AC   MF_03183;
DC   Protein; auto
TR   HAMAP; MF_03183; -; 1; level=0
XX
Names: Endonuclease_III_Nth
XX
ID   NTH
case <OC:Vertebrata>
DE   RecName: Full=Endonuclease III-like protein 1;
DE            EC=3.2.2.-;
DE            EC=4.2.99.18;
DE   AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase;
DE            Short=DNA glycosylase/AP lyase;
else
DE   RecName: Full=Endonuclease III homolog;
DE            EC=3.2.2.-;
DE            EC=4.2.99.18;
DE   AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase;
DE            Short=DNA glycosylase/AP lyase;
end case
case <OC:Vertebrata>
GN   Name=NTHL1;
else case <OC:Caenorhabditis>
GN   Name=nth-1;
else case <OC:Saccharomycotina>
GN   Name=NTG1;
else
GN   Name=NTH1;
end case
XX
CC   -!- FUNCTION: Bifunctional DNA N-glycosylase with associated
CC       apurinic/apyrimidinic (AP) lyase function that catalyzes the first step
CC       in base excision repair (BER), the primary repair pathway for the
CC       repair of oxidative DNA damage. The DNA N-glycosylase activity releases
CC       the damaged DNA base from DNA by cleaving the N-glycosidic bond,
CC       leaving an AP site. The AP lyase activity cleaves the phosphodiester
CC       bond 3' to the AP site by a beta-elimination. Primarily recognizes and
CC       repairs oxidative base damage of pyrimidines.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC         deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC         dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-phospho-2'-
CC         deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC         COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC         ChEBI:CHEBI:167181; EC=4.2.99.18;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC       Note=Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a
CC       role in catalysis, but is probably involved in the proper positioning
CC       of the enzyme along the DNA strand.;
end case
case <OC:Mammalia>
CC   -!- SUBUNIT: Interacts with YBX1.
end case
case not <OC:Viridiplantae>
CC   -!- SUBCELLULAR LOCATION: Nucleus. Mitochondrion.
end case
CC   -!- SIMILARITY: Belongs to the Nth/MutY family.
XX
DR   PROSITE; PS01155; ENDONUCLEASE_III_2; 1; trigger=no
DR   PROSITE; PS00764; ENDONUCLEASE_III_1; 1; trigger=no
DR   Pfam; PF00633; HHH; 1; trigger=yes
DR   Pfam; PF00730; HhH-GPD; 1; trigger=no
DR   Pfam; PF10576; EndIII_4Fe-2S; 1; trigger=no
DR   PIRSF; PIRSF001435; Nth; 1; trigger=no
case not <OC:Viridiplantae>
DR   General; TransitM; -; 0-1; trigger=yes
end case
XX
KW   DNA damage
KW   DNA repair
KW   Glycosidase
KW   Hydrolase
KW   Lyase
case not <OC:Viridiplantae>
KW   Mitochondrion
KW   Nucleus
end case
case <FTGroup:1>
KW   4Fe-4S
KW   Iron
KW   Iron-sulfur
KW   Metal-binding
end case
XX
case not <OC:Viridiplantae>
GO   GO:0005739; C:mitochondrion
GO   GO:0005634; C:nucleus
end case
GO   GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity
GO   GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity
GO   GO:0003677; F:DNA binding
case <FTGroup:1>
GO   GO:0051539; F:4 iron, 4 sulfur cluster binding
end case
GO   GO:0006285; P:base-excision repair, AP site formation
XX
FT   From: NTH_HUMAN (P78549)
FT   ACT_SITE        220
FT                   /note="Nucleophile; for N-glycosylase activity"
FT   Condition: K
FT   BINDING         290
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Group: 1; Condition: C
FT   BINDING         297
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Group: 1; Condition: C
FT   BINDING         300
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Group: 1; Condition: C
FT   BINDING         306
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT   Group: 1; Condition: C
FT   SITE            239
FT                   /note="Important for catalytic activity"
FT   Condition: D
XX
Size: 238-835;
Related: None;
Template: P78549; P31378; Q08214; Q09907;
Scope:
 Eukaryota
Fusion:
 Nter: None
 Cter: None
Duplicate: in ARATH, MUSAM, SOYBN, YEAST
Plasmid: None
Comments: None
XX
# Revision 1.14 2024/01/30
//