(data stored in ACNUC7421 zone)

SWISSPROT: END8_ECODH

ID   END8_ECODH              Reviewed;         263 AA.
AC   B1X6P5;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 57.
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=ECDH10B_0781;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Involved in base excision repair of DNA damaged by
CC       oxidation or by mutagenic agents. Acts as DNA glycosylase that
CC       recognizes and removes damaged bases. Has a preference for
CC       oxidized pyrimidines, such as thymine glycol, 5,6-dihydrouracil
CC       and 5,6-dihydrothymine. Has AP (apurinic/apyrimidinic) lyase
CC       activity and introduces nicks in the DNA strand. Cleaves the DNA
CC       backbone by beta-delta elimination to generate a single-strand
CC       break at the site of the removed base with both 3'- and 5'-
CC       phosphates. {ECO:0000255|HAMAP-Rule:MF_01253}.
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate. {ECO:0000255|HAMAP-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-
CC       Rule:MF_01253};
CC   -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|HAMAP-
CC       Rule:MF_01253}.
DR   EMBL; CP000948; ACB01923.1; -; Genomic_DNA.
DR   RefSeq; WP_001113989.1; NC_010473.1.
DR   ProteinModelPortal; B1X6P5; -.
DR   SMR; B1X6P5; -.
DR   EnsemblBacteria; ACB01923; ACB01923; ECDH10B_0781.
DR   KEGG; ecd:ECDH10B_0781; -.
DR   eggNOG; ENOG4108S0J; Bacteria.
DR   eggNOG; COG0266; LUCA.
DR   HOGENOM; HOG000020882; -.
DR   KO; K05522; -.
DR   OMA; EILWQAQ; -.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
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; IPR023713; Endonuclease-VIII.
DR   InterPro; IPR012319; FPG_cat.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_FPG/IleRS.
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; 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;
DR   PRODOM; B1X6P5.
DR   SWISS-2DPAGE; B1X6P5.
KW   DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase;
KW   Metal-binding; Multifunctional enzyme; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed. {ECO:0000255|HAMAP-
FT                                Rule:MF_01253}.
FT   CHAIN         2    263       Endonuclease 8.
FT                                /FTId=PRO_1000139934.
FT   ZN_FING     229    263       FPG-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_01253}.
FT   ACT_SITE      2      2       Schiff-base intermediate with DNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_01253}.
FT   ACT_SITE      3      3       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01253}.
FT   ACT_SITE     53     53       Proton donor; for beta-elimination
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_01253}.
FT   ACT_SITE    253    253       Proton donor; for delta-elimination
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_01253}.
FT   BINDING      70     70       DNA. {ECO:0000255|HAMAP-Rule:MF_01253}.
FT   BINDING     125    125       DNA. {ECO:0000255|HAMAP-Rule:MF_01253}.
FT   BINDING     169    169       DNA. {ECO:0000255|HAMAP-Rule:MF_01253}.
SQ   SEQUENCE   263 AA;  29845 MW;  7D10B79F58ADDA24 CRC64;
     MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF PQLKPYQSQL IGQHVTHVET RGKALLTHFS
     NDLTLYSHNQ LYGVWRVVDT GEEPQTTRVL RVKLQTADKT ILLYSASDIE MLTPEQLTTH
     PFLQRVGPDV LDPNLTPEVV KERLLSPRFR NRQFAGLLLD QAFLAGLGNY LRVEILWQVG
     LTGNHKAKDL NAAQLDALAH ALLEIPRFSY ATRGQVDENK HHGALFRFKV FHRDGEPCER
     CGSIIEKTTL SSRPFYWCPG CQH
//

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