ID   END8_ECOUT              Reviewed;         263 AA.
AC   Q1REK9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 27.
DE   RecName: Full=Endonuclease 8;
DE   AltName: Full=Endonuclease VIII;
DE   AltName: Full=DNA glycosylase/AP lyase Nei;
DE            EC=3.2.2.-;
DE            EC=4.2.99.18;
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase Nei;
GN   Name=nei; OrderedLocusNames=UTI89_C0712;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA   Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA   Hultgren S.J., Gordon J.I.;
RT   "Identification of genes subject to positive selection in
RT   uropathogenic strains of Escherichia coli: a comparative genomics
RT   approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: Removes damaged bases from DNA, leaving an
CC       abasic site.
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.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SIMILARITY: Belongs to the FPG family.
CC   -!- SIMILARITY: Contains 1 FPG-type zinc finger.
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DR   EMBL; CP000243; ABE06205.1; -; Genomic_DNA.
DR   RefSeq; YP_539736.1; -.
DR   SMR; Q1REK9; 2-263.
DR   GeneID; 3993974; -.
DR   GenomeReviews; CP000243_GR; UTI89_C0712.
DR   KEGG; eci:UTI89_C0712; -.
DR   HOGENOM; Q1REK9; -.
DR   OMA; Q1REK9; RSDFRVP.
DR   BioCyc; ECOL364106:UTI89_C0712-MON; -.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0000703; F:oxidized pyrimidine base lesion DNA N-glyco...; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   HAMAP; MF_01253; -; 1.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR000214; DNA_glyclase/AP_lyase_Znf_dom.
DR   InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
DR   InterPro; IPR012319; DNA_glycosylase/AP_lyase_cat.
DR   Pfam; PF01149; Fapy_DNA_glyco; 1.
DR   Pfam; PF06831; H2TH; 1.
DR   ProDom; PD003680; Fapy_DNA_glyco; 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   Complete proteome; DNA damage; DNA repair; DNA-binding; Glycosidase;
KW   Hydrolase; Lyase; Metal-binding; Multifunctional enzyme; Zinc;
KW   Zinc-finger.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    263       Endonuclease 8.
FT                                /FTId=PRO_1000067203.
FT   ZN_FING     229    263       FPG-type.
FT   ACT_SITE      2      2       Schiff-base intermediate with DNA (By
FT                                similarity).
FT   ACT_SITE      3      3       Proton donor (By similarity).
FT   ACT_SITE     53     53       Proton donor; for beta-elimination
FT                                activity (By similarity).
FT   ACT_SITE    253    253       Proton donor; for delta-elimination
FT                                activity (By similarity).
FT   BINDING      70     70       DNA (By similarity).
FT   BINDING     125    125       DNA (By similarity).
FT   BINDING     169    169       DNA (By similarity).
SQ   SEQUENCE   263 AA;  29799 MW;  0D8EE2D6C8C00727 CRC64;
     MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF PQLKSYQSRL IGQHVTHVET RGKALLTHFS
     NDLTLYSHNQ LYGVWRVVDT GEEPQTTRVL RVKLQTADKT ILLYSASDIE MLTPEQLTTH
     PFLQRVGPDV LDPNLTPEVV KERLLSPRFR NRQFAGLLLD QAFLAGLGNY LRVEILWQVG
     LTGNHKAKDL NAAQLDALAH ALLDTPRLSY ATRGQVDENK YHGALFRFKV FHRDGEPCER
     CGGIIEKTTL SSRPFYWCPG CQH
//