G6EZT0 · G6EZT0_9PROT
- ProteinDNA ligase
- GeneligA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids704 (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 | 49-53 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DATYD | ||||||
Binding site | 98-99 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: SL | ||||||
Binding site | 134 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 136 | N6-AMP-lysine intermediate | ||||
Sequence: K | ||||||
Binding site | 157 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 193 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 309 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 333 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 428 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 431 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 452 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
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
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Rhodospirillales > Acetobacteraceae
Accessions
- Primary accessionG6EZT0
Proteomes
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 620-692 | BRCT | ||||
Sequence: TQEGILVGKILVFTGTLSTMTRSEAKDIAERLGAKVTSSVSAKTDYVIEGVDGGSKARKAKELNIKCLDEKEW |
Sequence similarities
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length704
- Mass (Da)78,730
- Last updated2012-01-25 v1
- ChecksumAFB77A2085229932
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AGFR01000003 EMBL· GenBank· DDBJ | EHD14153.1 EMBL· GenBank· DDBJ | Genomic DNA |