ID END8_SALDC Reviewed; 263 AA. AC B5FNF0; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 14-OCT-2008, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=Endonuclease 8 {ECO:0000255|HAMAP-Rule:MF_01253}; DE AltName: Full=DNA glycosylase/AP lyase Nei {ECO:0000255|HAMAP-Rule:MF_01253}; DE EC=3.2.2.- {ECO:0000255|HAMAP-Rule:MF_01253}; DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_01253}; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase Nei {ECO:0000255|HAMAP-Rule:MF_01253}; DE AltName: Full=Endonuclease VIII {ECO:0000255|HAMAP-Rule:MF_01253}; GN Name=nei {ECO:0000255|HAMAP-Rule:MF_01253}; GN OrderedLocusNames=SeD_A0823; OS Salmonella dublin (strain CT_02021853). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=439851; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT_02021853; RX PubMed=21602358; DOI=10.1128/jb.00297-11; RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., RA Leclerc J.E., Ravel J., Cebula T.A.; RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for RT CRISPR-mediated adaptive sublineage evolution."; RL J. Bacteriol. 193:3556-3568(2011). CC -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation CC or by mutagenic agents. Acts as a DNA glycosylase that recognizes and CC removes damaged bases. Has a preference for oxidized pyrimidines, such CC as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Has AP CC (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA CC strand. Cleaves the DNA backbone by beta-delta elimination to generate CC a single-strand break at the site of the removed base with both 3'- and CC 5'-phosphates. {ECO:0000255|HAMAP-Rule:MF_01253}. 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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01253}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01253}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01253}; CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|HAMAP- CC Rule:MF_01253}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001144; ACH75911.1; -; Genomic_DNA. DR RefSeq; WP_001113972.1; NC_011205.1. DR AlphaFoldDB; B5FNF0; -. DR SMR; B5FNF0; -. DR KEGG; sed:SeD_A0823; -. DR HOGENOM; CLU_038423_2_2_6; -. DR Proteomes; UP000008322; Chromosome. DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR CDD; cd08965; EcNei-like_N; 1. DR Gene3D; 1.10.8.50; -; 1. DR Gene3D; 3.20.190.10; MutM-like, N-terminal; 1. DR HAMAP; MF_01253; Endonuclease_8; 1. DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd. DR InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS. DR InterPro; IPR044091; EcNei-like_N. DR InterPro; IPR023713; Endonuclease-VIII. DR InterPro; IPR012319; FPG_cat. DR InterPro; IPR035937; MutM-like_N-ter. DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH. DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase. DR InterPro; IPR010663; Znf_FPG/IleRS. DR PANTHER; PTHR42697; ENDONUCLEASE 8; 1. DR PANTHER; PTHR42697:SF1; ENDONUCLEASE 8; 1. DR Pfam; PF01149; Fapy_DNA_glyco; 1. DR Pfam; PF06831; H2TH; 1. DR Pfam; PF06827; zf-FPG_IleRS; 1. DR SMART; SM00898; Fapy_DNA_glyco; 1. DR SMART; SM01232; H2TH; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF81624; N-terminal domain of MutM-like DNA repair proteins; 1. DR SUPFAM; SSF46946; S13-like H2TH domain; 1. DR PROSITE; PS51068; FPG_CAT; 1. DR PROSITE; PS01242; ZF_FPG_1; 1. DR PROSITE; PS51066; ZF_FPG_2; 1. PE 3: Inferred from homology; KW DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase; KW Metal-binding; Multifunctional enzyme; Zinc; Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253" FT CHAIN 2..263 FT /note="Endonuclease 8" FT /id="PRO_1000139940" FT ZN_FING 229..263 FT /note="FPG-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253" FT ACT_SITE 2 FT /note="Schiff-base intermediate with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253" FT ACT_SITE 3 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253" FT ACT_SITE 53 FT /note="Proton donor; for beta-elimination activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253" FT ACT_SITE 253 FT /note="Proton donor; for delta-elimination activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253" FT BINDING 70 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253" FT BINDING 125 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253" FT BINDING 169 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253" SQ SEQUENCE 263 AA; 29877 MW; 7D6EB39AF536E787 CRC64; MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF AQLKPYESQL TGQLVTRIET RGKALLTHFS NGLTLYSHNQ LYGVWRVIDT GEIPQTTRIL RVRLQTADKT ILLYSASDIE MLTAEQLTTH PFLQRVGPDV LDARLTPEEV KVRLLSPRFR NRQFSGLLLD QAFLAGLGNY LRVEILWQVG LTGQHKAKDL NEAQLNALSH ALLDIPRLSY TTRGQSDENK HHGALFRFKV FHRDGEACER CGGIIEKTTL SSRPFYWCPH CQK //