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Database: UniProt
Entry: A6T6E8
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Original site: A6T6E8 
ID   END8_KLEP7              Reviewed;         263 AA.
AC   A6T6E8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   01-OCT-2014, entry version 47.
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=KPN78578_07080; ORFNames=KPN_00726;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH
OS   78578).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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: Removes damaged bases from DNA, leaving an
CC       abasic site. {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: 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}.
CC   -!- SIMILARITY: Contains 1 FPG-type zinc finger. {ECO:0000255|HAMAP-
CC       Rule:MF_01253}.
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DR   EMBL; CP000647; ABR76169.1; -; Genomic_DNA.
DR   RefSeq; YP_001334399.1; NC_009648.1.
DR   ProteinModelPortal; A6T6E8; -.
DR   SMR; A6T6E8; 2-263.
DR   STRING; 272620.KPN_00726; -.
DR   EnsemblBacteria; ABR76169; ABR76169; KPN_00726.
DR   GeneID; 5338075; -.
DR   KEGG; kpn:KPN_00726; -.
DR   PATRIC; 20455704; VBIKlePne13394_0750.
DR   eggNOG; COG0266; -.
DR   HOGENOM; HOG000020882; -.
DR   KO; K05522; -.
DR   OMA; GPDVLDM; -.
DR   OrthoDB; EOG6QP131; -.
DR   BioCyc; KPNE272620:GKDC-726-MONOMER; -.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
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; IPR012319; DNA_glycosylase/AP_lyase_cat.
DR   InterPro; IPR023713; Endonuclease-VIII.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_DNA_glyclase/IsotRNA_synth.
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   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   Complete proteome; DNA damage; DNA repair; DNA-binding; Glycosidase;
KW   Hydrolase; Lyase; Metal-binding; Multifunctional enzyme;
KW   Reference proteome; 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_1000067206.
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;  29500 MW;  F5E3F371925D0719 CRC64;
     MPEGPEIRRA ADKLEAAIKG EPLTNVWFAF PQLQPYQTQL TGQRVTHIAT RGKALLTHFS
     GGLTLYSHNQ LYGVWRVVDA GVEPQSNRVL RVRLQTASKA ILLYSASDID ILTAEQVANH
     PFLLRVGPDV LDMTLTAEQV KARLLSAKFR NRQFSGLLLD QAFLAGLGNY LRVEILWQVG
     LSGKRKAAEL SDSQLDALAH ALLDIPRLSY RTRGLVDDNK HHGALFRFKV FHRDGERCER
     CGGIIEKTTL SSRPFYWCPG CQH
//
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