DB code: D00511
CATH domain | 1.10.1670.10 : Endonuclease Iii, domain 2 | |
---|---|---|
1.10.340.30 : Endonuclease III; domain 1 | ||
E.C. | 3.2.2.- 4.2.99.18 | |
CSA | ||
M-CSA | ||
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
1.10.1670.10 : Endonuclease Iii, domain 2 | T00070 D00266 |
1.10.340.30 : Endonuclease III; domain 1 | S00749 T00070 D00266 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
---|---|---|---|---|
Q8U2D5 |
N-glycosylase/DNA lyase
|
8-oxoguanine DNA glycosylase
EC 3.2.2.- AGOG DNA-(apurinic or apyrimidinic site) lyase AP lyase EC 4.2.99.18 |
NP_578633.2
(Protein)
NC_003413.1 (DNA/RNA sequence) |
PF09171
(DUF1886)
[Graphical View] |
Q8ZVK6 |
N-glycosylase/DNA lyase
|
8-oxoguanine DNA glycosylase
EC 3.2.2.- AGOG DNA-(apurinic or apyrimidinic site) lyase AP lyase EC 4.2.99.18 Pa-AGOG |
NP_559868.1
(Protein)
NC_003364.1 (DNA/RNA sequence) |
PF09171
(DUF1886)
[Graphical View] |
KEGG enzyme name |
---|
DNA-(apurinic or apyrimidinic site) lyase
(EC 4.2.99.18 ) AP lyase (EC 4.2.99.18 ) AP endonuclease class I (EC 4.2.99.18 ) endodeoxyribonuclease (apurinic or apyrimidinic) (EC 4.2.99.18 ) deoxyribonuclease (apurinic or apyrimidinic) (EC 4.2.99.18 ) E. coli endonuclease III (EC 4.2.99.18 ) phage-T4 UV endonuclease (EC 4.2.99.18 ) Micrococcus luteus UV endonuclease (EC 4.2.99.18 ) AP site-DNA 5'-phosphomonoester-lyase (EC 4.2.99.18 ) X-ray endonuclease III (EC 4.2.99.18 ) |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
Q8U2D5 | AGOG_PYRFU | The C-O-P bond 3'' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3''-terminal unsaturated sugar and a product with a terminal 5''-phosphate. | |||
Q8ZVK6 | AGOG_PYRAE | The C-O-P bond 3'' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3''-terminal unsaturated sugar and a product with a terminal 5''-phosphate. |
KEGG Pathways | Map code | Pathways | E.C. |
---|
Compound table | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | ||||||||
KEGG-id | C02270 | C03484 | C00578 | L00013 | ||||||
E.C. |
4.2.99.18
|
4.2.99.18
|
4.2.99.18
|
4.2.99.18
|
||||||
Compound | Base-removed DNA | Apyrimidinic site in DNA | DNA 5'-phosphate | DNA 3'-trans-alpha,beta unsaturated aldehyde | ||||||
Type | carbohydrate,nucleic acids,phosphate group/phosphate ion | nucleic acids | nucleic acids,phosphate group/phosphate ion | nucleic acids,carbohydrate | ||||||
ChEBI | ||||||||||
PubChem | ||||||||||
1xg7A01 | Unbound | Unbound | Unbound | Unbound | ||||||
1xg7B01 | Unbound | Unbound | Unbound | Unbound | ||||||
1xqoA01 | Unbound | Unbound | Unbound | Unbound | ||||||
1xqpA01 | Analogue:8HG_255 | Unbound | Unbound | Unbound | ||||||
1xg7A02 | Unbound | Unbound | Unbound | Unbound | ||||||
1xg7B02 | Unbound | Unbound | Unbound | Unbound | ||||||
1xqoA02 | Unbound | Unbound | Unbound | Unbound | ||||||
1xqpA02 | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
literature [2], [3] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1xg7A01 | ASP 176 | |||||||||
1xg7B01 | ASP 176 | |||||||||
1xqoA01 | ASP 172 | |||||||||
1xqpA01 | ASP 172 | |||||||||
1xg7A02 | LYS 144 | |||||||||
1xg7B02 | LYS 144 | |||||||||
1xqoA02 | LYS 140 | |||||||||
1xqpA02 | LYS 140 |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[2]
|
Fig.1, p.1646-1647 | |
[3]
|
p.96 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15604455 |
Journal | Nucleic Acids Res |
Year | 2004 |
Volume | 32 |
Pages | 6531-9 |
Authors | Sartori AA, Lingaraju GM, Hunziker P, Winkler FK, Jiricny J |
Title |
Pa-AGOG, |
Related PDB | |
Related UniProtKB | Q8ZVK6 |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15610848 |
Journal | Chem Biol |
Year | 2004 |
Volume | 11 |
Pages | 1643-9 |
Authors | Chung SJ, Verdine GL |
Title | Structures of end products resulting from lesion processing by a DNA glycosylase/lyase. |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15642264 |
Journal | Structure |
Year | 2005 |
Volume | 13 |
Pages | 87-98 |
Authors | Lingaraju GM, Sartori AA, Kostrewa D, Prota AE, Jiricny J, Winkler FK |
Title | A DNA glycosylase from Pyrobaculum aerophilum with an 8-oxoguanine binding mode and a noncanonical helix-hairpin-helix structure. |
Related PDB | 1xqo 1xqp |
Related UniProtKB | Q8ZVK6 |
Comments |
---|
E.C. This enzyme is homologous to hOgg1 (PDB; 1m3h, According to the literature [2] and [3], (A) Transfer of DNA deoxyribose from DNA base nitrogen atom to sidechain of Lysine residue: (B) Intramolecular elimination (Sugar opening) leading to Schiff-base formation on Lysine residue: (C) Isomerization (Shift of double-bond): (D) Elimination of 5'-phosphate of DNA leading to formation of alpha,beta-unsaturated Schiff base and DNA-5'-phosphate: (E) Deformation of Schiff-base from Lysine residue: However, |
Created | Updated |
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2004-07-21 | 2009-02-26 |