END8_SALPB
ID END8_SALPB Reviewed; 263 AA.
AC A9MTR2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
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}; OrderedLocusNames=SPAB_02805;
OS Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1016998;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1250 / SPB7;
RG The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA Johnson M., Thiruvilangam P., Wilson R.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation
CC or by mutagenic agents. Acts as DNA glycosylase that recognizes and
CC removes damaged bases. Has a preference for oxidized pyrimidines, such
CC as thymine glycol, 5,6-dihydrouracil and 5,6-dihydrothymine. Has AP
CC (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA
CC strand. Cleaves the DNA backbone by beta-delta elimination to generate
CC a single-strand break at the site of the removed base with both 3'- and
CC 5'-phosphates. {ECO:0000255|HAMAP-Rule:MF_01253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|HAMAP-
CC 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-Rule:MF_01253};
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|HAMAP-
CC Rule:MF_01253}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000886; ABX68177.1; -; Genomic_DNA.
DR RefSeq; WP_001113966.1; NC_010102.1.
DR AlphaFoldDB; A9MTR2; -.
DR SMR; A9MTR2; -.
DR KEGG; spq:SPAB_02805; -.
DR PATRIC; fig|1016998.12.peg.2651; -.
DR HOGENOM; CLU_038423_2_2_6; -.
DR OMA; TYWCPRC; -.
DR BioCyc; SENT1016998:SPAB_RS11410-MON; -.
DR Proteomes; UP000008556; Chromosome.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
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-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR CDD; cd08965; EcNei-like_N; 1.
DR Gene3D; 3.20.190.10; -; 1.
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; IPR044091; EcNei-like_N.
DR InterPro; IPR023713; Endonuclease-VIII.
DR InterPro; IPR012319; FPG_cat.
DR InterPro; IPR035937; MutM-like_N-ter.
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;
KW DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase;
KW Metal-binding; Multifunctional enzyme; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT CHAIN 2..263
FT /note="Endonuclease 8"
FT /id="PRO_1000085802"
FT ZN_FING 229..263
FT /note="FPG-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT ACT_SITE 2
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT ACT_SITE 3
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT ACT_SITE 53
FT /note="Proton donor; for beta-elimination activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT ACT_SITE 253
FT /note="Proton donor; for delta-elimination activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT BINDING 70
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT BINDING 125
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
FT BINDING 169
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01253"
SQ SEQUENCE 263 AA; 29780 MW; 2D6A0AAB2E5B5141 CRC64;
MPEGPEIRRA ADNLEAAIKG KPLTDVWFAF AQLKPYESQL TGQLVTRIET RGKALLTHFS
NGLTLYSHNQ LYGVWRVIDT GEIPQTTRIL RVRLQTADKT ILLYSASDIE MLTAEQLTTH
PFLQRVGPDV LDARLTPEEV KARLLSPRFC NRQFSGLLLD QAFLAGLGNY LRVEILWQVG
LTGQHKAKDL NEAQLNALSH ALLDIPRLSY TTRGQADENK HHGALFRFKV FHRDGEACER
CGGIIEKTTL SSRPFYWCPH CQK
