A0A2B7M3I3 · A0A2B7M3I3_9ESCH

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.

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.

167150100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site32-36NAD+ (UniProtKB | ChEBI)
Binding site81-82NAD+ (UniProtKB | ChEBI)
Binding site113NAD+ (UniProtKB | ChEBI)
Active site115N6-AMP-lysine intermediate
Binding site136NAD+ (UniProtKB | ChEBI)
Binding site173NAD+ (UniProtKB | ChEBI)
Binding site290NAD+ (UniProtKB | ChEBI)
Binding site314NAD+ (UniProtKB | ChEBI)
Binding site408Zn2+ (UniProtKB | ChEBI)
Binding site411Zn2+ (UniProtKB | ChEBI)
Binding site432Zn2+ (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
    • ORF names
      C4A13_02786
      , HV018_15240
      , HV245_02845
      , HV276_16245
      , HV284_22235
      , NVV43_19670

Organism names

  • Taxonomic identifier
  • Organism
  • Strains
    • SC344
    • RHB42-C09
    • RHBSTW-00604
    • RHBSTW-00777
    • RHBSTW-00814
    • S1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    A0A2B7M3I3
  • Secondary accessions
    • A0A370V6T6

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain593-671BRCT

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    671
  • Mass (Da)
    73,590
  • Last updated
    2017-12-20 v1
  • Checksum
    8BF36A30E5CBC24F
MESIEQQLTELRTVLRHHEYLYHVMDAPEIPDAEYDRLMRELRELEAKHPELITPDSPTQRVGAAPLAAFSQIRHEVPMLSLDNVFDEESFLAFNKRVQDRLKSNEKVTWCCELKLDGLAVSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLHGENIPARLEVRGEVFLPQAGFEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGVLEGGELPDTHLGRLLQFKKWGLPVSDRVTLCESAEEVLAFYHKVEEDRPTLGFDIDGVVIKVNSLAQQEQLGFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHNADEIERLGLRIGDKVVIRRAGDVIPQVVNVVLSERPEDTREVVFPTHCPVCGSDVERVEGEAVARCTGGLICAAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFKLTAGKLTGLERMGPKSAQNVVNALEKAKETTFARFLYALGIREVGEATASGLAAYFGTLEALEAASIEELQKVPDVGIVVASHVHNFFAEESNRNVISELLAEGVHWPAPVVINAEEIDSPFAGKTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVIDEAEMLRLLGN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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