ID A0A096PAM0_OSTTA Unreviewed; 355 AA.
AC A0A096PAM0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Endonuclease III homolog {ECO:0000256|HAMAP-Rule:MF_03183};
DE EC=3.2.2.- {ECO:0000256|HAMAP-Rule:MF_03183};
DE EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_03183};
DE AltName: Full=Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|HAMAP-Rule:MF_03183};
DE Short=DNA glycosylase/AP lyase {ECO:0000256|HAMAP-Rule:MF_03183};
GN Name=NTH1 {ECO:0000256|HAMAP-Rule:MF_03183};
GN ORFNames=OT_ostta14g00980 {ECO:0000313|EMBL:CEG02021.1};
OS Ostreococcus tauri.
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=70448 {ECO:0000313|EMBL:CEG02021.1, ECO:0000313|Proteomes:UP000009170};
RN [1] {ECO:0000313|Proteomes:UP000009170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OTTH0595 {ECO:0000313|Proteomes:UP000009170};
RX PubMed=16868079; DOI=10.1073/pnas.0604795103;
RA Derelle E., Ferraz C., Rombauts S., Rouze P., Worden A.Z., Robbens S.,
RA Partensky F., Degroeve S., Echeynie S., Cooke R., Saeys Y., Wuyts J.,
RA Jabbari K., Bowler C., Panaud O., Piegu B., Ball S.G., Ral J.-P.,
RA Bouget F.-Y., Piganeau G., De Baets B., Picard A., Delseny M., Demaille J.,
RA Van de Peer Y., Moreau H.;
RT "Genome analysis of the smallest free-living eukaryote Ostreococcus tauri
RT unveils many unique features.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11647-11652(2006).
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. {ECO:0000256|HAMAP-
CC Rule:MF_03183}.
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'-monophospho-
CC 2'-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;
CC Evidence={ECO:0000256|ARBA:ARBA00024490, ECO:0000256|HAMAP-
CC Rule:MF_03183};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03183};
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. {ECO:0000256|HAMAP-Rule:MF_03183};
CC -!- SIMILARITY: Belongs to the Nth/MutY family.
CC {ECO:0000256|ARBA:ARBA00008343, ECO:0000256|HAMAP-Rule:MF_03183}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CEG02021.1}.
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DR EMBL; CAID01000014; CEG02021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A096PAM0; -.
DR STRING; 70448.A0A096PAM0; -.
DR InParanoid; A0A096PAM0; -.
DR OrthoDB; 3377194at2759; -.
DR Proteomes; UP000009170; Chromosome 14.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IEA:UniProtKB-UniRule.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1.
DR HAMAP; MF_03183; Endonuclease_III_Nth; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR004036; Endonuclease-III-like_CS2.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR030841; NTH1.
DR PANTHER; PTHR43286; ENDONUCLEASE III-LIKE PROTEIN 1; 1.
DR PANTHER; PTHR43286:SF1; ENDONUCLEASE III-LIKE PROTEIN 1; 1.
DR Pfam; PF00633; HHH; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SUPFAM; SSF48150; DNA-glycosylase; 1.
DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_03183};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP-
KW Rule:MF_03183};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP-
KW Rule:MF_03183};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP-
KW Rule:MF_03183};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03183};
KW Iron {ECO:0000256|HAMAP-Rule:MF_03183};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_03183};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03183};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_03183};
KW Reference proteome {ECO:0000313|Proteomes:UP000009170}.
FT DOMAIN 147..306
FT /note="HhH-GPD"
FT /evidence="ECO:0000259|SMART:SM00478"
FT REGION 26..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 229
FT /note="Nucleophile; for N-glycosylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03183"
FT BINDING 308
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03183"
FT BINDING 315
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03183"
FT BINDING 318
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03183"
FT BINDING 326
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03183"
FT SITE 248
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03183"
SQ SEQUENCE 355 AA; 39028 MW; 4C990F69F93F92A6 CRC64;
MYAHVARALS RLLAPVSIAF GRRARADPNA MSRRVAASPS RAKDGDAAPE PEKPSTSSAT
DDVTTPIRAK VNSRKKPVKT EDERSVVAIE PEGWEKTLET IKRWRADGPP AAVDTMGCEK
IADVEDDRVN VDGDRYRRYL TLTSAMLSSQ TKDEINHAAM RRLRAHGCTP ENILNTDEDA
LDAMINPVGF HRRKAQYLRA TAKILLDEYD GDIPPSVETL CALPGVGPKM AYLVMNVGWG
EPTGICVDVH VHRISERLGW VAKDVMGKNG SPRKKTPEDT RAALESWLPK HEWIEINPLL
VGFGQLTCTP LRPKCHACPL AKDGSCPSAF KENPASPESA KKRPKLELKL EGDDA
//
