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Database: UniProt
Entry: A9MAB2
LinkDB: A9MAB2
Original site: A9MAB2 
ID   FPG_BRUC2               Reviewed;         293 AA.
AC   A9MAB2;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   01-OCT-2014, entry version 45.
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=BCAN_A2225;
OS   Brucella canis (strain ATCC 23365 / NCTC 10854).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=483179;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23365 / NCTC 10854;
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J.,
RA   Dharmanolla C., Gillespie J.J., Kenyon R.W., Lu J., Mane S.,
RA   Mohapatra S., Nagrani S., Purkayastha A., Rajasimha H.K.,
RA   Shallom J.M., Shallom S., Shukla M., Snyder E.E., Sobral B.W.,
RA   Wattam A.R., Will R., Williams K., Yoo H., Bruce D., Detter C.,
RA   Munk C., Brettin T.S.;
RT   "Brucella canis ATCC 23365 whole genome shotgun sequencing project.";
RL   Submitted (OCT-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; CP000872; ABX63207.1; -; Genomic_DNA.
DR   RefSeq; YP_001593978.1; NC_010103.1.
DR   ProteinModelPortal; A9MAB2; -.
DR   STRING; 483179.BCAN_A2225; -.
DR   EnsemblBacteria; ABX63207; ABX63207; BCAN_A2225.
DR   GeneID; 5785374; -.
DR   KEGG; bcs:BCAN_A2225; -.
DR   PATRIC; 17833188; VBIBruCan25663_2220.
DR   eggNOG; COG0266; -.
DR   HOGENOM; HOG000020881; -.
DR   KO; K10563; -.
DR   OMA; IYCSESL; -.
DR   OrthoDB; EOG6QP131; -.
DR   BioCyc; BCAN483179:GJ7I-2205-MONOMER; -.
DR   PRO; PR:A9MAB2; -.
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    293       Formamidopyrimidine-DNA glycosylase.
FT                                /FTId=PRO_1000075693.
FT   ZN_FING     257    293       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    283    283       Proton donor; for delta-elimination
FT                                activity. {ECO:0000255|HAMAP-
FT                                Rule:MF_00103}.
FT   BINDING     104    104       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
FT   BINDING     127    127       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
FT   BINDING     170    170       DNA. {ECO:0000255|HAMAP-Rule:MF_00103}.
SQ   SEQUENCE   293 AA;  32007 MW;  31E7063C68DCEB65 CRC64;
     MPELPEVETV RRGLQPFMEG ATVVRVEQNR PDLRFAFPEN FAERLSGRRI EALGRRAKYL
     TVHLDDGLSI ISHLGMSGSF RIEAEDAQGL PGGFHHERSK NSLHDHVVFH LMRPDGASAR
     IIYNDPRRFG FMLFAEKGAL EEHPLLKDLG VEPTGNLLSG EVLAALFKGR RKPLKAALLD
     QRLIAGLGNI YVCEALWRAG LSPMRAAGSV AGEMDVMERL AGAIRSVIAQ AIAAGGSSLK
     DYIQADGALG YFQHSFSVYG REGKPCRNPA CGGTVERVVQ SGRSTFFCAS CQT
//
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