ID   FPG_ANAVT               Reviewed;         277 AA.
AC   Q3MDP1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=Ava_1271;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) 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; CP000117; ABA20895.1; -; Genomic_DNA.
DR   RefSeq; YP_321790.1; -.
DR   GeneID; 3683170; -.
DR   GenomeReviews; CP000117_GR; Ava_1271.
DR   KEGG; ava:Ava_1271; -.
DR   NMPDR; fig|240292.3.peg.1955; -.
DR   HOGENOM; Q3MDP1; -.
DR   OMA; Q3MDP1; RMTGQLL.
DR   BioCyc; AVAR240292:AVA_1271-MON; -.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0008534; F:oxidized purine base lesion DNA N-glycosyla...; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:InterPro.
DR   HAMAP; MF_00103; -; 1.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR000214; DNA_glyclase/AP_lyase_Znf_dom.
DR   InterPro; IPR010663; DNA_glyclase/IsotRNA_synth_Znf.
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   Pfam; PF01149; Fapy_DNA_glyco; 1.
DR   Pfam; PF06831; H2TH; 1.
DR   Pfam; PF06827; zf-FPG_IleRS; 1.
DR   ProDom; PD003680; Fapy_DNA_glyco; 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    277       Formamidopyrimidine-DNA glycosylase.
FT                                /FTId=PRO_1000008674.
FT   ZN_FING     243    277       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    267    267       Proton donor; for delta-elimination
FT                                activity (By similarity).
FT   BINDING      94     94       DNA (By similarity).
FT   BINDING     113    113       DNA (By similarity).
FT   BINDING     158    158       DNA (By similarity).
SQ   SEQUENCE   277 AA;  30933 MW;  3D67C43773CD2D78 CRC64;
     MPELPEVETV RRGLNQLTLN RKITGGDVLL HRTIAHPFSV GDFLNGITGD SISAWHRRGK
     YLLASTTSAA WLGVHLRMTG QLLWLNQDEP LHKHTRVRIF FEDQQELRFV DQRTFGQMWW
     VSSGMAVESV ITGLAKLAVD PFSPEFTVEY LANKLHNRRR PIKTALLDQS VVAGLGNIYA
     DEALFKSGVL PETLCTEVQL KQIELLRTAI IQVLETSIEA GGTTFSNFLN VKGVNGNYGG
     VAWVYNRAGE PCKVCGDVIQ RIKLGGRSSH FCRQCQV
//