ID END8_SALG2 Reviewed; 263 AA. AC B5R679; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 04-NOV-2008, sequence version 1. DT 27-MAR-2024, entry version 83. 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}; OrderedLocusNames=SG0711; OS Salmonella gallinarum (strain 287/91 / NCTC 13346). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=550538; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=287/91 / NCTC 13346; RX PubMed=18583645; DOI=10.1101/gr.077404.108; RA Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S., RA Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A., RA Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B., RA Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T., RA Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S., RA Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D., RA Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.; RT "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella RT gallinarum 287/91 provides insights into evolutionary and host adaptation RT pathways."; RL Genome Res. 18:1624-1637(2008). 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; AM933173; CAR36607.1; -; Genomic_DNA. DR RefSeq; WP_001113969.1; NC_011274.1. DR AlphaFoldDB; B5R679; -. DR SMR; B5R679; -. DR KEGG; seg:SG0711; -. DR HOGENOM; CLU_038423_2_2_6; -. DR Proteomes; UP000008321; 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_1000139942" 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; 29849 MW; 7D66A38DF536E790 CRC64; MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF AQLKPYESQL TGQLVTRIET RGKALLTHFS NGLTLYSHNQ LYGVWRVIDT GEIPQTTRIL RVRLQTADKT ILLYSASDIE MLTAEQLTTH PFLQRVGPDV LDARLTPEEV KARLLSPRFR NRQFSGLLLD QAFLAGLGNY LRVEILWQVG LTGQHKAKDL NEAQLNALSH ALLDIPRLSY TTRGQSDENK HHGALFRFKV FHRDGEACER CGGIIEKTTL SSRPFYWCPH CQK //