CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.920 | DNA primase, PRIM domain |
|
3.90.920.10 | DNA primase, PRIM domain |
Domain Context
CATH Clusters
| Superfamily | DNA primase, PRIM domain |
| Functional Family | Multifunctional non-homologous end joining protein LigD |
Enzyme Information
| 6.5.1.1 |
DNA ligase (ATP).
based on mapping to UniProt Q9I1X7
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)
| Q9I1X7 |
LIGD_PSEAE
Pseudomonas aeruginosa PAO1
Multifunctional non-homologous end joining protein LigD
|
PDB Structure
| PDB | 2FAR |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Atomic structure and nonhomologous end-joining function of the polymerase component of bacterial DNA ligase D
Proc.Natl.Acad.Sci.USA
|
