A0A7Y5XZ94 · A0A7Y5XZ94_9BURK

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

Lacks conserved residue(s) required for the propagation of feature annotation.
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 site46-50NAD+ (UniProtKB | ChEBI)
Binding site95-96NAD+ (UniProtKB | ChEBI)
Binding site127NAD+ (UniProtKB | ChEBI)
Active site129N6-AMP-lysine intermediate
Binding site150NAD+ (UniProtKB | ChEBI)
Binding site187NAD+ (UniProtKB | ChEBI)
Binding site304NAD+ (UniProtKB | ChEBI)
Binding site328NAD+ (UniProtKB | ChEBI)
Binding site422Zn2+ (UniProtKB | ChEBI)
Binding site425Zn2+ (UniProtKB | ChEBI)
Binding site447Zn2+ (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
      HNO82_01480

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • C9C3
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Oxalobacteraceae > Herbaspirillum

Accessions

  • Primary accession
    A0A7Y5XZ94

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain606-678BRCT

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    690
  • Mass (Da)
    75,243
  • Last updated
    2021-06-02 v1
  • Checksum
    319DB0554F91BADD
MQDDLFSAGRPPQGEPDWRARARTLRDELNRHNHSYYVLDQPSIPDAEYDRLFQQLQALETAHPELLTPDSPTQRVGAGPLPQFEPVRHDIPMLSLGNGFADEDIEAFDKRVRDGLETLQEVRYATELKFDGLAISLRYENGVLVQAATRGDGTTGENVTANIRTVRAIPLRLHGDNLPQVIDVRGEVLMYKEDFARLNQRQRDAGQKEFANPRNAAAGSLRQLDSRITAQRTLRFFAYGIGVLEGAEMPPSHSALLDWYQELGLPVCKERAVVSGAAGLLDFFRSIGAKRESLPYEIDGVVYKVDRLDQQKHLGFVSRAPRFALAHKFPAQEALTVVQDIEVQVGRTGAITPVARLNPVFVGGVTVTNATLHNEDEVRRKDIRIGDTVIVRRAGDVIPEVVAFVPEKRPEDARAFVMPVACPVCGSPIVRAEEEAVARCSGGWLKCSAQRKGGLQHFASRRAMDIEGLGEQLVEQLVDRQVVNTPADLYRLGLSALAELDRMAEKSAQNVLDALQKSKTTTLARFIYALGIRHVGEATAKELARHFGGIDKLLAASEEQLLEVADIGPVVASSIRAFFNDPINVELVEQLRAVGVHWPESEGVDAGAKHLAGKTFVLTGTLPNLSRDDASQMIEAAGGKVSGSVSKKTSYVVAGAEAGSKLAKAEELGVAILDEDALKALCAGQDVSGT

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JABFMQ010000001
EMBL· GenBank· DDBJ
NUT59772.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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