ID FPG_NEIMB Reviewed; 275 AA. AC P55044; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 27-MAR-2024, entry version 155. DE RecName: Full=Formamidopyrimidine-DNA glycosylase; DE Short=Fapy-DNA glycosylase; DE EC=3.2.2.23; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM; DE Short=AP lyase MutM; DE EC=4.2.99.18; GN Name=mutM; Synonyms=fpg; OrderedLocusNames=NMB1295; OS Neisseria meningitidis serogroup B (strain MC58). OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae; OC Neisseria. OX NCBI_TaxID=122586; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8586265; DOI=10.1111/j.1574-6968.1995.tb07933.x; RA Swartley J.S., Stephens D.S.; RT "Co-transcription of a homologue of the formamidopyrimidine-DNA glycosylase RT (fpg) and lysophosphatidic acid acyltransferase (nlaA) in Neisseria RT meningitidis."; RL FEMS Microbiol. Lett. 134:171-176(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MC58; RX PubMed=10710307; DOI=10.1126/science.287.5459.1809; RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M., RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., RA Moxon E.R., Rappuoli R., Venter J.C.; RT "Complete genome sequence of Neisseria meningitidis serogroup B strain RT MC58."; RL Science 287:1809-1815(2000). 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 (By CC similarity). {ECO:0000250}. 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 -!- 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; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000305}. 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; U21808; AAB01505.1; -; Genomic_DNA. DR EMBL; AE002098; AAF41671.1; -; Genomic_DNA. DR PIR; B81099; B81099. DR RefSeq; NP_274315.1; NC_003112.2. DR RefSeq; WP_002225172.1; NC_003112.2. DR AlphaFoldDB; P55044; -. DR SMR; P55044; -. DR STRING; 122586.NMB1295; -. DR PaxDb; 122586-NMB1295; -. DR KEGG; nme:NMB1295; -. DR PATRIC; fig|122586.8.peg.1621; -. DR HOGENOM; CLU_038423_1_1_4; -. DR InParanoid; P55044; -. DR OrthoDB; 9800855at2; -. DR Proteomes; UP000000425; Chromosome. DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IBA:GO_Central. 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:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central. 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..275 FT /note="Formamidopyrimidine-DNA glycosylase" FT /id="PRO_0000170843" FT ZN_FING 241..275 FT /note="FPG-type" FT ACT_SITE 2 FT /note="Schiff-base intermediate with DNA" FT /evidence="ECO:0000250" FT ACT_SITE 3 FT /note="Proton donor" FT /evidence="ECO:0000250" FT ACT_SITE 58 FT /note="Proton donor; for beta-elimination activity" FT /evidence="ECO:0000250" FT ACT_SITE 265 FT /note="Proton donor; for delta-elimination activity" FT /evidence="ECO:0000250" FT BINDING 95 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250" FT BINDING 114 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /evidence="ECO:0000250" FT CONFLICT 61..62 FT /note="LI -> IV (in Ref. 1; AAB01505)" FT /evidence="ECO:0000305" FT CONFLICT 66..68 FT /note="TGV -> KGI (in Ref. 1; AAB01505)" FT /evidence="ECO:0000305" FT CONFLICT 151 FT /note="A -> V (in Ref. 1; AAB01505)" FT /evidence="ECO:0000305" FT CONFLICT 213 FT /note="Q -> R (in Ref. 1; AAB01505)" FT /evidence="ECO:0000305" FT CONFLICT 252 FT /note="R -> Q (in Ref. 1; AAB01505)" FT /evidence="ECO:0000305" SQ SEQUENCE 275 AA; 30856 MW; 29A38C945C5EC559 CRC64; MPELPEVETT LRGIAPHIEG KTVEAVVLRQ LKLRWQINPD LGEILSGRQV LSCGRRAKYL LIRFQTGVLL IHLGMSGSLR IFTPSDGRIG RPDRHDHVDI VFSDGTVMRY RDPRKFGAIL WYEGIEEHHP LLEKLGPEPL SEAFCADYLY ARLKAQKRAV KLALMDNAVV VGVGNIYANE SLFRAGISPH RPANRLKKKE CALLVETVKA VLQRAIETGG STLRDFVDSD GKSGYFQQEY TVYGRHNQPC PRCGGLVVKE TLGQRGTFYC PNCQK //