ID A0A0G4BXC2_NEIME Unreviewed; 256 AA. AC A0A0G4BXC2; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 08-NOV-2023, entry version 24. DE SubName: Full=Exodeoxyribonuclease III {ECO:0000313|EMBL:AKM92108.1}; DE EC=3.1.11.2 {ECO:0000313|EMBL:AKM92108.1}; GN Name=xthA {ECO:0000313|EMBL:AKM92108.1}; GN ORFNames=M0579_00594 {ECO:0000313|EMBL:AKM92108.1}; OS Neisseria meningitidis M0579. OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=935590 {ECO:0000313|EMBL:AKM92108.1, ECO:0000313|Proteomes:UP000035660}; RN [1] {ECO:0000313|EMBL:AKM92108.1, ECO:0000313|Proteomes:UP000035660} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M0579 {ECO:0000313|EMBL:AKM92108.1, RC ECO:0000313|Proteomes:UP000035660}; RX PubMed=25845594; DOI=10.1093/nar/gkv219; RA Seib K.L., Jen F.E., Tan A., Scott A.L., Kumar R., Power P.M., Chen L.T., RA Wu H.J., Wang A.H., Hill D.M., Luyten Y.A., Morgan R.D., Roberts R.J., RA Maiden M.C., Boitano M., Clark T.A., Korlach J., Rao D.N., Jennings M.P.; RT "Specificity of the ModA11, ModA12 and ModD1 epigenetic regulator N6- RT adenine DNA methyltransferases of Neisseria meningitidis."; RL Nucleic Acids Res. 43:4150-4162(2015). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|PIRSR:PIRSR604808-2}; CC Note=Probably binds two magnesium or manganese ions per subunit. CC {ECO:0000256|PIRSR:PIRSR604808-2}; CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family. CC {ECO:0000256|ARBA:ARBA00007092}. 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; CP007668; AKM92108.1; -; Genomic_DNA. DR RefSeq; WP_002218768.1; NZ_CP007668.1. DR AlphaFoldDB; A0A0G4BXC2; -. DR EnsemblBacteria; AKM92108; AKM92108; M0579_00594. DR PATRIC; fig|935590.3.peg.479; -. DR Proteomes; UP000035660; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR CDD; cd09086; ExoIII-like_AP-endo; 1. DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1. DR InterPro; IPR004808; AP_endonuc_1. DR InterPro; IPR020847; AP_endonuclease_F1_BS. DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf. DR InterPro; IPR005135; Endo/exonuclease/phosphatase. DR InterPro; IPR037493; ExoIII-like. DR NCBIfam; TIGR00195; exoDNase_III; 1. DR NCBIfam; TIGR00633; xth; 1. DR PANTHER; PTHR43250; -; 1. DR PANTHER; PTHR43250:SF2; EXODEOXYRIBONUCLEASE III; 1. DR Pfam; PF03372; Exo_endo_phos; 1. DR SUPFAM; SSF56219; DNase I-like; 1. DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1. DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000313|EMBL:AKM92108.1}; KW Magnesium {ECO:0000256|PIRSR:PIRSR604808-2}; KW Manganese {ECO:0000256|PIRSR:PIRSR604808-2}; KW Metal-binding {ECO:0000256|PIRSR:PIRSR604808-2}. FT DOMAIN 5..247 FT /note="Endonuclease/exonuclease/phosphatase" FT /evidence="ECO:0000259|Pfam:PF03372" FT ACT_SITE 105 FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 146 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT ACT_SITE 247 FT /note="Proton acceptor" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-1" FT BINDING 7 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 34 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 146 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 148 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 246 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT BINDING 247 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-2" FT SITE 148 FT /note="Transition state stabilizer" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 217 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" FT SITE 247 FT /note="Interaction with DNA substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR604808-3" SQ SEQUENCE 256 AA; 29117 MW; 3BBA2AD467FBADAB CRC64; MKITTWNVNS LNVRLPQVQN LLADNPPDIL VLQELKLDQD KFPAAALQMM GWHCVWSGQK TYNGVAIVSR NAPEDVHIGL PALPDDPQRR VIAATVGGVR VINVYCVNGE ALDSPKFKYK EQWFAALTEF VRDEMTRYGK LVLLGDFNIA PADADCYDPE KWHEKIHCSS VERQWFKNLL DLGLTDSLRQ VHPEGAFYTW FDYRGAMFQR KLGLRIDHIL VSPAMAAALK DVRVDLETRA LERPSDHAPV TAEFDW //