ID END8_SALTI Reviewed; 263 AA. AC Q8Z8D2; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 142. 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=STY0771, t2148; OS Salmonella typhi. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=90370; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CT18; RX PubMed=11677608; DOI=10.1038/35101607; RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J., RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M., RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A., RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T., RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A., RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A., RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., RA Barrell B.G.; RT "Complete genome sequence of a multiple drug resistant Salmonella enterica RT serovar Typhi CT18."; RL Nature 413:848-852(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700931 / Ty2; RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003; RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V., RA Kodoyianni V., Schwartz D.C., Blattner F.R.; RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and RT CT18."; RL J. Bacteriol. 185:2330-2337(2003). 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; AL513382; CAD05190.1; -; Genomic_DNA. DR EMBL; AE014613; AAO69762.1; -; Genomic_DNA. DR RefSeq; NP_455284.1; NC_003198.1. DR RefSeq; WP_001113965.1; NZ_WSUR01000015.1. DR AlphaFoldDB; Q8Z8D2; -. DR SMR; Q8Z8D2; -. DR STRING; 220341.gene:17584777; -. DR KEGG; stt:t2148; -. DR KEGG; sty:STY0771; -. DR PATRIC; fig|220341.7.peg.776; -. DR eggNOG; COG0266; Bacteria. DR HOGENOM; CLU_038423_2_2_6; -. DR OMA; YKSELCF; -. DR OrthoDB; 5657047at2; -. DR Proteomes; UP000000541; Chromosome. DR Proteomes; UP000002670; 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_0000170897" 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; 29865 MW; 63257D84FF59BEE2 CRC64; MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF AQLKPYESQL TGQLVTRIET RGKALLTHFS NGLTLYSHNQ LYGVWRVIDT GEIPQTTRIL RVRLQTADKI ILLYSASDIE MLTAEQLMTH PFLQRVGPDV LDARLTPEEV KARLLSPRFR NRQFSGLLLD QSFLAGLGNY LRVEILWQVG LTGQHKAKDL NEAQLNALSH ALLDIPRLSY TTRGQADENK HHGALFRFKV FHRDGEACER CGGIIEKTTL SSRPFYWCAH CQK //