UniProt functional annotation for P05523

UniProt code: P05523.

Organism:		Escherichia coli (strain K12).
Taxonomy:		Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia.
Function:		Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) and its derivatives such as guanidinohydantoin:C and spiroiminodihydantoin:C, however it also acts on thymine glycol:G, 5,6-dihydrouracil:G and 5-hydroxyuracil:G. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Cleaves ssDNA containing an AP site. {ECO:0000269|PubMed:1689309, ECO:0000269|PubMed:20031487}.
Catalytic activity:		Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N- methyl)formamidopyrimidine.; EC=3.2.2.23;
Catalytic activity:		Reaction=(DNA)-(deoxyribonucleoside 5'-phosphate)-(deoxyribose 5'- phosphate)-(deoxyribonucleoside 5'-phosphate) = (DNA)-3'- (deoxyribonucleoside 5'-phosphate)-(2,3-dehydro-2,3-deoxyribose 5'- phosphate) + H(+) + phospho-5'-(DNA); Xref=Rhea:RHEA:66592, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18;
Cofactor:		Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:1689309}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:1689309};
Subunit:		Monomer. {ECO:0000269|PubMed:11912217, ECO:0000269|PubMed:1689309}.
Domain:		The zinc-finger is necessary for DNA binding.
Similarity:		Belongs to the FPG family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.