A0A2B7M3I3 · A0A2B7M3I3_9ESCH
- ProteinDNA ligase
- GeneligA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids671 (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 | 290 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 314 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 408 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 411 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 432 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | DNA binding | |
Molecular Function | DNA ligase (NAD+) activity | |
Molecular Function | metal ion binding | |
Biological Process | base-excision repair, DNA ligation | |
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
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A2B7M3I3
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 593-671 | BRCT | ||||
Sequence: EIDSPFAGKTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVIDEAEMLRLLGN |
Sequence similarities
Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length671
- Mass (Da)73,590
- Last updated2017-12-20 v1
- Checksum8BF36A30E5CBC24F
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JABXPT010000001 EMBL· GenBank· DDBJ | MBA7897137.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
JANPXH010000028 EMBL· GenBank· DDBJ | MCR6677806.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP058207 EMBL· GenBank· DDBJ | QLP27925.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP056159 EMBL· GenBank· DDBJ | QLV03579.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP056165 EMBL· GenBank· DDBJ | QLX31159.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
QONO01000096 EMBL· GenBank· DDBJ | RDR26558.1 EMBL· GenBank· DDBJ | Genomic DNA |