ID A0A4Y8TS91_9BURK Unreviewed; 218 AA. AC A0A4Y8TS91; DT 18-SEP-2019, integrated into UniProtKB/TrEMBL. DT 18-SEP-2019, sequence version 1. DT 11-DEC-2019, entry version 4. 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:TFF62843.1}; GN ORFNames=EIC84_01970 {ECO:0000313|EMBL:TFF62843.1}; OS Comamonas sp. A23. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Comamonas; unclassified Comamonas. OX NCBI_TaxID=2494248 {ECO:0000313|EMBL:TFF62843.1, ECO:0000313|Proteomes:UP000298026}; RN [1] {ECO:0000313|Proteomes:UP000298026} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A23 {ECO:0000313|Proteomes:UP000298026}; RA Wang X.; RT "Photobacterium sp. BEI247 sp. nov., a marine bacterium isolated from RT Yongle Blue Hole in the South China Sea."; RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases. 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=The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA CC is broken by a beta-elimination reaction, leaving a 3'-terminal CC unsaturated sugar and a product with a terminal 5'-phosphate.; CC EC=4.2.99.18; Evidence={ECO:0000256|HAMAP-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. {ECO:0000256|HAMAP- CC Rule:MF_00942}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:TFF62843.1}. 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; RSDT01000001; TFF62843.1; -; Genomic_DNA. DR RefSeq; WP_003063022.1; NZ_RSDT01000001.1. DR Proteomes; UP000298026; Unassembled WGS sequence. 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; -; 1. DR HAMAP; MF_00942; Nth; 1. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR004036; Endonuclease-III-like_CS2. DR InterPro; IPR004035; Endouclease-III_FeS-bd_BS. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR000445; HhH_motif. DR InterPro; IPR023170; HTH_base_excis_C. DR InterPro; IPR005759; Nth. DR Pfam; PF00633; HHH; 1. DR Pfam; PF00730; HhH-GPD; 1. DR SMART; SM00478; ENDO3c; 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 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00942}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00942}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00942}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00942}; KW Endonuclease {ECO:0000313|EMBL:TFF62843.1}; KW Glycosidase {ECO:0000256|HAMAP-Rule:MF_00942}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00942}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00942}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00942}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_00942}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00942}; KW Nuclease {ECO:0000313|EMBL:TFF62843.1}. FT DOMAIN 38..185 FT /note="ENDO3c" FT /evidence="ECO:0000259|SMART:SM00478" FT METAL 187 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT METAL 194 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT METAL 197 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT METAL 203 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" SQ SEQUENCE 218 AA; 24028 MW; ECB4BFAEDD2CFCDB CRC64; MKKNDIAPFF AALKAANPTP QTELEYTTVF ELLTAVLLSA QATDVGVNKA TRKLFPVANT PQAILDLGLE GLESYIKTIG LYRSKAKHLM ETCRMLVQLH GGTVPRTREE LEALPGVGRK TANVVLNVAF GQPTMAVDTH IFRVSNRTGL APGKNPLEVE KQLLKRVPDE YAVDSHHWLI LLGRYVCQAR KPRCWECVAS KYCDFTPQTP APAAGKKS //