ID   END8_SHIF8              Reviewed;         263 AA.
AC   Q0T6V4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 24.
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=SFV_0621;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z.,
RA   Peng J., Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y.,
RA   Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(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; CP000266; ABF02872.1; -; Genomic_DNA.
DR   RefSeq; YP_688177.1; -.
DR   SMR; Q0T6V4; 2-263.
DR   GeneID; 4207375; -.
DR   GenomeReviews; CP000266_GR; SFV_0621.
DR   KEGG; sfv:SFV_0621; -.
DR   HOGENOM; Q0T6V4; -.
DR   OMA; Q0T6V4; RSDFRVP.
DR   BioCyc; SFLE373384:SFV_0621-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_1000067211.
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;  29842 MW;  A8A12258DB4E6A2E CRC64;
     MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF PQLKTYQSQL IGQHVTHVET RGKALLTHFP
     NGLTLYSHNQ LYGVWRVVDT GEEPQTTRVL RVKLQTADKT ILLYSASDIE MLRPEQLTTH
     PFLQRVGPDV LDPNLTPEVV KERLLSPRFR NRQFAGLLLD QAFLAGLGNY LRVEILWQVG
     LTGNHKAKDL NAAQLDALAH ALLEIPRFSY ATRGQVDENK HHGALFRFKV FHRDGELCER
     CGGIIEKTTL SSRPFYWCPG CQH
//