END8B_MYCTO
ID END8B_MYCTO Reviewed; 255 AA.
AC P9WNC0; L0TDQ8; P64156; P96902;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Endonuclease 8 2;
DE AltName: Full=DNA glycosylase/AP lyase Nei 2;
DE EC=3.2.2.-;
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase Nei 2;
DE EC=4.2.99.18;
DE AltName: Full=Endonuclease VIII 2;
GN Name=nei2; Synonyms=nei1; OrderedLocusNames=MT3396;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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. {ECO:0000255|PROSITE-
CC ProRule:PRU00392}.
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|PROSITE-
CC ProRule:PRU00392};
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:0000255|PROSITE-
CC ProRule:PRU00392}.
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DR EMBL; AE000516; AAK47739.1; -; Genomic_DNA.
DR PIR; B70982; B70982.
DR RefSeq; WP_003900006.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WNC0; -.
DR SMR; P9WNC0; -.
DR EnsemblBacteria; AAK47739; AAK47739; MT3396.
DR KEGG; mtc:MT3396; -.
DR PATRIC; fig|83331.31.peg.3655; -.
DR HOGENOM; CLU_038423_2_0_11; -.
DR Proteomes; UP000001020; 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 CDD; cd08971; AcNei2_N; 1.
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; IPR044090; Nei2_N.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR Pfam; PF01149; Fapy_DNA_glyco; 1.
DR Pfam; PF06831; H2TH; 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:0000250"
FT CHAIN 2..255
FT /note="Endonuclease 8 2"
FT /id="PRO_0000427153"
FT ZN_FING 221..255
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:0000255|PROSITE-ProRule:PRU00392"
FT ACT_SITE 3
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392"
FT ACT_SITE 51
FT /note="Proton donor; for beta-elimination activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392"
FT ACT_SITE 245
FT /note="Proton donor; for delta-elimination activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392"
FT BINDING 67
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
SQ SEQUENCE 255 AA; 28526 MW; 2C97B16CD7CD4002 CRC64;
MPEGDTVWHT AATLRRHLAG RTLTRCDIRV PRFAAVDLTG EVVDEVISRG KHLFIRTGTA
SIHSHLQMDG SWRVGNRPVR VDHRARIILE ANQQEQAIRV VGVDLGLLEV IDRHNDGAVV
AHLGPDLLAD DWDPQRAAAN LIVAPDRPIA EALLDQRVLA GIGNVYCNEL CFVSGVLPTA
PVSAVADPRR LVTRARDMLW VNRFRWNRCT TGDTRAGRRL WVYGRAGQGC RRCGTLIAYD
TTDERVRYWC PACQR
