C1A6H2 · DNLJ_GEMAT

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

  • NAD+ + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
    EC:6.5.1.2 (UniProtKB | ENZYME | Rhea)

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Mn2+ (UniProtKB | Rhea| CHEBI:29035 )

Features

Showing features for binding site, active site.

168950100150200250300350400450500550600650
Type
IDPosition(s)Description
Binding site40-44NAD+ (UniProtKB | ChEBI)
Binding site89-90NAD+ (UniProtKB | ChEBI)
Binding site122NAD+ (UniProtKB | ChEBI)
Active site124N6-AMP-lysine intermediate
Binding site145NAD+ (UniProtKB | ChEBI)
Binding site182NAD+ (UniProtKB | ChEBI)
Binding site300NAD+ (UniProtKB | ChEBI)
Binding site325NAD+ (UniProtKB | ChEBI)
Binding site419Zn2+ (UniProtKB | ChEBI)
Binding site422Zn2+ (UniProtKB | ChEBI)
Binding site437Zn2+ (UniProtKB | ChEBI)
Binding site442Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
Molecular FunctionDNA binding
Molecular FunctionDNA ligase (NAD+) activity
Molecular Functionmetal ion binding
Biological Processbase-excision repair, DNA ligation
Biological ProcessDNA replication

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA ligase
  • EC number
  • Alternative names
    • Polydeoxyribonucleotide synthase [NAD(+)]

Gene names

    • Name
      ligA
    • Ordered locus names
      GAU_0790

Organism names

Accessions

  • Primary accession
    C1A6H2

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003803871-689DNA ligase

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain600-689BRCT

Sequence similarities

Belongs to the NAD-dependent DNA ligase family. LigA subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    689
  • Mass (Da)
    74,174
  • Last updated
    2009-05-26 v1
  • Checksum
    55B6927E11591FA1
MTASSGTPPHQTVERARELREQLGTAQHEYYVLDRPTLSDQEYDRLFRELQGIEAEYPTLCTEDSPTRRVGAPVQSAFSPHRHLVRMLSLDNAFDLSELEDFEQSLKRVVGDAIHTSGYTVELKIDGAAVALTYREGVLVTAATRGDGTDGEDVTANVRTIRGVPLRLHGDNHPPLMEVRGEVYLPFAGFERMNEARVAAGEPVYVNPRNAAAGSMRQLDSANTAARPLRFFGYAAVLPDGSAPARSQWELLEQLSAWGVPVAPHRQRCHTIQEAEAWATVVEHETRATLGFAIDGGVVKVNDMALQDELGIRADRTPRWGVARKFAPDMALTKLRRIDVNVGRTGVLTPFAVLEPVDVGGATVTFASLHNADQIAAKDLREGDTVQVVRAGDVIPYVLGPVPEQRDGSQQPWSMPTQCPRCNTPVERYGDDVAVYCPNVACPGRQLEGLVHFSSKDALDIDGLSYARIQQLLDAGLVHDVADLFDITVDQLTSLERFAKKSAENLVAAIAAAKQQPLSRLMFGLGIRHVGAQAAQLLSRQYGSLDALMNATAEQLGAVRGIGSIIAQSVASYFADPTTRALMERLRARGLRFDEPNAVQADGVLTGATVVLTGTLPSLSRGEATALVEQAGGRVTSSVSKKTTFVVAGEEAGSKLDKAKELGVTVLTEAELLEKLSGASADASADASA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP009153
EMBL· GenBank· DDBJ
BAH37832.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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