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Literature summary for 6.5.1.1 extracted from

  • Zhu, H.; Shuman, S.
    Characterization of Agrobacterium tumefaciens DNA ligases C and D (2007), Nucleic Acids Res., 35, 3631-3645.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.5.1.1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m Agrobacterium tumefaciens Agrobacterium LigD1 is composed of a central ligase domain fused to a C-terminal polymerase-like (POL) domain and an N-terminal 3'-phosphoesterase (PE) module. The LigD1 protein seals DNA nicks, albeit inefficiently. The LigD1 POL domain has no detectable polymerase activity. The PE domain catalyzes metal-dependent phosphodiesterase and phosphomonoesterase reactions at a primer-template with a 3'-terminal diribonucleotide to yield a primertemplate with a monoribonucleotide 3'-OH end. The PE domain also has a 3'-phosphatase activity on an all-DNA primer-template that yields a 3'-OH DNA end AMP + diphosphate + (deoxyribonucleotide)n+m
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 ?
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m Agrobacterium tumefaciens Agrobacterium LigD2 is composed of a central ligase domain fused to a C-terminal polymerase-like (POL) domain and an N-terminal 3'-phosphoesterase (PE) module. The LigD1 protein seals DNA nicks, albeit inefficiently. The LigD2 POL domain adds ribonucleotides or deoxyribonucleotides to a DNA primer-template, with rNTPs being the preferred substrates. The PE domain catalyzes metal-dependent phosphodiesterase and phosphomonoesterase reactions at a primer-template with a 3'-terminal diribonucleotide to yield a primer-template with a monoribonucleotide 3'-OH end. The PE domain also has a 3'-phosphatase activity on an all-DNA primer-template that yields a 3'-OH DNA end AMP + diphosphate + (deoxyribonucleotide)n+m
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 ?

Organism

Organism UniProt Comment Textmining
Agrobacterium tumefaciens
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m Agrobacterium LigD1 is composed of a central ligase domain fused to a C-terminal polymerase-like (POL) domain and an N-terminal 3'-phosphoesterase (PE) module. The LigD1 protein seals DNA nicks, albeit inefficiently. The LigD1 POL domain has no detectable polymerase activity. The PE domain catalyzes metal-dependent phosphodiesterase and phosphomonoesterase reactions at a primer-template with a 3'-terminal diribonucleotide to yield a primertemplate with a monoribonucleotide 3'-OH end. The PE domain also has a 3'-phosphatase activity on an all-DNA primer-template that yields a 3'-OH DNA end Agrobacterium tumefaciens AMP + diphosphate + (deoxyribonucleotide)n+m
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 ?
ATP + (deoxyribonucleotide)n + (deoxyribonucleotide)m Agrobacterium LigD2 is composed of a central ligase domain fused to a C-terminal polymerase-like (POL) domain and an N-terminal 3'-phosphoesterase (PE) module. The LigD1 protein seals DNA nicks, albeit inefficiently. The LigD2 POL domain adds ribonucleotides or deoxyribonucleotides to a DNA primer-template, with rNTPs being the preferred substrates. The PE domain catalyzes metal-dependent phosphodiesterase and phosphomonoesterase reactions at a primer-template with a 3'-terminal diribonucleotide to yield a primer-template with a monoribonucleotide 3'-OH end. The PE domain also has a 3'-phosphatase activity on an all-DNA primer-template that yields a 3'-OH DNA end Agrobacterium tumefaciens AMP + diphosphate + (deoxyribonucleotide)n+m
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 ?

Subunits

Subunits Comment Organism
More AtuLigD1 consists of a central ATP-dependent ligase domain fused to an N-terminal phosphoesterase module and a C-terminal polymerase-like domain Agrobacterium tumefaciens

Synonyms

Synonyms Comment Organism
AtuLigD1
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 Agrobacterium tumefaciens
AtuLigD2
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 Agrobacterium tumefaciens