CATH Domain 4ucvA03

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.30	2-Layer Sandwich
	3.30.470	D-amino Acid Aminotransferase; Chain A, domain 1
	3.30.470.30	DNA ligase/mRNA capping enzyme

Domain Context

CATH Clusters

Superfamily	DNA ligase/mRNA capping enzyme
Functional Family

Enzyme Information

6.5.1.2

DNA ligase (NAD(+)).

based on mapping to UniProt P43813

NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + beta- nicotinamide D-nucleotide.

-!- The enzyme, typically found in bacteria, 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 NAD(+), 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 6.5.1.1, EC 6.5.1.6 and EC 6.5.1.7.

UniProtKB Entries (1)

P43813

DNLJ_HAEIN

Haemophilus influenzae Rd KW20

DNA ligase

PDB Structure

PDB	4UCV
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	From Fragments to Leads: Novel Bacterial Nad+-Dependent DNA Ligase Inhibitors Hale, M., Brassington, C., Carcanague, D., Embrey, K., Eyermann, C.J., Giacobbe, R.A., Gingipali, L., Gowravaram, M., Harang, J., Howard, T., Ioannidis, G., Jahic, H., Kutschke, A., Laganas, V.A., Loch, J., Miller, M.D., Murphy-Benenato, K.E., Oguto, H., Otterbein, L., Patel, S.J., Shapiro, A.B., Boriack-Sjodin, P.A. Tetrahedron Lett.