ID END4_AKKM8 Reviewed; 277 AA. AC B2UQE3; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 29-MAY-2024, entry version 85. DE RecName: Full=Probable endonuclease 4 {ECO:0000255|HAMAP-Rule:MF_00152}; DE EC=3.1.21.2 {ECO:0000255|HAMAP-Rule:MF_00152}; DE AltName: Full=Endodeoxyribonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152}; DE AltName: Full=Endonuclease IV {ECO:0000255|HAMAP-Rule:MF_00152}; GN Name=nfo {ECO:0000255|HAMAP-Rule:MF_00152}; OrderedLocusNames=Amuc_0845; OS Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC OS 81048 / CCUG 64013 / CIP 107961 / Muc). OC Bacteria; Verrucomicrobiota; Verrucomicrobiae; Verrucomicrobiales; OC Akkermansiaceae; Akkermansia. OX NCBI_TaxID=349741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP RC 107961 / Muc; RX PubMed=21390229; DOI=10.1371/journal.pone.0016876; RA van Passel M.W., Kant R., Zoetendal E.G., Plugge C.M., Derrien M., RA Malfatti S.A., Chain P.S., Woyke T., Palva A., de Vos W.M., Smidt H.; RT "The genome of Akkermansia muciniphila, a dedicated intestinal mucin RT degrader, and its use in exploring intestinal metagenomes."; RL PLoS ONE 6:E16876-E16876(2011). CC -!- FUNCTION: Endonuclease IV plays a role in DNA repair. It cleaves CC phosphodiester bonds at apurinic or apyrimidinic (AP) sites, generating CC a 3'-hydroxyl group and a 5'-terminal sugar phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00152}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Endonucleolytic cleavage to 5'-phosphooligonucleotide end- CC products.; EC=3.1.21.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00152}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00152}; CC Note=Binds 3 Zn(2+) ions. {ECO:0000255|HAMAP-Rule:MF_00152}; CC -!- SIMILARITY: Belongs to the AP endonuclease 2 family. CC {ECO:0000255|HAMAP-Rule:MF_00152}. 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; CP001071; ACD04678.1; -; Genomic_DNA. DR RefSeq; WP_012419893.1; NZ_CP071807.1. DR AlphaFoldDB; B2UQE3; -. DR SMR; B2UQE3; -. DR STRING; 349741.Amuc_0845; -. DR PaxDb; 349741-Amuc_0845; -. DR KEGG; amu:Amuc_0845; -. DR eggNOG; COG0648; Bacteria. DR HOGENOM; CLU_025885_4_1_0; -. DR OrthoDB; 9805666at2; -. DR BioCyc; AMUC349741:G1GBX-916-MONOMER; -. DR Proteomes; UP000001031; Chromosome. DR GO; GO:0008833; F:deoxyribonuclease IV (phage-T4-induced) activity; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:TreeGrafter. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:TreeGrafter. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006284; P:base-excision repair; IEA:TreeGrafter. DR CDD; cd00019; AP2Ec; 1. DR Gene3D; 3.20.20.150; Divalent-metal-dependent TIM barrel enzymes; 1. DR HAMAP; MF_00152; Nfo; 1. DR InterPro; IPR001719; AP_endonuc_2. DR InterPro; IPR018246; AP_endonuc_F2_Zn_BS. DR InterPro; IPR036237; Xyl_isomerase-like_sf. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR NCBIfam; TIGR00587; nfo; 1. DR PANTHER; PTHR21445:SF0; APURINIC-APYRIMIDINIC ENDONUCLEASE; 1. DR PANTHER; PTHR21445; ENDONUCLEASE IV ENDODEOXYRIBONUCLEASE IV; 1. DR Pfam; PF01261; AP_endonuc_2; 1. DR SMART; SM00518; AP2Ec; 1. DR SUPFAM; SSF51658; Xylose isomerase-like; 1. DR PROSITE; PS00730; AP_NUCLEASE_F2_2; 1. DR PROSITE; PS51432; AP_NUCLEASE_F2_4; 1. PE 3: Inferred from homology; KW DNA damage; DNA repair; Endonuclease; Hydrolase; Metal-binding; Nuclease; KW Reference proteome; Zinc. FT CHAIN 1..277 FT /note="Probable endonuclease 4" FT /id="PRO_1000096867" FT BINDING 67 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 107 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 142 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 142 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 176 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 179 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 211 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 224 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 226 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" FT BINDING 256 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00152" SQ SEQUENCE 277 AA; 30780 MW; 0AB7EB291259D263 CRC64; MPYIGCHLSS AKGYEAMGRV ALSIGANTFQ FFTRNPRGSK AKAIDEQDIA RFLELARNNG FGTLLAHAPY TLNPCSADPS VARFAAQVLK EDLELMEHLP GNLYNFHPGC HVGQGVEKGI ELVADQLNDV LSPEQKTIVL LETMSGKGSE VGRTFEELAA IMERVDLKDK LGVCLDTCHV YSAGYDIVNR LDSVLEHFDA VLGLERLRAI HLNDSMTPFS SFKDRHETIG KGSLGEQAFI NIINHPVLRE LPFFLETPRD DAGHGEEITW LKEHYRN //