A0A350LZP5 · A0A350LZP5_UNCXX

  • Protein
    DNA ligase
  • Gene
    ligA
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Organism
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Type
IDPosition(s)Description
Binding site30-34NAD+ (UniProtKB | ChEBI)
Binding site79-80NAD+ (UniProtKB | ChEBI)
Binding site109NAD+ (UniProtKB | ChEBI)
Active site111N6-AMP-lysine intermediate
Binding site132NAD+ (UniProtKB | ChEBI)
Binding site168NAD+ (UniProtKB | ChEBI)
Binding site283NAD+ (UniProtKB | ChEBI)
Binding site307NAD+ (UniProtKB | ChEBI)
Binding site399Zn2+ (UniProtKB | ChEBI)
Binding site402Zn2+ (UniProtKB | ChEBI)
Binding site422Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytosol
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
      DCX16_03570

Organism names

Accessions

  • Primary accession
    A0A350LZP5

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain579-657BRCT

Sequence similarities

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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    657
  • Mass (Da)
    74,448
  • Last updated
    2018-11-07 v1
  • Checksum
    F7523AD0D6F0F165
MVKDEIENLKELIRYYDYKYYIEGQPEISDYEYDMLVKKLKDLEEKYPEFITGDSPTQRVSGFVQEEFSHVRHKIPMLSLDNAYSFDELDDFIERVRKNLRFIPEFTVELKIDGVGVSLIYEKGIFTRGITRGDGTTGDDITLNLKTISSLPLKLLGTPPEYLEVRGEVYLTKKGFCLINEERIKENLPTFASTRNAAAGSLHLLDPREVTRRPLRIFLHTLAESSFPFQTHHEALKSFLKFGLPVEPNFSLTKTAAEIKEYCKVWENKAKDLDYDTDGVVVKVNSYEYHKRLGWTSKAPRYAVAFKFTPEQATTKLLDIKIQVGRTGCLTPVAILDPVRLSGAIISRATLHNEDEVKKKDIRIGDSVIIERSGDVIPKVIVCIPAKKRNLPFSFPKTCPVCGAPVVRKEEEARNYCTGMNCQAQLKRKIEYFASRPCLDIEGLGEKNVSQLVDCGLLKKIQDIYTLKKEDIVNLPRWDEKSSKNLIDAIKRSKKMPLNRLICALGIPNIGSATSKVLEERFGSLRNLMNASYEELISINEIGEKTAVSIIQFLSQDDVSKLIEDLEVFGVCMEAVKEERPLPYKDIIVVITGTIPGMTRDEIKAKFESLGGVVSDSVSKKISYLVVGEEPGETKLKKAKELNIPIINGEEFIKKFL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
DNCM01000099
EMBL· GenBank· DDBJ
HAW50012.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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