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}; 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;
CC Evidence={ECO:0000255|HAMAP-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}.
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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
//
