END8B_MYCTU
ID END8B_MYCTU Reviewed; 255 AA.
AC P9WNC1; 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 42.
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=Rv3297; ORFNames=MTCY71.37;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP DISCUSSION OF FUNCTION.
RX PubMed=18457574; DOI=10.1134/s0006297908040093;
RA Sidorenko V.S., Rot M.A., Filipenko M.L., Nevinsky G.A., Zharkov D.O.;
RT "Novel DNA glycosylases from Mycobacterium tuberculosis.";
RL Biochemistry (Mosc.) 73:442-450(2008).
RN [3]
RP FUNCTION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20031487; DOI=10.1016/j.dnarep.2009.11.008;
RA Guo Y., Bandaru V., Jaruga P., Zhao X., Burrows C.J., Iwai S.,
RA Dizdaroglu M., Bond J.P., Wallace S.S.;
RT "The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit
RT different substrate preferences from their Escherichia coli counterparts.";
RL DNA Repair 9:177-190(2010).
RN [4]
RP REVIEW.
RX PubMed=21764637; DOI=10.1016/j.tube.2011.06.005;
RA Kurthkoti K., Varshney U.;
RT "Base excision and nucleotide excision repair pathways in mycobacteria.";
RL Tuberculosis 91:533-543(2011).
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 Complements an E.coli nei nth double mutant (PubMed:20031487).
CC {ECO:0000255|PROSITE-ProRule:PRU00392, ECO:0000269|PubMed:20031487}.
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}.
CC -!- CAUTION: There are 2 paralogs in M.tuberculosis, in a reference this
CC gene is called nei1. {ECO:0000305|PubMed:18457574}.
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DR EMBL; AL123456; CCP46116.1; -; Genomic_DNA.
DR PIR; B70982; B70982.
DR RefSeq; NP_217814.1; NC_000962.3.
DR RefSeq; WP_003900006.1; NZ_NVQJ01000003.1.
DR AlphaFoldDB; P9WNC1; -.
DR SMR; P9WNC1; -.
DR STRING; 83332.Rv3297; -.
DR PaxDb; P9WNC1; -.
DR DNASU; 887937; -.
DR GeneID; 887937; -.
DR KEGG; mtu:Rv3297; -.
DR TubercuList; Rv3297; -.
DR eggNOG; COG0266; Bacteria.
DR OMA; TYWCPRC; -.
DR PhylomeDB; P9WNC1; -.
DR Proteomes; UP000001584; 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; IDA:MTBBASE.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:MTBBASE.
DR GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IDA:MTBBASE.
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; Reference proteome; Zinc;
KW 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_0000170901"
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
