ID I6DHW4_SHIBO Unreviewed; 211 AA. AC I6DHW4; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 28-FEB-2018, entry version 35. 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:EIQ31356.1}; GN ORFNames=SB96558_1859 {ECO:0000313|EMBL:EIQ31356.1}; OS Shigella boydii 965-58. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Shigella. OX NCBI_TaxID=766138 {ECO:0000313|EMBL:EIQ31356.1, ECO:0000313|Proteomes:UP000004209}; RN [1] {ECO:0000313|EMBL:EIQ31356.1, ECO:0000313|Proteomes:UP000004209} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=965-58 {ECO:0000313|EMBL:EIQ31356.1, RC ECO:0000313|Proteomes:UP000004209}; RA Rasko D., Redman J., Daugherty S.C., Tallon L., Sadzewicz L., RA Jones K., Santana-Cruz I., Liu X.; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase CC activity and AP-lyase activity. The DNA N-glycosylase activity CC releases various damaged pyrimidines from DNA by cleaving the N- CC glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The CC AP-lyase activity cleaves the phosphodiester bond 3' to the AP CC site by a beta-elimination, leaving a 3'-terminal unsaturated CC sugar and a product with a terminal 5'-phosphate. CC {ECO:0000256|HAMAP-Rule:MF_00942}. CC -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or CC apyrimidinic site in DNA is broken by a beta-elimination reaction, CC leaving a 3'-terminal unsaturated sugar and a product with a CC terminal 5'-phosphate. {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 CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EIQ31356.1}. 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; AKNA01000046; EIQ31356.1; -; Genomic_DNA. DR RefSeq; WP_001030341.1; NZ_AKNA01000046.1. DR EnsemblBacteria; EIQ31356; EIQ31356; SB96558_1859. DR PATRIC; fig|766138.3.peg.1922; -. DR Proteomes; UP000004209; 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) lyase activity; IEA:UniProtKB-EC. DR GO; GO:0140080; F:class III/IV DNA-(apurinic or apyrimidinic site) lyase 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; -; 2. 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; IPR000445; HhH_motif. DR InterPro; IPR023170; HTH_base_excis_C. 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 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_00942}; KW Complete proteome {ECO:0000313|Proteomes:UP000004209}; 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:EIQ31356.1}; 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, ECO:0000313|EMBL:EIQ31356.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00942}; KW Nuclease {ECO:0000313|EMBL:EIQ31356.1}. FT DOMAIN 38 185 ENDO3c. {ECO:0000259|SMART:SM00478}. FT METAL 187 187 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_00942}. FT METAL 194 194 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_00942}. FT METAL 197 197 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_00942}. FT METAL 203 203 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_00942}. SQ SEQUENCE 211 AA; 23578 MW; FF425234E005902B CRC64; MNKAKRLEIL TRLRENNPHP TTELNFSSPF ELLIAVLLSA QATDVSVNKA TAKLYPVANT PAAMLELGVE GVKTYIKTIG LYNSKAENII KTCRILLEQH NGEVPEDRAA LEALPGVGRK TANVVLNTAF GWPTIAVDTH IFRVCNRTQF APGKNVEQVE EKLLKVVPSE FKVDCHHWLI LHGRYTCIAR KPRCGSCIIE DLCEYKEKVD I //