ID FPG_BACCR Reviewed; 276 AA.
AC Q817G5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 01-MAY-2013, entry version 79.
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=BC_4586;
OS Bacillus cereus (strain ATCC 14579 / DSM 31).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with
RT Bacillus anthracis.";
RL Nature 423:87-91(2003).
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; AE016877; AAP11493.1; -; Genomic_DNA.
DR RefSeq; NP_834292.1; NC_004722.1.
DR ProteinModelPortal; Q817G5; -.
DR SMR; Q817G5; 2-274.
DR STRING; 226900.BC4586; -.
DR EnsemblBacteria; EBBACT00000032088; EBBACP00000031294; EBBACG00000032079.
DR GeneID; 1206931; -.
DR KEGG; bce:BC4586; -.
DR PATRIC; 32605299; VBIBacCer54481_4748.
DR eggNOG; COG0266; -.
DR KO; K10563; -.
DR OMA; VLRYNDP; -.
DR ProtClustDB; PRK01103; -.
DR BioCyc; BCER226900:GJEU-4582-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;
KW Reference proteome; Zinc; Zinc-finger.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 276 Formamidopyrimidine-DNA glycosylase.
FT /FTId=PRO_0000170808.
FT ZN_FING 240 274 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 60 60 Proton donor; for beta-elimination
FT activity (By similarity).
FT ACT_SITE 264 264 Proton donor; for delta-elimination
FT activity (By similarity).
FT BINDING 93 93 DNA (By similarity).
FT BINDING 112 112 DNA (By similarity).
SQ SEQUENCE 276 AA; 31718 MW; 6C9B037A5AE85C39 CRC64;
MPELPEVENV RRTLENLVTG KTIEDVIVTY PKIVKRPDDA EIFKEMLKGE KIENIKRRGK
FLLLYVTNYV IVSHLRMEGK FLLHQEDEPI DKHTHVRFLF TDGTELHYKD VRKFGTMHLF
KKGEEMNQMP LADLGPEPFD AEMTPQYLQE RLQKTNRKIK VVLLDQRLLV GLGNIYVDEV
LFRSQIHPER EASSLTVEEI ERIYEATVTT LGEAVKRGGS TIRTYINSQG QIGSFQELLN
VYGKKGEPCV TCGTILEKTV VGGRGTHYCP ICQPRI
//
