Identification
Name:DNA ligase
Synonyms:
  • Polydeoxyribonucleotide synthase [NAD+]
Gene Name:ligA
Enzyme Class:
Biological Properties
General Function:Involved in DNA ligase (NAD+) activity
Specific 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
Cellular Location:Cytoplasmic
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb1.0Thumb+2.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0DNA1.0Thumb+1.0Thumb
EcoCyc Reactions:
1.0Thumb+1.0Thumb1.0Thumb+2.0Thumb+1.0Thumb+1.0Thumb
1.0DNAn+1.0(deoxynucleotides)(m)+1.0Thumb1.0(deoxynucleotides)(m)+1.0Thumb+1.0Thumb
1.0DNAn + 1.0(deoxynucleotides)(m) + 1.0NAD → 1.0(deoxynucleotides)(m) + 1.0Nicotinamide ribotide + 1.0Adenosine monophosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0(deoxyribonucleotide)(n)+1.0(deoxyribonucleotide)(m)1.0Thumb+1.0Thumb+1.0(deoxyribonucleotide)(n+m)
1.0NAD + 1.0(deoxyribonucleotide)(n) + 1.0(deoxyribonucleotide)(m) → 1.0Adenosine monophosphate + 1.0NMN + 1.0(deoxyribonucleotide)(n+m)
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00902NADMetaboCard
ECMDB00229Nicotinamide ribotideMetaboCard
ECMDB23222NMNMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
intracellular
Function
binding
catalytic activity
DNA binding
DNA ligase (NAD+) activity
DNA ligase activity
ligase activity
ligase activity, forming phosphoric ester bonds
nucleic acid binding
Process
cellular macromolecule metabolic process
DNA metabolic process
DNA repair
DNA replication
macromolecule metabolic process
metabolic process
Gene Properties
Blattner:b2411
Gene OrientationCounterclockwise
Centisome Percentage:54.45
Left Sequence End2526183
Right Sequence End2528198
Gene Sequence:
>2016 bp
ATGGAATCAATCGAACAACAACTGACAGAACTGCGAACGACGCTTCGCCATCATGAATAT
CTTTATCATGTGATGGATGCGCCGGAAATTCCCGACGCTGAATACGACAGGCTGATGCGC
GAACTGCGCGAGCTGGAAACCAAACATCCAGAACTGATTACGCCTGATTCGCCTACTCAA
CGTGTAGGCGCTGCGCCGCTGGCGGCTTTCAGCCAGATACGCCATGAAGTACCAATGCTG
TCACTGGATAACGTTTTTGATGAAGAAAGCTTTCTTGCTTTCAACAAACGTGTGCAGGAC
CGTCTGAAAAACAACGAGAAAGTCACCTGGTGCTGTGAGCTGAAGCTGGATGGTCTTGCC
GTCAGTATTCTGTATGAAAATGGCGTTTTAGTCAGTGCCGCGACCCGTGGCGATGGCACC
ACCGGGGAAGATATCACGTCTAATGTGCGTACTATTCGCGCCATTCCGCTGAAGCTGCAC
GGAGAGAATATCCCGGCGCGTCTGGAAGTGCGTGGTGAAGTGTTCCTGCCGCAGGCGGGG
TTCGAAAAGATTAACGAAGATGCGCGACGCACGGGCGGGAAAGTGTTTGCTAACCCACGT
AATGCGGCAGCTGGTTCACTGCGTCAGCTTGATCCGCGTATTACAGCGAAGCGACCGCTC
ACTTTTTTCTGCTATGGCGTTGGTGTTCTGGAAGGTGGCGAGCTGCCGGATACTCATCTT
GGCCGTTTACTGCAATTTAAAAAGTGGGGGTTGCCGGTCAGCGATCGGGTAACGCTTTGT
GAATCGGCGGAAGAAGTGCTGGCGTTCTATCACAAAGTGGAAGAAGACCGCCCGACGCTG
GGCTTTGATATCGACGGCGTGGTGATTAAGGTCAACTCACTGGCACAGCAGGAGCAGCTT
GGCTTTGTCGCGCGTGCCCCGCGCTGGGCGGTAGCGTTTAAATTCCCGGCGCAGGAGCAG
ATGACCTTTGTGCGTGACGTCGAGTTTCAGGTTGGGCGTACTGGCGCGATTACGCCTGTT
GCGCGTCTGGAACCTGTCCATGTTGCAGGCGTGCTGGTGAGTAACGCAACCTTACACAAT
GCGGATGAAATCGAACGTCTTGGTTTACGCATTGGCGATAAAGTGGTGATTCGCCGCGCT
GGCGACGTGATCCCGCAGGTGGTTAACGTCGTGCTTTCTGAACGCCCGGAAGATACCCGT
GAGGTTGTATTCCCGACGCATTGTCCGGTATGTGGTTCTGACGTTGAGCGTGTGGAAGGT
GAAGCGGTTGCCCGCTGTACCGGTGGCCTGATTTGCGGTGCGCAGCGTAAAGAGTCGCTG
AAACACTTTGTTTCCCGCCGTGCGATGGATGTTGACGGAATGGGCGACAAAATCATCGAT
CAGCTGGTTGAAAAAGAATATGTCCATACTCCGGCAGATCTGTTCAAACTCACCGCAGGC
AAACTGACCGGACTGGAGCGTATGGGGCCAAAATCGGCACAAAACGTGGTTAACGCGCTG
GAAAAAGCGAAAGAAACCACCTTTGCTCGCTTCCTCTATGCACTTGGCATCCGTGAAGTC
GGCGAGGCCACCGCAGCAGGTCTGGCGGCATATTTCGGCACGCTGGAAGCGCTGGAAGCC
GCTTCGATTGAAGAGCTGCAAAAGGTGCCTGATGTTGGCATTGTCGTTGCATCCCACGTT
CACAACTTCTTTGCCGAAGAAAGCAACCGCAATGTCATCAGCGAGCTGTTGGCGGAAGGT
GTTCACTGGCCTGCGCCGATCGTTATCAACGCGGAAGAGATTGACAGCCCGTTTGCTGGT
AAAACCGTGGTGCTTACGGGCAGCTTAAGCCAGATGTCGCGTGATGACGCTAAAGCTCGA
CTGGTCGAACTGGGCGCGAAAGTCGCGGGCAGCGTGTCGAAGAAAACCGATCTGGTGATA
GCGGGTGAAGCTGCAGGATCTAAACTGGCGAAGGCGCAGGAACTGGGCATTGAAGTCATC
GACGAAGCGGAAATGCTGCGTTTGCTGGGTAGCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:671
Protein Molecular Weight:73605
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>DNA ligase
MESIEQQLTELRTTLRHHEYLYHVMDAPEIPDAEYDRLMRELRELETKHPELITPDSPTQ
RVGAAPLAAFSQIRHEVPMLSLDNVFDEESFLAFNKRVQDRLKNNEKVTWCCELKLDGLA
VSILYENGVLVSAATRGDGTTGEDITSNVRTIRAIPLKLHGENIPARLEVRGEVFLPQAG
FEKINEDARRTGGKVFANPRNAAAGSLRQLDPRITAKRPLTFFCYGVGVLEGGELPDTHL
GRLLQFKKWGLPVSDRVTLCESAEEVLAFYHKVEEDRPTLGFDIDGVVIKVNSLAQQEQL
GFVARAPRWAVAFKFPAQEQMTFVRDVEFQVGRTGAITPVARLEPVHVAGVLVSNATLHN
ADEIERLGLRIGDKVVIRRAGDVIPQVVNVVLSERPEDTREVVFPTHCPVCGSDVERVEG
EAVARCTGGLICGAQRKESLKHFVSRRAMDVDGMGDKIIDQLVEKEYVHTPADLFKLTAG
KLTGLERMGPKSAQNVVNALEKAKETTFARFLYALGIREVGEATAAGLAAYFGTLEALEA
ASIEELQKVPDVGIVVASHVHNFFAEESNRNVISELLAEGVHWPAPIVINAEEIDSPFAG
KTVVLTGSLSQMSRDDAKARLVELGAKVAGSVSKKTDLVIAGEAAGSKLAKAQELGIEVI
DEAEMLRLLGS
References
External Links:
ResourceLink
Uniprot ID:P15042
Uniprot Name:DNLJ_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675396
Ecogene ID:EG10534
Ecocyc:EG10534
ColiBase:b2411
Kegg Gene:b2411
EchoBASE ID:EB0529
CCDB:DNLJ_ECOLI
BacMap:16130337
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hale, C. A., de Boer, P. A. (1997). "Direct binding of FtsZ to ZipA, an essential component of the septal ring structure that mediates cell division in E. coli." Cell 88:175-185. Pubmed: 9008158
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Ishino, Y., Shinagawa, H., Makino, K., Tsunasawa, S., Sakiyama, F., Nakata, A. (1986). "Nucleotide sequence of the lig gene and primary structure of DNA ligase of Escherichia coli." Mol Gen Genet 204:1-7. Pubmed: 3018436
  • Nandakumar, J., Nair, P. A., Shuman, S. (2007). "Last stop on the road to repair: structure of E. coli DNA ligase bound to nicked DNA-adenylate." Mol Cell 26:257-271. Pubmed: 17466627
  • Sriskanda, V., Shuman, S. (2002). "Conserved residues in domain Ia are required for the reaction of Escherichia coli DNA ligase with NAD+." J Biol Chem 277:9695-9700. Pubmed: 11781321
  • Wang, L. K., Nair, P. A., Shuman, S. (2008). "Structure-guided mutational analysis of the OB, HhH, and BRCT domains of Escherichia coli DNA ligase." J Biol Chem 283:23343-23352. Pubmed: 18515356
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837
  • Zhu, H., Shuman, S. (2005). "Structure-guided mutational analysis of the nucleotidyltransferase domain of Escherichia coli NAD+-dependent DNA ligase (LigA)." J Biol Chem 280:12137-12144. Pubmed: 15671015