ID FPG_SYMTH Reviewed; 305 AA. AC Q67R59; DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 118. DE RecName: Full=Formamidopyrimidine-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00103}; DE Short=Fapy-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00103}; DE EC=3.2.2.23 {ECO:0000255|HAMAP-Rule:MF_00103}; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM {ECO:0000255|HAMAP-Rule:MF_00103}; DE Short=AP lyase MutM {ECO:0000255|HAMAP-Rule:MF_00103}; DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00103}; GN Name=mutM {ECO:0000255|HAMAP-Rule:MF_00103}; GN Synonyms=fpg {ECO:0000255|HAMAP-Rule:MF_00103}; GN OrderedLocusNames=STH849; OS Symbiobacterium thermophilum (strain T / IAM 14863). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae; OC Symbiobacterium. OX NCBI_TaxID=292459; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=T / IAM 14863; RX PubMed=15383646; DOI=10.1093/nar/gkh830; RA Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K., RA Ikeda H., Hattori M., Beppu T.; RT "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium RT that depends on microbial commensalism."; RL Nucleic Acids Res. 32:4937-4944(2004). CC -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation CC or by mutagenic agents. Acts as a DNA glycosylase that recognizes and CC removes damaged bases. Has a preference for oxidized purines, such as CC 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase CC activity and introduces nicks in the DNA strand. Cleaves the DNA CC backbone by beta-delta elimination to generate a single-strand break at CC the site of the removed base with both 3'- and 5'-phosphates. CC {ECO:0000255|HAMAP-Rule:MF_00103}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine CC residues, releasing 2,6-diamino-4-hydroxy-5-(N- CC methyl)formamidopyrimidine.; EC=3.2.2.23; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00103}; 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:0000255|HAMAP- CC Rule:MF_00103}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00103}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00103}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00103}. CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|HAMAP- CC Rule:MF_00103}. 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; AP006840; BAD39834.1; -; Genomic_DNA. DR RefSeq; WP_011194981.1; NC_006177.1. DR AlphaFoldDB; Q67R59; -. DR SMR; Q67R59; -. DR STRING; 292459.STH849; -. DR KEGG; sth:STH849; -. DR eggNOG; COG0266; Bacteria. DR HOGENOM; CLU_038423_1_2_9; -. DR OrthoDB; 9800855at2; -. DR Proteomes; UP000000417; Chromosome. DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR CDD; cd08966; EcFpg-like_N; 1. DR Gene3D; 1.10.8.50; -; 1. DR Gene3D; 3.20.190.10; MutM-like, N-terminal; 1. DR HAMAP; MF_00103; Fapy_DNA_glycosyl; 1. DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd. DR InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS. DR InterPro; IPR020629; Formamido-pyr_DNA_Glyclase. DR InterPro; IPR012319; FPG_cat. DR InterPro; IPR035937; MutM-like_N-ter. DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH. DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase. DR InterPro; IPR010663; Znf_FPG/IleRS. DR NCBIfam; TIGR00577; fpg; 1. DR PANTHER; PTHR22993:SF9; ENDONUCLEASE 8-LIKE 1; 1. DR PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1. DR Pfam; PF01149; Fapy_DNA_glyco; 1. DR Pfam; PF06831; H2TH; 1. DR Pfam; PF06827; zf-FPG_IleRS; 1. DR SMART; SM00898; Fapy_DNA_glyco; 1. DR SMART; SM01232; H2TH; 1. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF81624; N-terminal domain of MutM-like DNA repair proteins; 1. DR SUPFAM; SSF46946; S13-like H2TH domain; 1. DR PROSITE; PS51068; FPG_CAT; 1. DR PROSITE; PS01242; ZF_FPG_1; 1. DR PROSITE; PS51066; ZF_FPG_2; 1. PE 3: Inferred from homology; KW DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase; KW Metal-binding; Multifunctional enzyme; Reference proteome; Zinc; KW Zinc-finger. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..305 FT /note="Formamidopyrimidine-DNA glycosylase" FT /id="PRO_0000228477" FT ZN_FING 239..273 FT /note="FPG-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT REGION 282..305 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 2 FT /note="Schiff-base intermediate with DNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT ACT_SITE 3 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT ACT_SITE 59 FT /note="Proton donor; for beta-elimination activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT ACT_SITE 263 FT /note="Proton donor; for delta-elimination activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT BINDING 92 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT BINDING 111 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT BINDING 154 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" SQ SEQUENCE 305 AA; 33684 MW; B47EDEC0828DB164 CRC64; MPELPEVETV RRTLCPRVVG RRIRRVEILT PRQIYHPDPA TFAADLEGAV FDDIERRGKY LLFRLGPRIL VAHLRMSGHL YVCGPEAPRP RHLHVVFHLD DGGELRYADQ RKFGGFHLLG PGGEGMPPGL ANLGPEPLSP EFTPQVLAER LAGRHTSIKA ALLNQALVAG LGNIYADEAL FCARIHPARE AGSLTPAEVE RLHGCIRRVL LRAVERRGTT FSLYRDGEGN EGDMYDELQV FDRAGEPCPV CGTPIRKVAV AQRGTHFCPR CQPVPEGVAL SPRRARPGRR GNSVRVAAEP PGTYE //