ID Q1RGX7_RICBR Unreviewed; 315 AA. AC Q1RGX7; DT 16-MAY-2006, integrated into UniProtKB/TrEMBL. DT 16-MAY-2006, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=Endonuclease III {ECO:0000256|HAMAP-Rule:MF_00942}; DE EC=4.2.99.18 {ECO:0000256|HAMAP-Rule:MF_00942}; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000256|HAMAP-Rule:MF_00942}; GN Name=nth {ECO:0000256|HAMAP-Rule:MF_00942, GN ECO:0000313|EMBL:ABE05387.1}; GN OrderedLocusNames=RBE_1306 {ECO:0000313|EMBL:ABE05387.1}; OS Rickettsia bellii (strain RML369-C). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group. OX NCBI_TaxID=336407 {ECO:0000313|EMBL:ABE05387.1, ECO:0000313|Proteomes:UP000001951}; RN [1] {ECO:0000313|EMBL:ABE05387.1, ECO:0000313|Proteomes:UP000001951} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RML369-C {ECO:0000313|EMBL:ABE05387.1, RC ECO:0000313|Proteomes:UP000001951}; RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076; RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C., RA Fournier P.-E., Claverie J.-M., Raoult D.; RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in RT gene exchanges between intracellular pathogens."; RL PLoS Genet. 2:733-744(2006). 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:0000256|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:0000256|HAMAP- CC Rule:MF_00942}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00942}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|HAMAP-Rule:MF_00942}; CC -!- SIMILARITY: Belongs to the Nth/MutY family. CC {ECO:0000256|ARBA:ARBA00008343, ECO:0000256|HAMAP-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; CP000087; ABE05387.1; -; Genomic_DNA. DR AlphaFoldDB; Q1RGX7; -. DR KEGG; rbe:RBE_1306; -. DR eggNOG; COG0177; Bacteria. DR HOGENOM; CLU_012862_3_4_5; -. DR Proteomes; UP000001951; 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:0004519; F:endonuclease activity; IEA:UniProtKB-KW. 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; 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 SMART; SM00478; ENDO3c; 1. DR SMART; SM00525; FES; 1. DR SUPFAM; SSF48150; DNA-glycosylase; 1. DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00942}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_00942}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_00942}; DNA-binding {ECO:0000256|HAMAP-Rule:MF_00942}; KW Endonuclease {ECO:0000313|EMBL:ABE05387.1}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|HAMAP- KW Rule:MF_00942}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00942}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00942}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_00942}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00942, ECO:0000313|EMBL:ABE05387.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00942}; Nuclease {ECO:0000313|EMBL:ABE05387.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001951}. FT DOMAIN 140..287 FT /note="HhH-GPD" FT /evidence="ECO:0000259|SMART:SM00478" FT BINDING 289 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT BINDING 296 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT BINDING 299 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT BINDING 305 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" SQ SEQUENCE 315 AA; 35162 MW; 03575C9BCD220E9D CRC64; MSQPPTNSPL IYNCGNVGQS LKTFKDSRNS GSDNTSISRN STPSLVKIIT TLPENPHIGA SLVPFMNNTT LLFFISFSIN LKLLFSNIKN LICLILFVTL YTMQAEIVNK IFEVFSKNNE NPKTELVYKN NFTLLVAVIL SAQATDVSVN LATKSLFEIY DTPEKILGLG EEGLKKYIKS IGLFNSKAKN VIALCQILIS NYDSKVPNNF EELVKLPGVG RKTANVVLNC LFGLPTMAVD THVFRVAKRI GLAKGNTPEA VEKELLQIID GKWLSHAHHW LILHGRYICK ARKPDCEICP IKEYCEYYKS ATKII //