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 29-MAY-2013, entry version 48.
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.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000518; ABL91195.1; -; Genomic_DNA.
DR RefSeq; YP_937985.1; NC_008705.1.
DR STRING; 189918.Mkms_1996; -.
DR EnsemblBacteria; EBMYCT00000058304; EBMYCP00000056528; EBMYCG00000058299.
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 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: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 2 296 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
//
