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Database: UniProt
Entry: A8GTA0
LinkDB: A8GTA0
Original site: A8GTA0 
ID   FPG_RICRS               Reviewed;         273 AA.
AC   A8GTA0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   01-OCT-2014, entry version 44.
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=A1G_05740;
OS   Rickettsia rickettsii (strain Sheila Smith).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=392021;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sheila Smith;
RA   Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Dasch G., Eremeeva M.;
RT   "Complete genome sequence of Rickettsia rickettsii.";
RL   Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in base excision repair of DNA damaged by
CC       oxidation or by mutagenic agents. Acts as DNA glycosylase that
CC       recognizes and removes damaged bases. Has a preference for
CC       oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has
CC       AP (apurinic/apyrimidinic) lyase activity and introduces nicks in
CC       the DNA strand. Cleaves the DNA backbone by beta-delta elimination
CC       to generate a single-strand break at the site of the removed base
CC       with both 3'- and 5'-phosphates. {ECO:0000255|HAMAP-
CC       Rule:MF_00103}.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7-
CC       methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC       methyl)formamidopyrimidine. {ECO:0000255|HAMAP-Rule:MF_00103}.
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate. {ECO:0000255|HAMAP-Rule:MF_00103}.
CC   -!- COFACTOR: Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       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   -!- SIMILARITY: Contains 1 FPG-type zinc finger. {ECO:0000255|HAMAP-
CC       Rule:MF_00103}.
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DR   EMBL; CP000848; ABV76625.1; -; Genomic_DNA.
DR   RefSeq; YP_001495133.1; NC_009882.1.
DR   ProteinModelPortal; A8GTA0; -.
DR   STRING; 392021.A1G_05740; -.
DR   EnsemblBacteria; ABV76625; ABV76625; A1G_05740.
DR   GeneID; 5647625; -.
DR   KEGG; rri:A1G_05740; -.
DR   PATRIC; 17905131; VBIRicRic5337_1209.
DR   eggNOG; COG0266; -.
DR   HOGENOM; HOG000020881; -.
DR   KO; K10563; -.
DR   OMA; GAHDHFE; -.
DR   OrthoDB; EOG6QP131; -.
DR   BioCyc; RRIC392021:GIY1-1057-MONOMER; -.
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-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
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; IPR000191; DNA_glycosylase/AP_lyase.
DR   InterPro; IPR012319; DNA_glycosylase/AP_lyase_cat.
DR   InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_DNA_glyclase/IsotRNA_synth.
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   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   3: Inferred from homology;
KW   Complete proteome; DNA damage; DNA repair; DNA-binding; Glycosidase;
KW   Hydrolase; Lyase; Metal-binding; Multifunctional enzyme; Zinc;
KW   Zinc-finger.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    273       Formamidopyrimidine-DNA glycosylase.
FT                                /FTId=PRO_1000008763.
FT   ZN_FING     238    272       FPG-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_00103}.
FT   ACT_SITE      2      2       Schiff-base intermediate with DNA.
FT                                {ECO:0000255|HAMAP-Rule:MF_00103}.
FT   ACT_SITE      3      3       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00103}.
FT   ACT_SITE     58     58       Proton donor; for beta-elimination
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_00103}.
FT   ACT_SITE    262    262       Proton donor; for delta-elimination
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_00103}.
FT   BINDING      92     92       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
FT   BINDING     111    111       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
FT   BINDING     153    153       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
SQ   SEQUENCE   273 AA;  31247 MW;  B67CE0618626C807 CRC64;
     MPELPEVETL KNSLKDKLIG LIIENVELKR DNLRYKLSPL LATEILNTNI LDVRRRAKYL
     IIDFNNDYSL IVHLGMSGRF TLQSANYKTQ KHDHVIFDLS NGEKLIFNDT RRFGMIYSFK
     TDLLEKEFFN DLGIEPFSDL LTLEYLKDKL QTKKIPIKNL IMDNRVIVGV GNIYASESLH
     LARIHPDKSG NDLRDDEIEN LIKAIRDVLT KAITAGGTTL KDFVNGDNKP GYFTKQLKVY
     GREGQSCLSC SSTIIKIKHS GRSTFYCKTC QYS
//
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