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Database: UniProt
Entry: Q4QLW2
LinkDB: Q4QLW2
Original site: Q4QLW2 
ID   FPG_HAEI8               Reviewed;         271 AA.
AC   Q4QLW2;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   14-MAY-2014, entry version 66.
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=NTHI1118;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP;
RX   PubMed=15968074; DOI=10.1128/JB.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable
RT   Haemophilus influenzae: comparative study with H. influenzae serotype
RT   d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(2005).
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; CP000057; AAX87985.1; -; Genomic_DNA.
DR   RefSeq; YP_248645.1; NC_007146.2.
DR   ProteinModelPortal; Q4QLW2; -.
DR   SMR; Q4QLW2; 2-269.
DR   STRING; 281310.NTHI1118; -.
DR   EnsemblBacteria; AAX87985; AAX87985; NTHI1118.
DR   GeneID; 3430410; -.
DR   KEGG; hit:NTHI1118; -.
DR   PATRIC; 20182393; VBIHaeInf100748_1040.
DR   eggNOG; COG0266; -.
DR   HOGENOM; HOG000020881; -.
DR   KO; K10563; -.
DR   OMA; DHVDLKL; -.
DR   OrthoDB; EOG6QP131; -.
DR   BioCyc; HINF281310:GJ89-1062-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    271       Formamidopyrimidine-DNA glycosylase.
FT                                /FTId=PRO_0000228438.
FT   ZN_FING     235    269       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     57     57       Proton donor; for beta-elimination
FT                                activity (By similarity).
FT   ACT_SITE    259    259       Proton donor; for delta-elimination
FT                                activity (By similarity).
FT   BINDING      90     90       DNA (By similarity).
FT   BINDING     109    109       DNA (By similarity).
FT   BINDING     150    150       DNA (By similarity).
SQ   SEQUENCE   271 AA;  30742 MW;  F70B51EEC7A81557 CRC64;
     MPELPEVETA LRGISPYLKN FTIEKVVVRK PKLRWAVSEE LITLKNVKIV DLTRRAKYLI
     IHTEKGYIIG HLGMSGSVRI VPQDSAIDKH DHIDIVVNNG KLLRYNDPRR FGAWLWTENL
     DDFHLFLKLG PEPLSDEFNA EYLFKKSRQK STALKTFLMD NAVVVGVGNI YANESLFICG
     IHPLKLAKNL TRNQCFSLVN TIKDVLRKAI IQGGTTLKDF LQPDGRPGYF AQELLVYGNK
     DKPCPKCGGK IESLIIGQRN SFFCPKCQKR G
//
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