ID B2IC70_BEII9 Unreviewed; 252 AA. AC B2IC70; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 27-MAR-2024, entry version 88. 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 OrderedLocusNames=Bind_3106 {ECO:0000313|EMBL:ACB96667.1}; OS Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIMB OS 8712). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Beijerinckiaceae; Beijerinckia. OX NCBI_TaxID=395963 {ECO:0000313|EMBL:ACB96667.1, ECO:0000313|Proteomes:UP000001695}; RN [1] {ECO:0000313|Proteomes:UP000001695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712 RC {ECO:0000313|Proteomes:UP000001695}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., LaButti K., Schmutz J., Larimer F., RA Land M., Hauser L., Kyrpides N., Mikhailova N., Dunfield P.F., Dedysh S.N., RA Liesack W., Saw J.H., Alam M., Chen Y., Murrell J.C., Richardson P.; RT "Complete sequence of chromosome of Beijerinckia indica subsp. indica ATCC RT 9039."; RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACB96667.1, ECO:0000313|Proteomes:UP000001695} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9039 / DSM 1715 / NCIMB 8712 RC {ECO:0000313|Proteomes:UP000001695}; RX PubMed=20601475; DOI=10.1128/JB.00656-10; RA Tamas I., Dedysh S.N., Liesack W., Stott M.B., Alam M., Murrell J.C., RA Dunfield P.F.; RT "Complete genome sequence of Beijerinckia indica subsp. indica."; RL J. Bacteriol. 192:4532-4533(2010). 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; CP001016; ACB96667.1; -; Genomic_DNA. DR AlphaFoldDB; B2IC70; -. DR STRING; 395963.Bind_3106; -. DR KEGG; bid:Bind_3106; -. DR eggNOG; COG0177; Bacteria. DR HOGENOM; CLU_012862_3_2_5; -. DR OrthoDB; 9800977at2; -. DR Proteomes; UP000001695; 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 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:ACB96667.1}; 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:ACB96667.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00942}; Nuclease {ECO:0000313|EMBL:ACB96667.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001695}. FT DOMAIN 80..227 FT /note="HhH-GPD" FT /evidence="ECO:0000259|SMART:SM00478" FT BINDING 229 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT BINDING 236 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT BINDING 239 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT BINDING 245 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" SQ SEQUENCE 252 AA; 27502 MW; DC44E7E1FD16E44E CRC64; MKEPQTPVSV PPEAALTPIG AAKIRETKIR ASAKTRKAKA KLPDLAEVAE IFRRFAAADP HPEGELYSVN DFTFLIAVVL SAQATDAGVN KATKALFAIA DSPEKMLALG EDKLRDMIKT IGLYQAKAKN IMALCANLIE NYGGQVPHDR EALQSLAGVG RKTANVVLNI AFGEPTIAVD THIFRVSNRI PLAIGKTPLA VEQGLEKIVP PEYKLHAHVW LILHGRHVCK ARRPECERCI ISDLCHSPEK RV //