CATH Classification

Domain Context

CATH Clusters

Superfamily 3.30.70.3300
Functional Family

Enzyme Information

6.5.1.1
DNA ligase (ATP).
based on mapping to UniProt P9WNV3
ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate.
-!- The enzyme catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA. -!- Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue. -!- The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA). -!- Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate. -!- RNA can also act as substrate, to some extent. -!- Cf. EC 6.5.1.2, EC 6.5.1.6 and EC 6.5.1.7.

UniProtKB Entries (1)

P9WNV3
LIGD_MYCTU
Mycobacterium tuberculosis H37Rv
Multifunctional non-homologous end joining DNA repair protein LigD

PDB Structure

PDB 2IRY
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Structure and function of a mycobacterial NHEJ DNA repair polymerase.
Pitcher, R.S., Brissett, N.C., Picher, A.J., Andrade, P., Juarez, R., Thompson, D., Fox, G.C., Blanco, L., Doherty, A.J.
J.Mol.Biol.
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