| Description | Uracil-DNA glycosylases are DNA repair enzymes that excise uracil residues from DNA by cleaving the N-glycosylic bond, initiating the base excision repair pathway. Uracil in DNA can arise either through the deamination of cytosine to form mutagenic U:G mispairs, or through the incorporation of dUMP by DNA polymerase to form U:A pairs [ ]. These aberrant uracil residues are genotoxic []. The sequence of uracil-DNA glycosylase is extremely well conserved [] in bacteria and eukaryotes as well as in herpes viruses. More distantly related uracil-DNA glycosylases are also found in poxviruses [].Uracil DNA glycosylase family 5 includes Thermus thermophilus HB8 TTUDGB (also called UDGb) which is not only a Uracil-DNA glycosylase (UDG) acting on double-stranded uracil-containing DNA, but also a hypoxanthine DNA glycosylase acting on double-stranded hypoxanthine-containing DNA (except for the C/I base pair), as well as a xanthine DNA glycosylase acting on both, double-stranded and single-stranded xanthine-containing DNA. TTUDGB also excises thymine from G:T mismatched DNA, and removes analogs of uracil from DNA, including 5-hydroxymethyluracil (hmU) and 5-fluorouracil (fU) [ , , ]. This entry also contains Bradyrhizobium diazoefficiens family 5 homologue Blr5068 (UdgB) which has been found to efficiently excise uracil from ssDNA and dsDNA []. Similar to family 4 UDGs, members of family 5 possess four conserved cysteine residues required to coordinate the [4Fe-4S]iron-sulfur cluster [ ]. | Name | Uracil DNA glycosylase family 5 |
| Short Name | UdgB-like | Type | Domain |
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