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A0A0D6KJW9 · A0A0D6KJW9_9CYAN

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.

Type
IDPosition(s)Description
Binding site35-39NAD+ (UniProtKB | ChEBI)
Binding site84-85NAD+ (UniProtKB | ChEBI)
Binding site116NAD+ (UniProtKB | ChEBI)
Active site118N6-AMP-lysine intermediate
Binding site139NAD+ (UniProtKB | ChEBI)
Binding site178NAD+ (UniProtKB | ChEBI)
Binding site297NAD+ (UniProtKB | ChEBI)
Binding site321NAD+ (UniProtKB | ChEBI)
Binding site415Zn2+ (UniProtKB | ChEBI)
Binding site418Zn2+ (UniProtKB | ChEBI)
Binding site433Zn2+ (UniProtKB | ChEBI)
Binding site438Zn2+ (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
      FDUTEX481_09612

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • PCC 7601 / UTEX B 481
  • Taxonomic lineage
    Bacteria > Cyanobacteriota > Cyanophyceae > Nostocales > Tolypothrichaceae > Tolypothrix

Accessions

  • Primary accession
    A0A0D6KJW9

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain600-678BRCT

Sequence similarities

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    678
  • Mass (Da)
    75,699
  • Last updated
    2015-05-27 v1
  • MD5 Checksum
    304DD24C8D916C0F55AAD575A50F8E3C
MIQSQPETKRVEELRRLLQQASYAYYVLDAPIMEDAVYDQLYRELQQLEIQYPELITPDSPTQRVGERPATQFTSVRHNIPLYSLENAFNIDELQSWDQRWRRQAPKIAAAEYVSELKIDGSAIALTYQNGILTRGATRGDGVMGEDITQNVRTIRSIPLRLNFEGLEILEKVEVRGEAFLPLDVFKQINEERQKAGEQLFANPRNAAAGTLRQLDSKIVARRRLDFFAYTLHIPGRDDASIANTQWEALELLQKMGFRVNPNHKLCPSLAEVAEYYNYWDTERLNLPYMTDGVVVKLNSFKLQEQLGFTQKFPRWAVALKYAAEEAPTRVENIAVNVGRTGALTPLAEMRPVQLAGTTVSRATLHNSDRIAQLDIRIGDTVIVRKAGEIIPEVVRVLTELRPPNTQPFIMPSNCPVCGQPVVRELGEAVTRCVNASCAAILKGAIEHWVSRDALDIKGMGEKLVHQLVDKGLVHSVADLYDLTEEKLYVLERMGQKSAQKLIDAIAQSKNQPWSRVLYGLGIRHVGSVNAQLLTEKFSDVEKITQARQSDIAGIYGIGVEIAESVHQWFQIHANQTLISRLQAAGLQLANSAETSTITDSNPQFTDKTFVVTGTLPTLKRDEAKALIQKAGGKVTDSVSKKTDYLVVGEDAGSKLAKAEALGITQLTEAQLLQMLES

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AGCR01000067
EMBL· GenBank· DDBJ
EKE99735.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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