A0A098MEL3 · A0A098MEL3_9BACL

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.

TypeIDPosition(s)Description
Binding site28-32NAD+ (UniProtKB | ChEBI)
Binding site76-77NAD+ (UniProtKB | ChEBI)
Binding site117NAD+ (UniProtKB | ChEBI)
Active site119N6-AMP-lysine intermediate
Binding site140NAD+ (UniProtKB | ChEBI)
Binding site175NAD+ (UniProtKB | ChEBI)
Binding site287NAD+ (UniProtKB | ChEBI)
Binding site311NAD+ (UniProtKB | ChEBI)
Binding site405Zn2+ (UniProtKB | ChEBI)
Binding site408Zn2+ (UniProtKB | ChEBI)
Binding site421Zn2+ (UniProtKB | ChEBI)
Binding site427Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular FunctionDNA binding
Molecular FunctionDNA ligase (NAD+) activity
Molecular Functionmetal ion binding
Biological ProcessDNA repair
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
    • ORF names
      PWYN_14980

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DSM 18334
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Paenibacillaceae > Paenibacillus

Accessions

  • Primary accession
    A0A098MEL3

Proteomes

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain588-667BRCT

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    667
  • Mass (Da)
    74,067
  • Last updated
    2015-01-07 v1
  • Checksum
    7E3CA1049A2F3DC8
MDQMHTWVAELNKYNYHYYTLDTPLVSDKEYDAIYDKLVALEAETGTVLPDSPTQRVGGELLKGFTPHRHLAPLWSLDKAQNIEQLRSWNVRVHRLVNEYNTRNPENPLPDPCYAVELKYDGLTLNLTYRDGVLVQAATRGNGVTGEGILAQVKTIKSVPLTIPFEDGVIEVQGEGIMNLSVLADYNTRAAEPLKNARNGAAGALRNLNPKTTASRRLNAFFYNIGYADGVEFADHQEMMDFLRNNRFKVNPYLTYYSNFDDVTEQLAEIEESRSGLDYLIDGAVIKITDFRTREALGYTDKFPRWAVAYKFEAEETTTILESVSWNVGRTGKVTPLARVEAVELAGVTVQNCTLNNVGDIERKNLKHALGTRVFIRRSNDVIPEILGKVTEESDGGEIIFPENCPSCGFPLEMRGAHLFCNNKLDCKPQIISRITHFASRDAMDIETFSEKTAGQLHEELNVREPADLYELTFEQLLKLDRFGDKKASNLIQALEDSKGRDLASFLYALGIPNTGKATTKMLAEHFRDLTAVMEASAEELTGLPDIGGIVAESIVSYFKDPFVVTAINRMLALGVEAKAPEAPRPVSTNSFFSGKTVVLTGTLHKLTRDEAAERLEALGAKVSGSVSKKTDLVIAGEKAGSKLAKAQQLGIQVIEDEDELLRLLES

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JQCR01000002
EMBL· GenBank· DDBJ
KGE20501.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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