DNA-3-methyladenine glycosylase AlkA, N-terminal (IPR010316)

Short name: AlkA_N

Overlapping homologous superfamilies

Domain relationships



AlkA (DNA-3-methyladenine glycosylase II) is a base excision repair glycosylase from Escherichia coli. It removes a variety of alkylated bases from DNA, primarily by removing alkylation damage from duplex and single stranded DNA. AlkA is similar in fold and active site location to the bifunctional glycosylase/lyase endonuclease III. This suggests that the two may use similar mechanisms for base excision [PMID: 8706136]. The structural analysis of the AlkA and AlkA-hypoxanthine structures indicate that free hypoxanthine binding in the active site may inhibit glycosylase activity [PMID: 12009927].

The AlkA protein consists of three domains: an N-terminal mixed alpha-beta structure, a central seven-helix bundle, and a C-terminal domain of four a helices [PMID: 8706136]. This entry represents the N-terminal domain.

Contributing signatures

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