Family

DNA ligase, ATP-dependent, bacterial/archaeal (IPR022865)

Short name: DNA_ligae_ATP-dep_bac/arc

Family relationships

Description

DNA ligase (polydeoxyribonucleotide synthase) is the enzyme that joins two DNA fragments by catalysing the formation of an internucleotide ester bond between phosphate and deoxyribose. It is active during DNA replication, DNA repair and DNA recombination. There are two forms of DNA ligase, one requires ATP (EC:6.5.1.1), the other NAD (EC:6.5.1.2), the latter being restricted to eubacteria. Eukaryotic, archaebacterial, viral and some eubacterial DNA ligases are ATP-dependent. The first step in the ligation reaction is the formation of a covalent enzyme-AMP complex. The co-factor ATP is cleaved to pyrophosphate and AMP, with the AMP being covalently joined to a highly conserved lysine residue in the active site of the ligase. The activated AMP residue is then transferred to the 5'phosphate of the nick, before the nick is sealed by phosphodiester-bond formation and AMP elimination [PMID: 1988940,PMID: 1497311].

This entry represents bacterial and archaeal ATP-depdendent DNA ligases.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0003910 DNA ligase (ATP) activity

Cellular Component

No terms assigned in this category.

Contributing signatures

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