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Information on EC 3.2.2.27 - uracil-DNA glycosylase and Organism(s) Rattus norvegicus and UniProt Accession Q811Q1

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.2 Hydrolysing N-glycosyl compounds
                3.2.2.27 uracil-DNA glycosylase
IUBMB 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.
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This record set is specific for:
Rattus norvegicus
UNIPROT: Q811Q1
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-formyluracil-DNA glycosylase
-
uracil-DNA glycosylase
-
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 hide
59088-21-0
cf. EC 3.2.2.28
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
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
5-hydroxymethyluracil-mismatched single-stranded DNA + H2O
5-hydroxymethyluracil + single-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
5-hydroxyuracil-mismatched single-stranded DNA + H2O
5-hydroxyuracil + single-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
uracil-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SMUG1_RAT
278
0
30562
Swiss-Prot
other Location (Reliability: 2)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GST-tagged SMUG1 from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, the tag is cleaved off by thrombin
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
SMUG1 from kidney, expression of GST-tagged SMUG1 in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Masaoka,A.; Matsubara, M.; Hasegawa, R.; Tanaka,T.; Kurisu,S.; Terato,H.; Ohyama,Y.; Karino, N.; Matsuda,A
Ide, H.: Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions
Biochemistry
42
5003-5012
2003
Homo sapiens (Q53HV7), Homo sapiens, Rattus norvegicus (Q811Q1)
Manually annotated by BRENDA team