END8B_STRCO
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 03-AUG-2022, entry version 127.
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; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC 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 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;
CC Evidence={ECO:0000255|PROSITE-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}.
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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.SCO5760; -.
DR GeneID; 1101202; -.
DR KEGG; sco:SCO5760; -.
DR PATRIC; fig|100226.15.peg.5849; -.
DR eggNOG; COG0266; Bacteria.
DR HOGENOM; CLU_038423_2_0_11; -.
DR InParanoid; O86820; -.
DR OMA; TYWCPRC; -.
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; 3.20.190.10; -; 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_S13-like_H2TH.
DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
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; SSF46946; SSF46946; 1.
DR SUPFAM; SSF81624; SSF81624; 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
