位置:首页 > 蛋白库 > FPG_SYNP6
FPG_SYNP6
ID   FPG_SYNP6               Reviewed;         282 AA.
AC   Q08079; Q5N5J8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   03-AUG-2022, entry version 137.
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=syc0230_c;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS   nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT   Synechococcus elongatus PCC 6301 chromosome: gene content and
RT   organization.";
RL   Photosyn. Res. 93:55-67(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
RX   PubMed=8278517; DOI=10.1104/pp.101.2.701;
RA   Rhiel E., Bryant D.A.;
RT   "Nucleotide sequence of the psaE gene of cyanobacterium Synechococcus sp.
RT   PCC 6301.";
RL   Plant Physiol. 101:701-702(1993).
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 (By
CC       similarity). {ECO:0000250}.
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   -!- 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;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FPG family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD78420.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AP008231; BAD78420.1; ALT_INIT; Genomic_DNA.
DR   EMBL; M99432; AAA18569.2; -; Genomic_DNA.
DR   RefSeq; WP_011377983.1; NC_006576.1.
DR   AlphaFoldDB; Q08079; -.
DR   SMR; Q08079; -.
DR   STRING; 269084.syc0230_c; -.
DR   EnsemblBacteria; BAD78420; BAD78420; syc0230_c.
DR   KEGG; syc:syc0230_c; -.
DR   eggNOG; COG0266; Bacteria.
DR   Proteomes; UP000001175; 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; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
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; PS01242; ZF_FPG_1; 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; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..282
FT                   /note="Formamidopyrimidine-DNA glycosylase"
FT                   /id="PRO_0000170877"
FT   ZN_FING         246..280
FT                   /note="FPG-type"
FT   ACT_SITE        2
FT                   /note="Schiff-base intermediate with DNA"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        3
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        59
FT                   /note="Proton donor; for beta-elimination activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        270
FT                   /note="Proton donor; for delta-elimination activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   282 AA;  31794 MW;  D13CE1DCD43503B1 CRC64;
     MPELPEVETV RRGLTQQTLQ RVCTGGEVLL SRTIATPTPE LFLVALQQTQ IQEWRRRGKY
     LLADLSREGE PAGTWGVHLR MTGQFFWTEP ATPLTKHTRV RLRFEGDREL RFIDIRSFGQ
     MWWVPPDRPV ESVITGLSKL GPEPFAPEFT ARYLRDRLRR SQRPIKTALL DQSLVAGIGN
     IYADESLFRT GIHPTTPSDR LTKIQAEKLR EAIVEVLTAS IGAGGTTFSD FRDLTGVNGN
     YGGQAWVYGR KDQPCRTCGT PIQKLKLAGR SSHFCPRCQP CS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024