HAMAP rule MF_03183

General rule information [?]

PURL	https://purl.expasy.org/hamap/rule/MF_03183
Accession	MF_03183
Dates	6-MAR-2014 (Created) 30-JAN-2024 (Last updated, Version 14)
Name	Endonuclease_III_Nth
Scope(s)	Eukaryota
Template(s)	P78549 (NTH_HUMAN); P31378 (NTH1_YEAST); Q08214 (NTH2_YEAST); Q09907 (NTH_SCHPO); [ Recover all ]
Triggered by	HAMAP; MF_03183 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

Identifier	NTH
case <OC:Vertebrata>
Protein name	RecName: Full=Endonuclease III-like protein 1; EC=3.2.2.-; EC=4.2.99.18; AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase; Short=DNA glycosylase/AP lyase;
else
Protein name	RecName: Full=Endonuclease III homolog; EC=3.2.2.-; EC=4.2.99.18; AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase; Short=DNA glycosylase/AP lyase;
end case
case <OC:Vertebrata>
Gene name	Name=NTHL1;
else case <OC:Caenorhabditis>
Gene name	Name=nth-1;
else case <OC:Saccharomycotina>
Gene name	Name=NTG1;
else
Gene name	Name=NTH1;
end case

Comments [?]

FUNCTION	Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
CATALYTIC ACTIVITY	Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'- deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3- dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'- deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA- COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695, ChEBI:CHEBI:167181; EC=4.2.99.18;
case <FTGroup:1>
COFACTOR	Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.;
end case
case <OC:Mammalia>
SUBUNIT	Interacts with YBX1.
end case
case not <OC:Viridiplantae>
SUBCELLULAR LOCATION	Nucleus. Mitochondrion.
end case
SIMILARITY	Belongs to the Nth/MutY family.

Keywords [?]

Gene Ontology [?]

case not <OCellular component:Viridiplantae>
GO:0005739; Cellular component:mitochondrion
GO:0005634; Cellular component:nucleus
end case
GO:0000703; Molecular function:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity
GO:0003906; Molecular function:DNA-(apurinic or apyrimidinic site) endonuclease activity
GO:0003677; Molecular function:DNA binding
case <FTGroup:1>
GO:0051539; Molecular function:4 iron, 4 sulfur cluster binding
end case
GO:0006285; Biological process:base-excision repair, AP site formation

Cross-references [?]

Features [?]

From: NTH_HUMAN (P78549)

Key

From

Description

Tag

Condition

FTGroup

ACT_SITE

220

/note="Nucleophile; for N-glycosylase activity"

BINDING

290

/ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"

BINDING

297

/ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"

BINDING

300

/ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"

BINDING

306

/ligand="[4Fe-4S] cluster"
/ligand_id="ChEBI:CHEBI:49883"

SITE

239

/note="Important for catalytic activity"

Additional information [?]