ID FPG_TRIV2 Reviewed; 277 AA. AC Q3MDP1; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2005, sequence version 1. DT 10-JUN-2026, entry version 116. 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=Ava_1271; OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales; OC Nostocaceae; Trichormus. OX NCBI_TaxID=240292; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29413 / PCC 7937; RX PubMed=25197444; DOI=10.4056/sigs.3899418; RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C., RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.; RT "Complete genome sequence of Anabaena variabilis ATCC 29413."; RL Stand. Genomic Sci. 9:562-573(2014). 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'-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: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; CP000117; ABA20895.1; -; Genomic_DNA. DR RefSeq; WP_011318111.1; NC_007413.1. DR AlphaFoldDB; Q3MDP1; -. DR SMR; Q3MDP1; -. DR STRING; 240292.Ava_1271; -. DR GeneID; 58723939; -. DR KEGG; ava:Ava_1271; -. DR eggNOG; COG0266; Bacteria. DR HOGENOM; CLU_038423_1_2_3; -. DR Proteomes; UP000002533; Chromosome. DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IEA:TreeGrafter. 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:0003690; F:double-stranded DNA binding; IEA:UniProtKB-ARBA. 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 FunFam; 1.10.8.50:FF:000003; Formamidopyrimidine-DNA glycosylase; 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; IPR015887; DNA_glyclase_Znf_dom_DNA_BS. DR InterPro; IPR012319; FPG_cat. DR InterPro; IPR020629; FPG_Glyclase. DR InterPro; IPR035937; FPG_N. DR InterPro; IPR015886; H2TH_FPG. 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 NCBIfam; NF002211; PRK01103.1; 1. DR NCBIfam; NF010551; PRK13945.1; 1. DR PANTHER; PTHR22993; FORMAMIDOPYRIMIDINE-DNA GLYCOSYLASE; 1. DR PANTHER; PTHR22993:SF9; 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..277 FT /note="Formamidopyrimidine-DNA glycosylase" FT /id="PRO_1000008674" FT ZN_FING 243..277 FT /note="FPG-type" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" 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 60 FT /note="Proton donor; for beta-elimination activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT ACT_SITE 267 FT /note="Proton donor; for delta-elimination activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT BINDING 94 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT BINDING 113 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" FT BINDING 158 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00103" SQ SEQUENCE 277 AA; 30933 MW; 3D67C43773CD2D78 CRC64; MPELPEVETV RRGLNQLTLN RKITGGDVLL HRTIAHPFSV GDFLNGITGD SISAWHRRGK YLLASTTSAA WLGVHLRMTG QLLWLNQDEP LHKHTRVRIF FEDQQELRFV DQRTFGQMWW VSSGMAVESV ITGLAKLAVD PFSPEFTVEY LANKLHNRRR PIKTALLDQS VVAGLGNIYA DEALFKSGVL PETLCTEVQL KQIELLRTAI IQVLETSIEA GGTTFSNFLN VKGVNGNYGG VAWVYNRAGE PCKVCGDVIQ RIKLGGRSSH FCRQCQV //