位置:首页 > 蛋白库 > FPG_SALTO
FPG_SALTO
ID   FPG_SALTO               Reviewed;         287 AA.
AC   A4X4F8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Formamidopyrimidine-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00103};
DE            Short=Fapy-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00103};
DE            EC=3.2.2.23 {ECO:0000255|HAMAP-Rule:MF_00103};
DE   AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM {ECO:0000255|HAMAP-Rule:MF_00103};
DE            Short=AP lyase MutM {ECO:0000255|HAMAP-Rule:MF_00103};
DE            EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00103};
GN   Name=mutM {ECO:0000255|HAMAP-Rule:MF_00103};
GN   Synonyms=fpg {ECO:0000255|HAMAP-Rule:MF_00103};
GN   OrderedLocusNames=Strop_1288;
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440).
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Salinispora.
OX   NCBI_TaxID=369723;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440;
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
CC   -!- FUNCTION: Involved in base excision repair of DNA damaged by oxidation
CC       or by mutagenic agents. Acts as DNA glycosylase that recognizes and
CC       removes damaged bases. Has a preference for oxidized purines, such as
CC       7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase
CC       activity and introduces nicks in the DNA strand. Cleaves the DNA
CC       backbone by beta-delta elimination to generate a single-strand break at
CC       the site of the removed base with both 3'- and 5'-phosphates.
CC       {ECO:0000255|HAMAP-Rule:MF_00103}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC         residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC         methyl)formamidopyrimidine.; EC=3.2.2.23;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00103};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC         deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC         dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC         2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC         COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC         ChEBI:CHEBI:167181; EC=4.2.99.18; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00103};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00103};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00103};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00103}.
CC   -!- SIMILARITY: Belongs to the FPG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00103}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000667; ABP53758.1; -; Genomic_DNA.
DR   RefSeq; WP_011905190.1; NC_009380.1.
DR   AlphaFoldDB; A4X4F8; -.
DR   SMR; A4X4F8; -.
DR   STRING; 369723.Strop_1288; -.
DR   EnsemblBacteria; ABP53758; ABP53758; Strop_1288.
DR   KEGG; stp:Strop_1288; -.
DR   PATRIC; fig|369723.5.peg.1312; -.
DR   eggNOG; COG0266; Bacteria.
DR   HOGENOM; CLU_038423_1_2_11; -.
DR   OMA; GVHLRMT; -.
DR   Proteomes; UP000000235; Chromosome.
DR   GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
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-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006284; P:base-excision repair; IEA:InterPro.
DR   Gene3D; 3.20.190.10; -; 1.
DR   HAMAP; MF_00103; Fapy_DNA_glycosyl; 1.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
DR   InterPro; IPR012319; FPG_cat.
DR   InterPro; IPR035937; MutM-like_N-ter.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_FPG/IleRS.
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   SMART; SM01232; H2TH; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   SUPFAM; SSF81624; SSF81624; 1.
DR   TIGRFAMs; TIGR00577; fpg; 1.
DR   PROSITE; PS51068; FPG_CAT; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase;
KW   Metal-binding; Multifunctional enzyme; Reference proteome; Zinc;
KW   Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..287
FT                   /note="Formamidopyrimidine-DNA glycosylase"
FT                   /id="PRO_1000075711"
FT   ZN_FING         243..277
FT                   /note="FPG-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   ACT_SITE        2
FT                   /note="Schiff-base intermediate with DNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   ACT_SITE        3
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   ACT_SITE        61
FT                   /note="Proton donor; for beta-elimination activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   ACT_SITE        267
FT                   /note="Proton donor; for delta-elimination activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   BINDING         95
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   BINDING         115
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
FT   BINDING         157
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00103"
SQ   SEQUENCE   287 AA;  31814 MW;  53426DC341B3BE96 CRC64;
     MPELPEVETV RQGLAQWVTD RRIAEVQVLH PRAVRRHAAG AAHFADVLRE TTVRDVRRRG
     KYLWLPLDSG DAVVGHLGMS GQLLLQPAAA PDETHLRVRF RFADDGPELR FVDQRTFGGL
     SVSAGGAELP TEIAHIARDP LDPEFSDATF VAALRRRRTE IKRALLDQTL LSGVGNIYAD
     EALWRARLHG TRPTDGLTGP AVLRLLGHVR DVLGEAVKEG GTSFDALYVN VNGESGYFDR
     ALNVYGRADQ PCRRCGEPVR REAFMNRSSF SCPRCQPRPR RAVPARG
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024