ID END8B_STRCO Reviewed; 276 AA. AC O86820; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 135. DE RecName: Full=Probable 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=nei; OrderedLocusNames=SCO5760; ORFNames=SC7C7.15c; OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145). OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales; OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group. OX NCBI_TaxID=100226; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-471 / A3(2) / M145; RX PubMed=12000953; DOI=10.1038/417141a; RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H., RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.; RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor RT A3(2)."; RL Nature 417:141-147(2002). 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; AL939125; CAA19861.1; -; Genomic_DNA. DR PIR; T35693; T35693. DR RefSeq; NP_629885.1; NC_003888.3. DR RefSeq; WP_011030437.1; NZ_VNID01000007.1. DR AlphaFoldDB; O86820; -. DR SMR; O86820; -. DR STRING; 100226.gene:17763420; -. DR PaxDb; 100226-SCO5760; -. DR PATRIC; fig|100226.15.peg.5849; -. DR eggNOG; COG0266; Bacteria. DR HOGENOM; CLU_038423_2_0_11; -. DR InParanoid; O86820; -. DR OrthoDB; 9800855at2; -. DR PhylomeDB; O86820; -. DR Proteomes; UP000001973; 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:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central. DR GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central. 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 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..276 FT /note="Probable endonuclease 8 2" FT /id="PRO_0000170902" FT ZN_FING 222..260 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 250 FT /note="Proton donor; for delta-elimination activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392" FT BINDING 165 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250" SQ SEQUENCE 276 AA; 30408 MW; 01106CD65EF94DE9 CRC64; MPEGDTVWQA ARRLHDALAG RVLTRSDFRV PRYATVDLTG RTVLDVTPRG KHLLTRVEGG LTVHSHLRMD GSWKVFAPGQ RWSGGPAHQI RVILGTADRT AVGYRLPVLD ILRTAEEQRA VGHLGPDLLG PDWDPERALD NLRADPPRAL GEALLDQRNL AGIGNVYKSE LCFLLGVTPW LPVGELPADR AARLPTLAKK LLEANRDRPV RRTTGLRGQD LFVYGRAPRP CLRCGTSVRV ADQGDGSRER PTYWCPTCQA GPAPRPGGRT GVRPRR //