END8A_MYCBO
ID END8A_MYCBO Reviewed; 268 AA.
AC P64159; A0A1R3Y1I4; O53191; X2BKL9;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Endonuclease 8 1;
DE AltName: Full=DNA glycosylase/AP lyase Nei 1;
DE EC=3.2.2.-;
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase Nei 1;
DE EC=4.2.99.18;
DE AltName: Full=Endonuclease VIII 1;
GN Name=nei1; OrderedLocusNames=BQ2027_MB2491C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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 AP (apurinic/apyrimidinic) lyase activity
CC and introduces nicks in the DNA strand. Cleaves the DNA backbone by
CC beta-delta elimination to generate a single-strand break at the site of
CC the removed base with both 3'- and 5'-phosphates (By similarity).
CC {ECO:0000250}.
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;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00391};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00391};
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000305}.
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DR EMBL; LT708304; SIU01106.1; -; Genomic_DNA.
DR RefSeq; NP_856138.1; NC_002945.3.
DR RefSeq; WP_003412657.1; NC_002945.4.
DR AlphaFoldDB; P64159; -.
DR SMR; P64159; -.
DR EnsemblBacteria; SIU01106; SIU01106; BQ2027_MB2491C.
DR PATRIC; fig|233413.5.peg.2742; -.
DR OMA; ARNLFWC; -.
DR Proteomes; UP000001419; 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:0019104; F:DNA N-glycosylase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR Gene3D; 3.20.190.10; -; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
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; 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:0000250"
FT CHAIN 2..268
FT /note="Endonuclease 8 1"
FT /id="PRO_0000170904"
FT ZN_FING 234..268
FT /note="FPG-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00391"
FT ACT_SITE 2
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 3
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 52
FT /note="Proton donor; for beta-elimination activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 258
FT /note="Proton donor; for delta-elimination activity"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
SQ SEQUENCE 268 AA; 29714 MW; 1142DE185BD14F24 CRC64;
MPEGHTLHRL ARLHQRRFAG APVSVSSPQG RFADSASALN GRVLRRASAW GKHLFHHYVG
GPVVHVHLGL YGTFTEWARP TDGWLPEPAG QVRMRMVGAE FGTDLRGPTV CESIDDGEVA
DVVARLGPDP LRSDANPSSA WSRITKSRRP IGALLMDQTV IAGVGNVYRN ELLFRHRIDP
QRPGRGIGEP EFDAAWNDLV SLMKVGLRRG KIIVVRPEHD HGLPSYLPDR PRTYVYRRAG
EPCRVCGGVI RTALLEGRNV FWCPVCQT
