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Information on EC 3.2.2.27 - uracil-DNA glycosylase and Organism(s) Chlamydia pneumoniae and UniProt Accession Q9Z7D3

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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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Chlamydia pneumoniae
UNIPROT: Q9Z7D3
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Word Map
The taxonomic range for the selected organisms is: Chlamydia pneumoniae
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
additional information
the enzyme is a member of the UDG family I
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-mismatched double-stranded DNA + H2O
uracil + double-stranded DNA with abasic site
show the reaction diagram
duplex DNA with A/U mismatch, substrate specificity, the base opposite to uracil in double strand DNAs affects uracil removal efficiencies in descending order U/-, U/T, U/C, U/G, U/A. Free uracil and abasic sites inhibit the reaction. Amino acids D77, H200, and A205 are important for the catalytic activity of UDG
-
-
?
uracil-mismatched double-stranded DNA with A-U mismatch + H2O
uracil + double-stranded DNA with abasic site
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0052 - 0.256
uracil-mismatched double-stranded DNA
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.042 - 0.73
uracil-mismatched double-stranded DNA
-
5.9
uracil-mismatched double-stranded DNA with A-U mismatch +
pH 8.0, 37°C, recombinant wild-type enzyme
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
UNG_CHLPN
236
0
27006
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A205S
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D77N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H200Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant UDGs from Escherichia coli strain BL21 (DE3) by nickel affinity and anion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutant UDGs in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liu, X.; Liu, J.
Cloning, expression, and characterization of uracil-DNA glycosylase of Chlamydia pneumoniae in Escherichia coli
Protein Expr. Purif.
35
46-53
2004
Chlamydia pneumoniae (Q9Z7D3), Chlamydia pneumoniae, Chlamydia pneumoniae AR39 (Q9Z7D3), Chlamydia pneumoniae AR39
Manually annotated by BRENDA team