FPG_MIMIV
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 29-SEP-2021, entry version 74.
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; Mimivirus.
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}.
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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 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 Gene3D; 3.20.190.10; -; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR012319; FPG_cat.
DR InterPro; IPR035937; MutM-like_N-ter.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR Pfam; PF01149; Fapy_DNA_glyco; 1.
DR Pfam; PF06831; H2TH; 1.
DR SMART; SM00898; Fapy_DNA_glyco; 1.
DR SMART; SM01232; H2TH; 1.
DR SUPFAM; SSF46946; SSF46946; 1.
DR SUPFAM; SSF81624; SSF81624; 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
