ID END3_THEMA Reviewed; 213 AA. AC Q9WYK0; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 27-MAR-2024, entry version 147. 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=TM_0366; OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 OS / MSB8). OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae; OC Thermotoga. OX NCBI_TaxID=243274; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8; RX PubMed=10360571; DOI=10.1038/20601; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F., RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., RA Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). 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. {ECO:0000255|HAMAP-Rule:MF_00942}. 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}. 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; AE000512; AAD35453.1; -; Genomic_DNA. DR PIR; F72387; F72387. DR RefSeq; NP_228177.1; NC_000853.1. DR RefSeq; WP_004083173.1; NZ_CP011107.1. DR AlphaFoldDB; Q9WYK0; -. DR SMR; Q9WYK0; -. DR STRING; 243274.TM_0366; -. DR PaxDb; 243274-THEMA_02885; -. DR EnsemblBacteria; AAD35453; AAD35453; TM_0366. DR KEGG; tma:TM0366; -. DR eggNOG; COG0177; Bacteria. DR InParanoid; Q9WYK0; -. DR OrthoDB; 9800977at2; -. DR Proteomes; UP000008183; Chromosome. 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:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000703; F:oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity; IBA:GO_Central. DR GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central. DR CDD; cd00056; ENDO3c; 1. DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 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 NCBIfam; TIGR01083; nth; 1. DR PANTHER; PTHR43286; ENDONUCLEASE III-LIKE PROTEIN 1; 1. DR PANTHER; PTHR43286:SF1; ENDONUCLEASE III-LIKE PROTEIN 1; 1. DR Pfam; PF10576; EndIII_4Fe-2S; 1. DR Pfam; PF00633; HHH; 1. DR Pfam; PF00730; HhH-GPD; 1. DR PIRSF; PIRSF001435; Nth; 1. DR SMART; SM00478; ENDO3c; 1. DR SMART; SM00525; FES; 1. DR SUPFAM; SSF48150; DNA-glycosylase; 1. DR PROSITE; PS00764; ENDONUCLEASE_III_1; 1. DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Iron; KW Iron-sulfur; Lyase; Metal-binding; Reference proteome. FT CHAIN 1..213 FT /note="Endonuclease III" FT /id="PRO_0000102224" FT DOMAIN 101..120 FT /note="HhH" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00942" FT BINDING 180 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00942" FT BINDING 187 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00942" FT BINDING 190 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00942" FT BINDING 196 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00942" SQ SEQUENCE 213 AA; 24928 MW; D9716CD6FEFA85D4 CRC64; MIEELAREIV KRFPRNHKET DPFRVLISTV LSQRTRDENT EKASKKLFEV YRTPQELAKA KPEDLYDLIK ESGMYRQKAE RIVEISRILV EKYGGRVPDS LEELLKLPGV GRKTANIVLW VGFKKPALAV DTHVHRISNR LGWVKTRTPE ETEEALKKLL PEDLWGPING SMVEFGRRIC KPQNPLCEEC FLKNHCEFYR RRGKGEVRNR TER //