FPG_THET8
ID FPG_THET8 Reviewed; 267 AA.
AC O50606; Q5SHC4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 151.
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=TTHA1806;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=9461446; DOI=10.1093/nar/26.4.903;
RA Mikawa T., Kato R., Sugahara M., Kuramitsu S.;
RT "Thermostable repair enzyme for oxidative DNA damage from extremely
RT thermophilic bacterium, Thermus thermophilus HB8.";
RL Nucleic Acids Res. 26:903-910(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=10921868; DOI=10.1093/emboj/19.15.3857;
RA Sugahara M., Mikawa T., Kumasaka T., Yamamoto M., Kato R., Fukuyama K.,
RA Inoue Y., Kuramitsu S.;
RT "Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM
RT (Fpg), from an extreme thermophile, Thermus thermophilus HB8.";
RL EMBO J. 19:3857-3869(2000).
CC -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation
CC or by mutagenic agents. Acts as 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;
CC Note=Binds 1 zinc ion per subunit.;
CC -!- SUBUNIT: Monomer.
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000305}.
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DR EMBL; AB008520; BAA24892.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD71629.1; -; Genomic_DNA.
DR RefSeq; WP_011173830.1; NC_006461.1.
DR RefSeq; YP_145072.1; NC_006461.1.
DR PDB; 1EE8; X-ray; 1.90 A; A/B=2-267.
DR PDBsum; 1EE8; -.
DR AlphaFoldDB; O50606; -.
DR SMR; O50606; -.
DR STRING; 300852.55773188; -.
DR PRIDE; O50606; -.
DR EnsemblBacteria; BAD71629; BAD71629; BAD71629.
DR GeneID; 3169771; -.
DR KEGG; ttj:TTHA1806; -.
DR PATRIC; fig|300852.9.peg.1777; -.
DR eggNOG; COG0266; Bacteria.
DR HOGENOM; CLU_038423_1_2_0; -.
DR OMA; GVHLRMT; -.
DR PhylomeDB; O50606; -.
DR BRENDA; 3.2.2.23; 2305.
DR EvolutionaryTrace; O50606; -.
DR Proteomes; UP000000532; 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 Gene3D; 3.20.190.10; -; 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_S13-like_H2TH.
DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR InterPro; IPR010663; Znf_FPG/IleRS.
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; SSF46946; SSF46946; 1.
DR SUPFAM; SSF81624; SSF81624; 1.
DR TIGRFAMs; TIGR00577; fpg; 1.
DR PROSITE; PS51068; FPG_CAT; 1.
DR PROSITE; PS01242; ZF_FPG_1; 1.
DR PROSITE; PS51066; ZF_FPG_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase;
KW Lyase; Metal-binding; Multifunctional enzyme; Reference proteome; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..267
FT /note="Formamidopyrimidine-DNA glycosylase"
FT /id="PRO_0000170880"
FT ZN_FING 230..264
FT /note="FPG-type"
FT ACT_SITE 2
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000305"
FT ACT_SITE 3
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT ACT_SITE 53
FT /note="Proton donor; for beta-elimination activity"
FT /evidence="ECO:0000305"
FT ACT_SITE 254
FT /note="Proton donor; for delta-elimination activity"
FT /evidence="ECO:0000305"
FT BINDING 82
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:1EE8"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:1EE8"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:1EE8"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1EE8"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1EE8"
FT STRAND 43..51
FT /evidence="ECO:0007829|PDB:1EE8"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1EE8"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1EE8"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:1EE8"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:1EE8"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1EE8"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:1EE8"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:1EE8"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1EE8"
FT HELIX 118..121
FT /evidence="ECO:0007829|PDB:1EE8"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:1EE8"
FT HELIX 147..153
FT /evidence="ECO:0007829|PDB:1EE8"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:1EE8"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:1EE8"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1EE8"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1EE8"
FT HELIX 185..204
FT /evidence="ECO:0007829|PDB:1EE8"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:1EE8"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:1EE8"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:1EE8"
FT STRAND 255..258
FT /evidence="ECO:0007829|PDB:1EE8"
FT TURN 260..264
FT /evidence="ECO:0007829|PDB:1EE8"
SQ SEQUENCE 267 AA; 29915 MW; CDEAEAB2BED893EA CRC64;
MPELPEVETT RRRLRPLVLG QTLRQVVHRD PARYRNTALA EGRRILEVDR RGKFLLFALE
GGVELVAHLG MTGGFRLEPT PHTRAALVLE GRTLYFHDPR RFGRLFGVRR GDYREIPLLL
RLGPEPLSEA FAFPGFFRGL KESARPLKAL LLDQRLAAGV GNIYADEALF RARLSPFRPA
RSLTEEEARR LYRALREVLA EAVELGGSTL SDQSYRQPDG LPGGFQTRHA VYGREGLPCP
ACGRPVERRV VAGRGTHFCP TCQGEGP
