ID END3_RICPR Reviewed; 212 AA. AC O05956; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 27-MAR-2024, entry version 134. 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=RP746; OS Rickettsia prowazekii (strain Madrid E). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group. OX NCBI_TaxID=272947; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9274032; DOI=10.1099/00221287-143-8-2783; RA Andersson J.O., Andersson S.G.E.; RT "Genomic rearrangements during evolution of the obligate intracellular RT parasite Rickettsia prowazekii as inferred from an analysis of 52015 bp RT nucleotide sequence."; RL Microbiology 143:2783-2795(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Madrid E; RX PubMed=9823893; DOI=10.1038/24094; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T., RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H., RA Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). 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; Y11778; CAA72458.1; -; Genomic_DNA. DR EMBL; AJ235273; CAA15174.1; -; Genomic_DNA. DR PIR; F71634; F71634. DR RefSeq; NP_221098.1; NC_000963.1. DR RefSeq; WP_004597010.1; NC_000963.1. DR AlphaFoldDB; O05956; -. DR SMR; O05956; -. DR STRING; 272947.gene:17555816; -. DR EnsemblBacteria; CAA15174; CAA15174; CAA15174. DR GeneID; 57569867; -. DR KEGG; rpr:RP746; -. DR PATRIC; fig|272947.5.peg.779; -. DR eggNOG; COG0177; Bacteria. DR HOGENOM; CLU_012862_3_3_5; -. DR OrthoDB; 9800977at2; -. DR Proteomes; UP000002480; 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:0019104; F:DNA N-glycosylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. 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; PTHR10359; A/G-SPECIFIC ADENINE GLYCOSYLASE/ENDONUCLEASE III; 1. DR PANTHER; PTHR10359:SF18; ENDONUCLEASE III; 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..212 FT /note="Endonuclease III" FT /id="PRO_0000102221" FT DOMAIN 108..127 FT /note="HhH" 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 194 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00942" FT BINDING 197 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00942" FT BINDING 203 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00942" SQ SEQUENCE 212 AA; 24174 MW; A7FDA4F6033A6382 CRC64; MQAQIMNKIF EIFSKNNPKP QTELIYKNDF TLLVAVILSA RATDISVNLA TKHLFETYNT PEKFLELGEE GLKKYIKSIG LFNSKAKNII ALCQILIKNY QTSIPNNFKE LVKLPGVGRK TANVVLNCLF AMPTMAVDTH VFRVSKRIGL AKGNTAAIVE KELLQIIDEK WLTYAHHWLI LHGRYICKAR KPGCNICPIK EYCEYYINTF SS //