ID FPG_RICRO Reviewed; 273 AA.
AC B0BUU0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 01-MAY-2013, entry version 40.
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=RrIowa_1236;
OS Rickettsia rickettsii (strain Iowa).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=452659;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Iowa;
RX PubMed=18025092; DOI=10.1128/IAI.00952-07;
RA Ellison D.W., Clark T.R., Sturdevant D.E., Virtaneva K.,
RA Porcella S.F., Hackstadt T.;
RT "Genomic comparison of virulent Rickettsia rickettsii Sheila Smith and
RT avirulent Rickettsia rickettsii Iowa.";
RL Infect. Immun. 76:542-550(2008).
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 (By similarity).
CC -!- CATALYTIC ACTIVITY: Hydrolysis of DNA containing ring-opened 7-
CC methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC methyl)formamidopyrimidine.
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.
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SIMILARITY: Belongs to the FPG family.
CC -!- SIMILARITY: Contains 1 FPG-type zinc finger.
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DR EMBL; CP000766; ABY73000.1; -; Genomic_DNA.
DR RefSeq; YP_001650406.1; NC_010263.2.
DR ProteinModelPortal; B0BUU0; -.
DR STRING; 452659.RrIowa_1236; -.
DR GeneID; 5849766; -.
DR KEGG; rrj:RrIowa_1236; -.
DR PATRIC; 17908389; VBIRicRic59104_1223.
DR eggNOG; COG0266; -.
DR HOGENOM; HOG000020881; -.
DR KO; K10563; -.
DR OMA; FVFSDNS; -.
DR ProtClustDB; PRK01103; -.
DR BioCyc; RRIC452659:GHSN-1152-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:HAMAP.
DR GO; GO:0008270; F:zinc ion binding; IEA: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; SSF81624; Form_DNAglyc_cat; 1.
DR SUPFAM; SSF46946; Ribosomal_H2TH; 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 (By similarity).
FT CHAIN 2 273 Formamidopyrimidine-DNA glycosylase.
FT /FTId=PRO_1000075706.
FT ZN_FING 238 272 FPG-type.
FT ACT_SITE 2 2 Schiff-base intermediate with DNA (By
FT similarity).
FT ACT_SITE 3 3 Proton donor (By similarity).
FT ACT_SITE 58 58 Proton donor; for beta-elimination
FT activity (By similarity).
FT ACT_SITE 262 262 Proton donor; for delta-elimination
FT activity (By similarity).
FT BINDING 92 92 DNA (By similarity).
FT BINDING 111 111 DNA (By similarity).
FT BINDING 153 153 DNA (By similarity).
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
//
