DB code: T00254
CATH domain | 3.30.1490.70 : Dna Ligase; domain 1 | Catalytic domain |
---|---|---|
2.40.50.140 : OB fold (Dihydrolipoamide Acetyltransferase, E2P) | Catalytic domain | |
3.30.470.30 : D-amino Acid Aminotransferase; Chain A, domain 1 | ||
E.C. | 6.5.1.1 | |
CSA | 1a0i | |
M-CSA | 1a0i | |
MACiE | M0202 |
CATH domain | Related DB codes (homologues) |
---|---|
2.40.50.140 : OB fold (Dihydrolipoamide Acetyltransferase, E2P) | M00220 M00186 T00050 D00291 D00294 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
---|---|---|---|---|
P00969 |
DNA ligase
|
EC
6.5.1.1
Polydeoxyribonucleotide synthase [ATP] |
NP_041963.1
(Protein)
NC_001604.1 (DNA/RNA sequence) |
PF01068
(DNA_ligase_A_M)
[Graphical View] |
O41026 |
|
A544R protein
|
NP_048900.1
(Protein)
NC_000852.5 (DNA/RNA sequence) |
PF01068
(DNA_ligase_A_M)
[Graphical View] |
KEGG enzyme name |
---|
deoxyribonucleic acid-joining enzyme
deoxyribonucleic repair enzyme deoxyribonucleic joinase deoxyribonucleic acid ligase deoxyribonucleic acid joinase deoxyribonucleic acid repair enzyme DNA ligase (ATP) polydeoxyribonucleotide synthase (ATP) polynucleotide ligase sealase DNA repair enzyme DNA joinase DNA ligase deoxyribonucleic ligase deoxyribonucleate ligase DNA-joining enzyme deoxyribonucleic-joining enzyme |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P00969 | DNLI_BPT7 | ATP + (deoxyribonucleotide)(n) + (deoxyribonucleotide)(m) = AMP + diphosphate + (deoxyribonucleotide)(n+m). | |||
O41026 | O41026_PBCV1 |
KEGG Pathways | Map code | Pathways | E.C. |
---|
Compound table | ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Cofactors | Substrates | Products | Intermediates | |||||||||||||
KEGG-id | C00305 | C00002 | C00039 | C00039 | C00046 | C00046 | C00020 | C00013 | C00039 | C00046 | ||||||
E.C. | ||||||||||||||||
Compound | Magnesium | ATP | (Deoxyribonucleotide)n | (Deoxyribonucleotide)m | (Ribonucleotide)n | (Ribonucleotide)m | AMP | Pyrophosphate | (Deoxyribonucleotide)n+m | (Ribonucleotide)n+m | ||||||
Type | divalent metal (Ca2+, Mg2+) | amine group,nucleotide | nucleic acids | nucleic acids | nucleic acids | nucleic acids | amine group,nucleotide | phosphate group/phosphate ion | nucleic acids | nucleic acids | ||||||
ChEBI |
18420 18420 |
15422 15422 |
16027 16027 |
29888 29888 |
||||||||||||
PubChem |
888 888 |
5957 5957 |
6083 6083 |
1023 21961011 1023 21961011 |
||||||||||||
1a0iA01 | Unbound | Bound:ATP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||
1fviA01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-bound:AMP (bound to Lys27) | |||||
1a0iA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||
1fviA02 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||
1a0iA03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||
1fviA03 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Analogue:SO4 | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
PDB;1a0i & literature [1], [7] & [8] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1a0iA01 | LYS 34;LYS 238 | ASP 36(divalent metal binding) | mutant M2V | |||||||
1fviA01 | LYS 27;LYS 186 | mutant D29A | ||||||||
1a0iA02 | LYS 240 | |||||||||
1fviA02 | LYS 188 | |||||||||
1a0iA03 | ||||||||||
1fviA03 |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[1]
|
p.608, p.611-612 | |
[2]
|
Fig.1 | 3 |
[7]
|
p.47, p.51-52, Fig.10 | 5 |
[8]
|
References | |
---|---|
[1] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) |
Medline ID | 96222302 |
PubMed ID | 8653795 |
Journal | Cell |
Year | 1996 |
Volume | 85 |
Pages | 607-15 |
Authors | Subramanya HS, Doherty AJ, Ashford SR, Wigley DB |
Title | Crystal structure of an ATP-dependent DNA ligase from bacteriophage T7. |
Related PDB | 1a0i |
Related UniProtKB | P00969 |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8626651 |
Journal | J Biol Chem |
Year | 1996 |
Volume | 271 |
Pages | 11083-9 |
Authors | Doherty AJ, Ashford SR, Subramanya HS, Wigley DB |
Title |
Bacteriophage T7 DNA ligase. |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8646532 |
Journal | Nat Struct Biol |
Year | 1996 |
Volume | 3 |
Pages | 496 |
Authors | Riddihough G |
Title | DNA ligase shows restraint. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9254695 |
Journal | Nucleic Acids Res |
Year | 1997 |
Volume | 25 |
Pages | 3403-7 |
Authors | Pritchard CE, Southern EM |
Title | Effects of base mismatches on joining of short oligodeoxynucleotides by DNA ligases. |
Related PDB | |
Related UniProtKB | |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9016621 |
Journal | Nucleic Acids Res |
Year | 1997 |
Volume | 25 |
Pages | 727-34 |
Authors | Sekiguchi J, Shuman S |
Title | Domain structure of vaccinia DNA ligase. |
Related PDB | |
Related UniProtKB | |
[6] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9878388 |
Journal | J Mol Biol |
Year | 1999 |
Volume | 285 |
Pages | 63-71 |
Authors | Doherty AJ, Wigley DB |
Title | Functional domains of an ATP-dependent DNA ligase. |
Related PDB | |
Related UniProtKB | |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10656817 |
Journal | J Mol Biol |
Year | 2000 |
Volume | 296 |
Pages | 43-56 |
Authors | Doherty AJ, Dafforn TR |
Title | Nick recognition by DNA ligases. |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11106756 |
Journal | Mol Cell |
Year | 2000 |
Volume | 6 |
Pages | 1183-93 |
Authors | Odell M, Sriskanda V, Shuman S, Nikolov DB |
Title | Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining. |
Related PDB | 1fvi |
Related UniProtKB |
Comments |
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Created | Updated |
---|---|
2004-03-25 | 2009-02-26 |