ID FPG_MIMIV Reviewed; 287 AA. AC Q5UQ00; DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 80. DE RecName: Full=Probable formamidopyrimidine-DNA glycosylase; DE Short=Fapy-DNA glycosylase; DE EC=3.2.2.23; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase; DE Short=AP lyase; DE EC=4.2.99.18; GN OrderedLocusNames=MIMI_L315; OS Acanthamoeba polyphaga mimivirus (APMV). OC Viruses; Varidnaviria; Bamfordvirae; Nucleocytoviricota; Megaviricetes; OC Imitervirales; Mimiviridae; Megamimivirinae; Mimivirus; OC Mimivirus bradfordmassiliense. OX NCBI_TaxID=212035; OH NCBI_TaxID=5757; Acanthamoeba polyphaga (Amoeba). RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Rowbotham-Bradford; RX PubMed=15486256; DOI=10.1126/science.1101485; RA Raoult D., Audic S., Robert C., Abergel C., Renesto P., Ogata H., RA La Scola B., Susan M., Claverie J.-M.; RT "The 1.2-megabase genome sequence of Mimivirus."; RL Science 306:1344-1350(2004). 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; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00392}; CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|PROSITE- CC ProRule:PRU00392}. 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; AY653733; AAV50585.1; -; Genomic_DNA. DR RefSeq; YP_003986818.1; NC_014649.1. DR PDB; 3A42; X-ray; 2.60 A; A=1-287. DR PDB; 3A45; X-ray; 2.30 A; A/B=1-287. DR PDB; 3A46; X-ray; 2.20 A; A/B=1-287. DR PDB; 3VK7; X-ray; 2.10 A; A/B=1-287. DR PDB; 3VK8; X-ray; 2.00 A; A/B=1-287. DR PDB; 4NRW; X-ray; 2.84 A; A/B=2-287. DR PDBsum; 3A42; -. DR PDBsum; 3A45; -. DR PDBsum; 3A46; -. DR PDBsum; 3VK7; -. DR PDBsum; 3VK8; -. DR PDBsum; 4NRW; -. DR SMR; Q5UQ00; -. DR GeneID; 9924932; -. DR KEGG; vg:9924932; -. DR OrthoDB; 9330at10239; -. DR EvolutionaryTrace; Q5UQ00; -. DR Proteomes; UP000001134; Genome. 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-EC. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR CDD; cd08773; FpgNei_N; 1. DR Gene3D; 1.10.8.50; -; 1. DR Gene3D; 3.20.190.10; MutM-like, N-terminal; 1. DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd. DR InterPro; IPR049392; FPG_C. DR InterPro; IPR012319; FPG_cat. DR InterPro; IPR035937; MutM-like_N-ter. DR InterPro; IPR010979; Ribosomal_uS13-like_H2TH. 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; PF21025; Fapy_DNA_glyco_C; 1. DR Pfam; PF06831; H2TH; 1. DR SMART; SM00898; Fapy_DNA_glyco; 1. DR SMART; SM01232; H2TH; 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. PE 1: Evidence at protein level; KW 3D-structure; DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; KW Lyase; Multifunctional enzyme; Reference proteome. FT INIT_MET 1 FT /note="Removed; by host" FT /evidence="ECO:0000250" FT CHAIN 2..287 FT /note="Probable formamidopyrimidine-DNA glycosylase" FT /id="PRO_0000170892" FT ACT_SITE 2 FT /note="Schiff-base intermediate with DNA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392" FT ACT_SITE 3 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392" FT ACT_SITE 58 FT /note="Proton donor; for beta-elimination activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392" FT ACT_SITE 277 FT /note="Proton donor; for delta-elimination activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00392" FT HELIX 4..18 FT /evidence="ECO:0007829|PDB:3VK8" FT STRAND 22..28 FT /evidence="ECO:0007829|PDB:3VK8" FT HELIX 32..35 FT /evidence="ECO:0007829|PDB:3VK8" FT HELIX 41..45 FT /evidence="ECO:0007829|PDB:3VK8" FT STRAND 49..58 FT /evidence="ECO:0007829|PDB:3VK8" FT STRAND 61..68 FT /evidence="ECO:0007829|PDB:3VK8" FT STRAND 71..81 FT /evidence="ECO:0007829|PDB:3VK8" FT TURN 83..85 FT /evidence="ECO:0007829|PDB:3VK8" FT STRAND 86..91 FT /evidence="ECO:0007829|PDB:3VK8" FT STRAND 96..102 FT /evidence="ECO:0007829|PDB:3VK8" FT HELIX 103..105 FT /evidence="ECO:0007829|PDB:3VK8" FT STRAND 107..112 FT /evidence="ECO:0007829|PDB:3VK8" FT STRAND 118..123 FT /evidence="ECO:0007829|PDB:3VK8" FT HELIX 125..132 FT /evidence="ECO:0007829|PDB:3VK8" FT TURN 139..141 FT /evidence="ECO:0007829|PDB:3VK8" FT HELIX 147..152 FT /evidence="ECO:0007829|PDB:3VK8" FT HELIX 157..162 FT /evidence="ECO:0007829|PDB:3VK8" FT STRAND 164..167 FT /evidence="ECO:0007829|PDB:3VK8" FT HELIX 173..182 FT /evidence="ECO:0007829|PDB:3VK8" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:3VK8" FT HELIX 196..215 FT /evidence="ECO:0007829|PDB:3VK8" FT STRAND 219..221 FT /evidence="ECO:0007829|PDB:3A46" FT HELIX 223..225 FT /evidence="ECO:0007829|PDB:3VK8" FT HELIX 226..229 FT /evidence="ECO:0007829|PDB:3VK8" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:4NRW" FT STRAND 244..247 FT /evidence="ECO:0007829|PDB:3VK8" FT STRAND 259..261 FT /evidence="ECO:0007829|PDB:3A45" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:3VK8" FT HELIX 273..275 FT /evidence="ECO:0007829|PDB:3A45" FT STRAND 278..281 FT /evidence="ECO:0007829|PDB:3VK8" FT TURN 283..285 FT /evidence="ECO:0007829|PDB:3VK8" SQ SEQUENCE 287 AA; 33463 MW; 745EE3385D9581AB CRC64; MPEGPEVALT ADILEKYFKG KTLEYIDFIS GRYSKSEPEG YDDFIANLPL KVSNVDTKGK FLWFELFDPN DKSNKWYIWN TFGLTGMWSL FEAKYTRAVL SFDNELMAYF SDMRNFGTFK FSNSEKELKR KLNELGPDFL KNDDIDISKI KKYKQPIVAL LMDQKKIGSG LGNYLVAEIL YRAKIDPHKL GSNLTDQEIE NLWYWIKYET KLAYDSNHIG YMVNLENESS KIGRKNYHPN IHPTEKEFDF LVYRKKKDPN GNKVIADKII GSGKNKRTTY WAPAIQK //