Any feedback?
Information on EC 3.2.2.27 - uracil-DNA glycosylase and Organism(s) Mycolicibacterium smegmatis and UniProt Accession A0QV01
for references in articles please use BRENDA:EC3.2.2.27Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.2.2.27 uracil-DNA glycosylaseIUBMB Comments
Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. EC 3.2.2.27 and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA.
Specify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Mycolicibacterium smegmatis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Hydrolyses single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil
Synonyms
uracil-dna glycosylase, smug1, dna n-glycosylase, ung-1, ul114, uracil dna-glycosylase, uracil-dna n-glycosylase, uracil dna glycosylase 2, thd1p, mjudg, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
uracil-DNA deoxyribohydrolase (uracil-releasing)
Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms. EC 3.2.2.27 and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolysing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalysing the removal of mis-incorporated uracil from DNA.
CAS REGISTRY NUMBER
COMMENTARY
59088-21-0
cf. EC 3.2.2.28
SUBSTRATE
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
additional information
?
-
-
UDG initiates uracil excision repair to safeguard the genomic integrity, mechanism, overview
-
-
?
additional information
?
-
-
Mycobacterium smegmatis UDG excises uracil from different loop positions of tetraloop hairpin substrates with comparable efficiencies, substrate Escherichia coli RZ1032 dut1 ung1 genomic DNA
-
-
?
additional information
?
-
-
UdgB removes aberrant bases uracil, from deaminated cytosine, and hypoxanthine, from deaminated adenine, and 5-fluorouracil from DNA with high efficiency
-
-
?
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
additional information
?
-
-
UDG initiates uracil excision repair to safeguard the genomic integrity, mechanism, overview
-
-
?
additional information
?
-
-
UdgB removes aberrant bases uracil, from deaminated cytosine, and hypoxanthine, from deaminated adenine, and 5-fluorouracil from DNA with high efficiency
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
UGD inhibition protein from Bacillus subtilis
-
phage PBS-2-encoded uracil DNA glycosylase inhibitor, UDG forms a dissociable, activity-reduced complex with the inhibitor protein Ugi in 1:1 molar stoichiometry
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
association of Ung with the replication fork
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
thymidylate synthase inhibition leads to UDG-dependent cell death
physiological function
-
UdgB from Mycobacterium smegmatis protects this organism against mutagenesis associated with deamination of both cytosine and adenine. Together with Ung-type uracil glycosylase, UdgB also helps attenuate the cytotoxicity of the antimicrobial agent 5-fluorouracil
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the initiating amino acid, formyl-methionine is cleaved from the mature UDG protein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
generation of udgB and ung knockout mutants by allelic replacement techniques. The general mutation frequency is increased in UDG knockout strains, frequencies of A:T to G:C mutations, which may arise through adenine deamination, in the udgB knockout mutant and in the double-knockout mutant are 10fold and 31fold higher that those in the wild-type strain, respectively, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 3111fold by anion exchange chromatography, gel filtration, another step of a different anion exchange chromatography, and DNA affinity and hydroxyapatatite chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
the UDG from Mycobacterium smegmatis might be a useful target for inhibitor design
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Purnapatre, K.; Varshney, U.
Uracil DNA glycosylase from Mycobacterium smegmatis and its distinct biochemical properties
Eur. J. Biochem.
256
580-588
1998
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis SN2
Wanner, R.M.; Castor, D.; Guethlein, C.; Boettger, E.C.; Springer, B.; Jiricny, J.
The uracil DNA glycosylase UdgB of Mycobacterium smegmatis protects the organism from the mutagenic effects of cytosine and adenine deamination
J. Bacteriol.
191
6312-6319
2009
Mycolicibacterium smegmatis
EXTERNAL LINKS (specific for EC-Number 3.2.2.27)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
