Family

Formamidopyrimidine-DNA glycosylase (IPR020629)

Short name: Formamido-pyr_DNA_Glyclase

Family relationships

None.

Description

Formamidopyrimidine-DNA glycosylase (Fpg, MutM) is a trifunctional DNA base excision repair enzyme that removes a wide range of oxidation-damaged bases (N-glycosylase activity; EC:3.2.2.23) and cleaves both the 3'- and 5'-phosphodiester bonds of the resulting apurinic/apyrimidinic site (AP lyase activity; EC:4.2.99.18). Fpg has a preference for oxidised purines, excising oxidized purine bases such as 7,8-dihydro-8-oxoguanine (8-oxoG). ITs AP (apurinic/apyrimidinic) lyase activity introduces nicks in the DNA strand, cleaving 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. Fpg is a monomer composed of 2 domains connected by a flexible hinge [PMID: 10921868]. The two DNA-binding motifs (a zinc finger and the helix-two-turns-helix motifs) suggest that the oxidized base is flipped out from double-stranded DNA in the binding mode and excised by a catalytic mechanism similar to that of bifunctional base excision repair enzymes [PMID: 10921868]. Fpg binds one ion of zinc at the C terminus, which contains four conserved and essential cysteines [PMID: 8473347, PMID: 7704272].

GO terms

Biological Process

GO:0006281 DNA repair

Molecular Function

GO:0003906 DNA-(apurinic or apyrimidinic site) lyase activity
GO:0008534 oxidized purine nucleobase lesion DNA N-glycosylase activity
GO:0008270 zinc ion binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
HAMAP
TIGRFAMs