AC   MF_01588;
DC   Protein; auto
TR   HAMAP; MF_01588; -; 1; level=0
XX
Names: DNA_ligase_A
XX
ID   DNLJ
DE   RecName: Full=DNA ligase;
DE            EC=6.5.1.2;
DE   AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)];
GN   Name=ligA;
XX
CC   -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester
CC       linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-
CC       stranded DNA using NAD as a coenzyme and as the energy source for the
CC       reaction. It is essential for DNA replication and repair of damaged
CC       DNA.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-
CC         nicotinamide D-nucleotide.; EC=6.5.1.2;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC   -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA
CC       subfamily.
XX
DR   PROSITE; PS50172; BRCT; 1; trigger=yes
DR   PROSITE; PS01055; DNA_LIGASE_N1; 1; trigger=no
DR   PROSITE; PS01056; DNA_LIGASE_N2; 1; trigger=no
DR   Pfam; PF00533; BRCT; 1; trigger=no
DR   Pfam; PF01653; DNA_ligase_aden; 1; trigger=no
DR   Pfam; PF03120; DNA_ligase_OB; 1; trigger=no
DR   Pfam; PF03119; DNA_ligase_ZBD; 1; trigger=no
DR   PIRSF; PIRSF001604; LigA; 1; trigger=no
DR   NCBIfam; TIGR00575; Dnlj; 1; trigger=no
XX
KW   DNA damage
KW   DNA repair
KW   DNA replication
KW   Ligase
KW   Magnesium
KW   Manganese
KW   Metal-binding
KW   NAD
KW   Zinc
XX
GO   GO:0003911; F:DNA ligase (NAD+) activity
GO   GO:0006259; P:DNA metabolic process
XX
FT   From: DNLJ_ENTFA (Q837V6)
FT   BINDING         39..43
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: D-x-x-[YF]-D
FT   BINDING         88..89
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: S-x
FT   ACT_SITE        120
FT                   /note="N6-AMP-lysine intermediate"
FT   Condition: K
FT   BINDING         409
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: C
FT   BINDING         412
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: C
FT   BINDING         427
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: C
FT   BINDING         432
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Condition: C
FT   BINDING         118
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Optional; Condition: [ED]
FT   BINDING         141
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: R
FT   BINDING         175
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: E
FT   BINDING         291
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Optional; Condition: K
FT   BINDING         315
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT   Condition: K
XX
Size: 587-921;
Related: MF_01577!;
Template: O87703; P15042; Q9AIU7; P9WNV1; Q837V6; Q9ZHI0;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: in PSECP, CLOAB, DEIDV, DESVV, NOCFA, OPITP, STRCO, STRGG
Plasmid: in PSECP, DEIDV
Comments: None
XX
# Revision 1.21 2023/06/01
//