ID F4A1P4_MAHA5 Unreviewed; 213 AA. AC F4A1P4; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAR-2024, entry version 65. 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=Mahau_1918 {ECO:0000313|EMBL:AEE97094.1}; OS Mahella australiensis (strain DSM 15567 / CIP 107919 / 50-1 BON). OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacterales Family IV. Incertae Sedis; Mahella. OX NCBI_TaxID=697281 {ECO:0000313|EMBL:AEE97094.1, ECO:0000313|Proteomes:UP000008457}; RN [1] {ECO:0000313|Proteomes:UP000008457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15567 / CIP 107919 / 50-1 BON RC {ECO:0000313|Proteomes:UP000008457}; RG US DOE Joint Genome Institute (JGI-PGF); RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S., RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Teshima H., Brettin T., RA Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V., RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Pukall R., RA Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.; RT "The complete genome of Mahella australiensis DSM 15567."; RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AEE97094.1, ECO:0000313|Proteomes:UP000008457} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 15567 / CIP 107919 / 50-1 BON RC {ECO:0000313|Proteomes:UP000008457}; RX PubMed=21886860; RA Sikorski J., Teshima H., Nolan M., Lucas S., Hammon N., Deshpande S., RA Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Huntemann M., RA Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L., RA Chen A., Palaniappan K., Land M., Hauser L., Ngatchou-Djao O.D., Rohde M., RA Pukall R., Spring S., Abt B., Goker M., Detter J.C., Woyke T., Bristow J., RA Markowitz V., Hugenholtz P., Eisen J.A., Kyrpides N.C., Klenk H.P., RA Lapidus A.; RT "Complete genome sequence of Mahella australiensis type strain (50-1 RT BON)."; RL Stand. Genomic Sci. 4:331-341(2011). 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; CP002360; AEE97094.1; -; Genomic_DNA. DR RefSeq; WP_013781522.1; NC_015520.1. DR AlphaFoldDB; F4A1P4; -. DR STRING; 697281.Mahau_1918; -. DR KEGG; mas:Mahau_1918; -. DR eggNOG; COG0177; Bacteria. DR HOGENOM; CLU_012862_3_3_9; -. DR OrthoDB; 9800977at2; -. DR Proteomes; UP000008457; 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; PF00633; HHH; 1. DR Pfam; PF00730; HhH-GPD; 1. DR PIRSF; PIRSF001435; Nth; 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:AEE97094.1}; 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:AEE97094.1}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00942}; Nuclease {ECO:0000313|EMBL:AEE97094.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008457}. FT DOMAIN 39..186 FT /note="HhH-GPD" FT /evidence="ECO:0000259|SMART:SM00478" FT BINDING 188 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT BINDING 195 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT BINDING 198 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" FT BINDING 204 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00942" SQ SEQUENCE 213 AA; 23988 MW; 0D3885B3ECF4E51E CRC64; MKTRDDIEHI LDILADCYPQ AKTALVYSNA FELLIATILS AQSTDKQVNK VTGKLFGKYK TPEDFAALEP QTLEEEIKSC GLYRTKALNI INMSKILVER YGSQVPSDPD ELQKLPGVGR KTANVVVSNA FGRPAIAVDT HVFRVTHRLG LAKSSTPLGT EKELMACIPR VLWSQAHHWF IYHGRNVCRA RQPKCDECRL RQYCDFYNSE AGL //