ID Q0KCI3_CUPNH Unreviewed; 214 AA. AC Q0KCI3; DT 03-OCT-2006, integrated into UniProtKB/TrEMBL. DT 03-OCT-2006, sequence version 1. DT 04-NOV-2026, entry version 124. 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:CAJ92288.1}; GN OrderedLocusNames=H16_A1147 {ECO:0000313|EMBL:CAJ92288.1}; OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 OS / H16 / Stanier 337) (Ralstonia eutropha). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Cupriavidus. OX NCBI_TaxID=381666 {ECO:0000313|EMBL:CAJ92288.1, ECO:0000313|Proteomes:UP000008210}; RN [1] {ECO:0000313|EMBL:CAJ92288.1, ECO:0000313|Proteomes:UP000008210} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier RC 337 {ECO:0000313|Proteomes:UP000008210}; RX PubMed=16964242; DOI=10.1038/nbt1244; RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., RA Eitinger T., Ewering C., Potter M., Schwartz E., Strittmatter A., Voss I., RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.; RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia RT eutropha H16."; RL Nat. Biotechnol. 24:1257-1262(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'-phospho-2'- CC 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; AM260479; CAJ92288.1; -; Genomic_DNA. DR RefSeq; WP_011614905.1; NC_008313.1. DR AlphaFoldDB; Q0KCI3; -. DR STRING; 381666.H16_A1147; -. DR PaxDb; 381666-H16_A1147; -. DR KEGG; reh:H16_A1147; -. DR PATRIC; fig|381666.6.peg.1533; -. DR eggNOG; COG0177; Bacteria. DR HOGENOM; CLU_012862_3_3_4; -. DR OMA; AACEMIV; -. DR OrthoDB; 9800977at2; -. DR Proteomes; UP000008210; Chromosome 1. 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:0006285; P:base-excision repair, AP site formation; IEA:TreeGrafter. DR CDD; cd00056; ENDO3c; 1. DR FunFam; 1.10.1670.10:FF:000001; Endonuclease III; 1. DR FunFam; 1.10.340.30:FF:000001; Endonuclease III; 1. DR Gene3D; 1.10.1670.10; Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal); 1. DR Gene3D; 1.10.340.30; Hypothetical protein, domain 2; 1. DR HAMAP; MF_00942; Nth; 1. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR004036; Endonuclease-III-like_CS2. 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; PF00633; HHH; 1. DR Pfam; PF00730; HhH-GPD; 1. DR PIRSF; PIRSF001435; Nth; 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}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_00942}; Endonuclease {ECO:0000313|EMBL:CAJ92288.1}; 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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00942}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00942}; Nuclease {ECO:0000313|EMBL:CAJ92288.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008210}. FT DOMAIN 38..185 FT /note="HhH-GPD" FT /evidence="ECO:0000259|SMART:SM00478" FT BINDING 187 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT BINDING 194 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT BINDING 197 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT BINDING 203 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" SQ SEQUENCE 214 AA; 23853 MW; 463C3543E9AB36F1 CRC64; MNAAKCRAIF ETLRETNPAP ATELEYSSPF ELLIAVLLSA QATDVGVNKA TRRLFPVAHT PRQMLDLGEA GLSEYIKTIG LYKTKAKHVI ETCRILVERH GGKVPPEREA LEALPGVGRK TANVVLNTAF GEPTIAVDTH IFRVANRTGL APGKTVQIVE QKLLKCVPHE FLHDAHHWLI LHGRYVCKAR KPECWHCVIE PLCEFREKTP APQL //