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, the founding member of a new family of archaeal 8-oxoguanine DNA-glycosylases.
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. 3.1.25.2 was transferred to E.C. 4.2.99.18.
This enzyme is homologous to hOgg1 (PDB; 1m3h, 1m3q), and probably catalyzes similar reactions to those by hOgg1. The literature [2] suggests the catalytic mechanism of hOgg1.
According to the literature [2] and [3], this enzyme catalyzes the following reactions:
(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, the detailed mechanism has not been elucidated yet.

Created Updated
2004-07-21 2009-02-26