ID END8B_MYCBO Reviewed; 255 AA. AC P64157; A0A1R3Y3Q6; P96902; X2BMS5; DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 114. DE RecName: Full=Endonuclease 8 2; DE AltName: Full=DNA glycosylase/AP lyase Nei 2; DE EC=3.2.2.-; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase Nei 2; DE EC=4.2.99.18; DE AltName: Full=Endonuclease VIII 2; GN Name=nei2; OrderedLocusNames=BQ2027_MB3325; OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=233413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=28385856; DOI=10.1128/genomea.00157-17; RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R., RA Robbe-Austerman S., Gordon S.V.; RT "Updated reference genome sequence and annotation of Mycobacterium bovis RT AF2122/97."; RL Genome Announc. 5:E00157-E00157(2017). 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 AP (apurinic/apyrimidinic) lyase activity CC and introduces nicks in the DNA strand. Cleaves the DNA backbone by CC beta-delta elimination to generate a single-strand break at the site of CC the removed base with both 3'- and 5'-phosphates. {ECO:0000255|PROSITE- CC ProRule:PRU00392}. 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|PROSITE- CC ProRule:PRU00392}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00391}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE- CC ProRule:PRU00391}; CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|PROSITE- CC ProRule:PRU00392}. 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; LT708304; SIU01954.1; -; Genomic_DNA. DR RefSeq; NP_856970.1; NC_002945.3. DR RefSeq; WP_003900006.1; NC_002945.4. DR AlphaFoldDB; P64157; -. DR SMR; P64157; -. DR PATRIC; fig|233413.5.peg.3655; -. DR Proteomes; UP000001419; 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:0019104; F:DNA N-glycosylase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR CDD; cd08971; AcNei2_N; 1. DR Gene3D; 1.10.8.50; -; 1. DR Gene3D; 3.20.190.10; MutM-like, N-terminal; 1. DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd. DR InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS. DR InterPro; IPR012319; FPG_cat. DR InterPro; IPR035937; MutM-like_N-ter. DR InterPro; IPR044090; Nei2_N. DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH. DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase. DR NCBIfam; NF040775; endonuc_Nei2; 1. 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 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; Reference proteome; Zinc; KW Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..255 FT /note="Endonuclease 8 2" FT /id="PRO_0000170900" FT ZN_FING 221..255 FT /note="FPG-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00391" FT ACT_SITE 2 FT /note="Schiff-base intermediate with DNA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392" FT ACT_SITE 3 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392" FT ACT_SITE 51 FT /note="Proton donor; for beta-elimination activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392" FT ACT_SITE 245 FT /note="Proton donor; for delta-elimination activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392" FT BINDING 67 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250" FT BINDING 164 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250" SQ SEQUENCE 255 AA; 28526 MW; 2C97B16CD7CD4002 CRC64; MPEGDTVWHT AATLRRHLAG RTLTRCDIRV PRFAAVDLTG EVVDEVISRG KHLFIRTGTA SIHSHLQMDG SWRVGNRPVR VDHRARIILE ANQQEQAIRV VGVDLGLLEV IDRHNDGAVV AHLGPDLLAD DWDPQRAAAN LIVAPDRPIA EALLDQRVLA GIGNVYCNEL CFVSGVLPTA PVSAVADPRR LVTRARDMLW VNRFRWNRCT TGDTRAGRRL WVYGRAGQGC RRCGTLIAYD TTDERVRYWC PACQR //