END3_MYCTU
ID END3_MYCTU Reviewed; 245 AA.
AC P9WQ11; L0TEW4; O69642; P63540;
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 III {ECO:0000255|HAMAP-Rule:MF_00942};
DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00942};
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_00942};
GN Name=nth {ECO:0000255|HAMAP-Rule:MF_00942}; OrderedLocusNames=Rv3674c;
GN ORFNames=MTV025.022c;
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 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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: DNA repair enzyme that has both DNA N-glycosylase activity
CC and AP-lyase activity. The DNA N-glycosylase activity releases various
CC damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving
CC an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the
CC phosphodiester bond 3' to the AP site by a beta-elimination, leaving a
CC 3'-terminal unsaturated sugar and a product with a terminal 5'-
CC phosphate. Has a preference for oxidized pyrimidines, such as thymine
CC glycol (prefers 5S isomers) 5,6-dihydrouracil:G, 5-hydroxyuracil:G, 5-
CC hydroxycytosine:G and urea:A. Cleaves ssDNA containing an AP site.
CC {ECO:0000255|HAMAP-Rule:MF_00942, 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|HAMAP-
CC Rule:MF_00942};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00942};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00942};
CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000255|HAMAP-
CC Rule:MF_00942}.
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DR EMBL; AL123456; CCP46497.1; -; Genomic_DNA.
DR PIR; C70790; C70790.
DR RefSeq; NP_218191.2; NC_000962.3.
DR RefSeq; WP_003419724.1; NZ_NVQJ01000028.1.
DR AlphaFoldDB; P9WQ11; -.
DR SMR; P9WQ11; -.
DR STRING; 83332.Rv3674c; -.
DR PaxDb; P9WQ11; -.
DR DNASU; 885058; -.
DR GeneID; 45427669; -.
DR GeneID; 885058; -.
DR KEGG; mtu:Rv3674c; -.
DR PATRIC; fig|83332.111.peg.4085; -.
DR TubercuList; Rv3674c; -.
DR eggNOG; COG0177; Bacteria.
DR OMA; QIIWYGR; -.
DR PhylomeDB; P9WQ11; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0019104; F:DNA N-glycosylase activity; IDA:MTBBASE.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:MTBBASE.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IDA:MTBBASE.
DR CDD; cd00056; ENDO3c; 1.
DR Gene3D; 1.10.1670.10; -; 1.
DR HAMAP; MF_00942; Nth; 1.
DR InterPro; IPR011257; DNA_glycosylase.
DR InterPro; IPR004036; Endonuclease-III-like_CS2.
DR InterPro; IPR003651; Endonuclease3_FeS-loop_motif.
DR InterPro; IPR004035; Endouclease-III_FeS-bd_BS.
DR InterPro; IPR003265; HhH-GPD_domain.
DR InterPro; IPR023170; HhH_base_excis_C.
DR InterPro; IPR000445; HhH_motif.
DR InterPro; IPR005759; Nth.
DR Pfam; PF10576; EndIII_4Fe-2S; 1.
DR Pfam; PF00633; HHH; 1.
DR Pfam; PF00730; HhH-GPD; 1.
DR SMART; SM00478; ENDO3c; 1.
DR SMART; SM00525; FES; 1.
DR SUPFAM; SSF48150; SSF48150; 1.
DR TIGRFAMs; TIGR01083; nth; 1.
DR PROSITE; PS00764; ENDONUCLEASE_III_1; 1.
DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Iron;
KW Iron-sulfur; Lyase; Metal-binding; Multifunctional enzyme;
KW Reference proteome.
FT CHAIN 1..245
FT /note="Endonuclease III"
FT /id="PRO_0000102219"
FT DOMAIN 119..138
FT /note="HhH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00942"
FT BINDING 198
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00942"
FT BINDING 205
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00942"
FT BINDING 208
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00942"
FT BINDING 214
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00942"
SQ SEQUENCE 245 AA; 27030 MW; 2B6D16195DD090DE CRC64;
MPGRWSAETR LALVRRARRM NRALAQAFPH VYCELDFTTP LELAVATILS AQSTDKRVNL
TTPALFARYR TARDYAQADR TELESLIRPT GFYRNKAASL IGLGQALVER FGGEVPATMD
KLVTLPGVGR KTANVILGNA FGIPGITVDT HFGRLVRRWR WTTAEDPVKV EQAVGELIER
KEWTLLSHRV IFHGRRVCHA RRPACGVCVL AKDCPSFGLG PTEPLLAAPL VQGPETDHLL
ALAGL
