Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.2.2.27 - uracil-DNA glycosylase and Organism(s) Sulfurisphaera tokodaii and UniProt Accession Q96YD0

for references in articles please use BRENDA:EC3.2.2.27
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Sulfurisphaera tokodaii
UNIPROT: Q96YD0
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Sulfurisphaera tokodaii
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
family 4 uracil-DNA glycosylase
-
STK_22380
locus name
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
uracil-containing DNA + H2O
uracil + DNA with abasic site
show the reaction diagram
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free enzyme and in complex with uracil
sitting-drop vapour diffusion method, deletion mutant enzyme and deletion mutant enzyme complexed with uracil are crystallized and analyzed by X-ray crystallography. The crystals are found to belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 52.2, b = 52.3, c = 74.7 A and a = 52.1, b = 52.2, c = 74.1 A for the apoenzyme and the enzyme complexed with uracil, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L169A
the mutant retains most of the wild type activity
N171A
the mutant retains most of the wild type activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expression in Escherichia coli BL21
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kawai, A.; Higuchi, S.; Tsunoda, M.; Nakamura, K.T.; Miyamoto, S.
Purification, crystallization and preliminary X-ray analysis of uracil-DNA glycosylase from Sulfolobus tokodaii strain 7
Acta Crystallogr. Sect. F
68
1102-1105
2012
Sulfurisphaera tokodaii (Q96YD0), Sulfurisphaera tokodaii 7 (Q96YD0)
Manually annotated by BRENDA team
Kawai, A.; Higuchi, S.; Tsunoda, M.; Nakamura, K.T.; Yamagata, Y.; Miyamoto, S.
Crystal structure of family 4 uracil-DNA glycosylase from Sulfolobus tokodaii and a function of tyrosine 170 in DNA binding
FEBS Lett.
589
2675-2682
2015
Sulfurisphaera tokodaii (Q96YD0), Sulfurisphaera tokodaii
Manually annotated by BRENDA team