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Database: UniProt
Entry: B2J5G0
LinkDB: B2J5G0
Original site: B2J5G0 
ID   FPG_NOSP7               Reviewed;         291 AA.
AC   B2J5G0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   09-JUL-2014, entry version 43.
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=Npun_R3936;
OS   Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=63737;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29133 / PCC 73102;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Meeks J.C., Elhai J., Campbell E.L., Thiel T., Longmire J., Potts M.,
RA   Atlas R.;
RT   "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133.";
RL   Submitted (APR-2008) 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 (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; CP001037; ACC82317.1; -; Genomic_DNA.
DR   RefSeq; YP_001867260.1; NC_010628.1.
DR   STRING; 63737.Npun_R3936; -.
DR   EnsemblBacteria; ACC82317; ACC82317; Npun_R3936.
DR   GeneID; 6253282; -.
DR   KEGG; npu:Npun_R3936; -.
DR   PATRIC; 22760916; VBINosPun48114_4617.
DR   eggNOG; COG0266; -.
DR   HOGENOM; HOG000020884; -.
DR   KO; K10563; -.
DR   OMA; ISHLRMN; -.
DR   OrthoDB; EOG6QP131; -.
DR   PhylomeDB; B2J5G0; -.
DR   BioCyc; NPUN63737:GJNP-3806-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 (By similarity).
FT   CHAIN         2    291       Formamidopyrimidine-DNA glycosylase.
FT                                /FTId=PRO_1000094058.
FT   ZN_FING     246    280       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    270    270       Proton donor; for delta-elimination
FT                                activity (By similarity).
FT   BINDING      97     97       DNA (By similarity).
FT   BINDING     116    116       DNA (By similarity).
FT   BINDING     161    161       DNA (By similarity).
SQ   SEQUENCE   291 AA;  32664 MW;  130916708BDA286A CRC64;
     MPELPEVETV RKGLNQLTLN QEITGGDVLL NRTIAYPFSV GEFVDGIEKN AIATWHRRGK
     YLLAELSSPC STSWLGVHLR MTGQLLWLHR DEPLHKHTRV RLFFGDQQEL RFVDQRTFGK
     IWWVPPGVAV ESIITGLAKL AADPFSPEFS VEYLASKLKN RRRPIKTALL DQSVVAGLGN
     IYADEALFKS GILPETLCID LQLKQIELLR TAIIQVLETS IEAGGTTFSN FLNVKGTNGN
     YGGVAWVYNR AGEPCRVCGM PIQRIRLAGR SSHFCSECQT LRGVENRERR D
//
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