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-MAY-2013, entry version 39.
DE RecName: Full=Endonuclease 8;
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;
DE AltName: Full=Endonuclease VIII;
GN Name=nei; 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 (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; 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 GeneID; 5338075; -.
DR KEGG; kpn:KPN_00726; -.
DR PATRIC; 20455704; VBIKlePne13394_0750.
DR eggNOG; COG0266; -.
DR HOGENOM; HOG000020882; -.
DR KO; K05522; -.
DR OMA; WFAFPEL; -.
DR ProtClustDB; PRK10445; -.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IEA:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA: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; SSF81624; Form_DNAglyc_cat; 1.
DR SUPFAM; SSF46946; Ribosomal_H2TH; 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_1000067206.
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; 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
//
