AC   MF_00407;
DC   Protein; auto
TR   HAMAP; MF_00407; -; 1; level=0
XX
Names: DNA_ligase
XX
ID   DNLI
case <OC:Archaea> and not <OC:Thermococcus>
DE   RecName: Full=DNA ligase;
DE            EC=6.5.1.1;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP];
else case <OC:Thermococcus>
DE   RecName: Full=DNA ligase;
DE            EC=6.5.1.6;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP/NAD(+)];
else case <OC:Bacteria>
DE   RecName: Full=Probable DNA ligase;
DE            EC=6.5.1.1;
DE   AltName: Full=Polydeoxyribonucleotide synthase [ATP];
end case
GN   Name=lig;
XX
CC   -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA
CC       replication, DNA recombination and DNA repair.
case <OC:Archaea> and not <OC:Thermococcus>
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1;
else case <OC:Thermococcus>
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.6;
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=6.5.1.6;
else case <OC:Bacteria>
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1;
end case
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
XX
DR   Pfam; PF04679; DNA_ligase_A_C; 1; trigger=no
DR   Pfam; PF01068; DNA_ligase_A_M; 1; trigger=no
DR   Pfam; PF04675; DNA_ligase_A_N; 1; trigger=no
DR   NCBIfam; TIGR00574; Dnl1; 1; trigger=no
DR   PROSITE; PS00697; DNA_LIGASE_A1; 1; trigger=no
DR   PROSITE; PS00333; DNA_LIGASE_A2; 1; trigger=no
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1; trigger=no
XX
KW   DNA damage
KW   DNA repair
KW   DNA replication
KW   DNA recombination
KW   Cell cycle
KW   Cell division
KW   Ligase
KW   ATP-binding
KW   Magnesium
KW   Metal-binding
case <OC:Thermococcus>
KW   NAD
end case
KW   Nucleotide-binding
XX
GO   GO:0005524; F:ATP binding
GO   GO:0003910; F:DNA ligase (ATP) activity
GO   GO:0006310; P:DNA recombination
GO   GO:0006281; P:DNA repair
GO   GO:0006260; P:DNA replication
XX
FT   From: DNLI_PYRFU (P56709)
FT   ACT_SITE        249
FT                   /note="N6-AMP-lysine intermediate"
FT   Condition: K
FT   BINDING         247
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: [DE]
FT   BINDING         254
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
FT   BINDING         269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
FT   BINDING         299
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: E
FT   BINDING         339
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: F
FT   BINDING         414
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R
FT   BINDING         420
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: K
XX
Size: 503-618;
Related: None;
Template: P56709; Q9HHC4; Q980T8; Q9P9K9; A2BJX6;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: <Unknown>
 Cter: None
Duplicate: None
Plasmid: None
Comments: Shorter N-terminus in the first copy of lig in METBF.
 Some archaea use additional nucleotide cofactors (such as NAD(+), ADP or GTP) next to ATP.
XX
# Revision 1.33 2023/06/01
//