A0A4D6XY52 · A0A4D6XY52_9GAMM
- ProteinDNA ligase
- GeneligA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids677 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic activity
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 32-36 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DAEYD | ||||||
Binding site | 81-82 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SL | ||||||
Binding site | 113 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 115 | N6-AMP-lysine intermediate | ||||
Sequence: K | ||||||
Binding site | 136 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 173 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 291 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 315 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 409 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 412 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 433 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | DNA binding | |
Molecular Function | DNA ligase (NAD+) activity | |
Molecular Function | metal ion binding | |
Biological Process | DNA repair | |
Biological Process | DNA replication |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Erwiniaceae > Buchnera
Accessions
- Primary accessionA0A4D6XY52
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 596-677 | BRCT | ||||
Sequence: IKKTYFFHKKIVLTGVFKSFSRMELKRILINLGAKILNNISQKTDCLIYGKNFGSKFFKAKNLNIRMINEEELESLILIEKN |
Sequence similarities
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length677
- Mass (Da)77,886
- Last updated2019-07-31 v1
- ChecksumA35EDF559ED07D7F