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Database: UniProt
Entry: A1UED7
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ID   FPG_MYCSK               Reviewed;         296 AA.
AC   A1UED7;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   19-FEB-2014, entry version 53.
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=Mkms_1996;
OS   Mycobacterium sp. (strain KMS).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=189918;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Miller C.D., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL   Submitted (DEC-2006) 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; CP000518; ABL91195.1; -; Genomic_DNA.
DR   RefSeq; YP_937985.1; NC_008705.1.
DR   STRING; 189918.Mkms_1996; -.
DR   EnsemblBacteria; ABL91195; ABL91195; Mkms_1996.
DR   GeneID; 4613562; -.
DR   KEGG; mkm:Mkms_1996; -.
DR   PATRIC; 18102910; VBIMycSp70743_2497.
DR   eggNOG; COG0266; -.
DR   HOGENOM; HOG000020884; -.
DR   KO; K10563; -.
DR   OMA; RREKFMN; -.
DR   OrthoDB; EOG6QP131; -.
DR   ProtClustDB; PRK01103; -.
DR   BioCyc; MSP189918:GH4X-2009-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    296       Formamidopyrimidine-DNA glycosylase.
FT                                /FTId=PRO_1000008721.
FT   ZN_FING     255    289       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     61     61       Proton donor; for beta-elimination
FT                                activity (By similarity).
FT   ACT_SITE    279    279       Proton donor; for delta-elimination
FT                                activity (By similarity).
FT   BINDING     104    104       DNA (By similarity).
FT   BINDING     123    123       DNA (By similarity).
FT   BINDING     169    169       DNA (By similarity).
SQ   SEQUENCE   296 AA;  32719 MW;  365210B62DFEA922 CRC64;
     MPELPEVEVV RRGLDAHVTG KAITAVRVHH PRAVRRHEAG PADLTARLLG MRITGTGRRG
     KYLWLTLDDG DEPLARRAES SVALVVHLGM SGQMLLGPIP KEDHLRIAAL FDDGTALSFV
     DQRTFGGWLL ADLVTVDGTD VPVPVAHVAR DPLDPRFDRD AVVKVLRGKH SEIKRQLLDQ
     TVVSGIGNIY ADEALWRAKV NGARLAESLT KPKLAEILDH AADVMRDALG QGGTSFDSLY
     VNVNGESGYF DRSLDAYGRE GEPCRRCGAI MRRDKFMNRS SFYCPRCQPR PRVRRA
//
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