to the removal of uracil from U:G contexts in immunoglobulin genes as part of somatic hypermutation and class-switch recombination processes in adaptive immunity. UNG2 and SMUG1 contribute to U:G repair. UNG2 is highly specific for uracil, SMUG1 also efficiently removes 5-hydroxymethyluracil
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additional information
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MtuNei1 recognizes oxidized pyrimidines on both double-stranded and single-stranded DNA and exhibits uracil DNA glycosylase activity. MtuNei2 and MtuNei1 can prevent G to T transversions probably by removing oxidized guanine products, such as Sp and urea
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additional information
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MtuNei1 recognizes oxidized pyrimidines on both double-stranded and single-stranded DNA and exhibits uracil DNA glycosylase activity. MtuNei2 and MtuNei1 can prevent G to T transversions probably by removing oxidized guanine products, such as Sp and urea
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UDG initiates uracil excision repair to safeguard the genomic integrity, mechanism, overview
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UdgB removes aberrant bases uracil, from deaminated cytosine, and hypoxanthine, from deaminated adenine, and 5-fluorouracil from DNA with high efficiency
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additional information
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UDG initiates uracil excision repair to safeguard the genomic integrity, mechanism, overview
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the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates, no activity on G-T pairs, overview
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additional information
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the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates, no activity on G-T pairs, overview
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additional information
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the preferred substrate of UDGb is hydroxymethyl-uracil mispaired with guanine, followed by G-U and A-U, UDGb is active on ethenocytosine-G and 5-fluorouracil-G pairs, and UDGb also performs processing of uracil and hydroxymethyluracil from single-stranded DNA, but highly prefers double-stranded DNA substrates, no activity on G-T pairs, overview
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Q7WYV4
UDG is an essential enzyme for maintaining the integrity of genomic information, it is the first enzyme of a base excision repair, BER, pathway that corrects uracil lesions. TthUDG specifically recognizes uracil that is flipped out from double-stranded DNA, in a manner similar to that of the family 1 human UDG, rather than binding to the guanine base of the complementary strand in mismatched DNA, as does the family 2 Escherichia coli MUG
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UDG removes uracil generated by the deamination of cytosine or misincorporation of deoxyuridine monophosphate. The fifth UDG family lacks a polar residue in the active-site motif, which mediates the hydrolysis of the glycosidic bond by activation of a water molecule in UDG families 1 to 4
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
UDG removes uracil generated by the deamination of cytosine or misincorporation of deoxyuridine monophosphate. The fifth UDG family lacks a polar residue in the active-site motif, which mediates the hydrolysis of the glycosidic bond by activation of a water molecule in UDG families 1 to 4
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additional information
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Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Q7WYV4
UDG is an essential enzyme for maintaining the integrity of genomic information, it is the first enzyme of a base excision repair, BER, pathway that corrects uracil lesions. TthUDG specifically recognizes uracil that is flipped out from double-stranded DNA, in a manner similar to that of the family 1 human UDG, rather than binding to the guanine base of the complementary strand in mismatched DNA, as does the family 2 Escherichia coli MUG
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