ECOLI:FPG

Species (Taxon ID)	Escherichia coli (strain K12). (83333)
Gene Name(s)	mutM (synonyms: fpg)
Protein Name(s)	Formamidopyrimidine-DNA glycosylase Fapy-DNA glycosylase DNA-(apurinic or apyrimidinic site) lyase MutM AP lyase MutM
External Links
UniProt	P05523
EMBL	M86305 X06036 L10328 U00039 U00096 AP009048 M60670
PIR	A30254
RefSeq	NP_418092.1 YP_491798.1
PDB	1K82
PDBsum	1K82
ProteinModelPortal	P05523
SMR	P05523
DIP	DIP-10286N
IntAct	P05523
STRING	511145.b3635
PaxDb	P05523
PRIDE	P05523
EnsemblBacteria	AAC76659 BAE77657
GeneID	12933569 946765
KEGG	ecj:Y75_p3539 eco:b3635
PATRIC	32122757
EchoBASE	EB0325
EcoGene	EG10329
eggNOG	COG0266
HOGENOM	HOG000020881
InParanoid	P05523
KO	K10563
OMA	DGWIIVH
OrthoDB	EOG6QP131
PhylomeDB	P05523
BioCyc	EcoCyc:EG10329-MONOMER ECOL316407:JW3610-MONOMER MetaCyc:EG10329-MONOMER
EvolutionaryTrace	P05523
PRO	PR:P05523
Proteomes	UP000000318 UP000000625
Genevestigator	P05523
GO	GO:0003684 GO:0019104 GO:0003906 GO:0004519 GO:0046872 GO:0008534 GO:0000703 GO:0008270 GO:0006285 GO:0006974 GO:0000737 GO:0090305 GO:0006289
HAMAP	MF_00103
InterPro	IPR015886 IPR015887 IPR000191 IPR012319 IPR020629 IPR010979 IPR000214 IPR010663
Pfam	PF01149 PF06831 PF06827
SMART	SM00898
SUPFAM	SSF46946 SSF81624
TIGRFAMs	TIGR00577
PROSITE	PS51068 PS01242 PS51066

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
enables	GO:0034039	8-oxo-7,8-dihydroguanine DNA N-glycosylase activity	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000543066 UniProtKB:P9WNC3	F	Seeded From UniProt	complete
enables	GO:0019104	DNA N-glycosylase activity	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10329 MGI:MGI:1920024 MGI:MGI:2384588 PANTHER:PTN000542974 TAIR:locus:2035195 UniProtKB:Q8TAT5	F	Seeded From UniProt	complete
involved_in	GO:0006285	base-excision repair, AP site formation	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10329 PANTHER:PTN000543066	P	Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:2384588 PANTHER:PTN000542974 UniProtKB:P9WNC3 UniProtKB:Q8TAT5 UniProtKB:Q96FI4	P	Seeded From UniProt	complete
enables	GO:0003906	DNA-(apurinic or apyrimidinic site) endonuclease activity	PMID:21873635^[1]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	EcoGene:EG10329 MGI:MGI:2384588 PANTHER:PTN000542974 UniProtKB:Q8TAT5	F	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	PMID:8473347^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0019104	DNA N-glycosylase activity	PMID:8473347^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0019104	DNA N-glycosylase activity	PMID:2664776^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0019104	DNA N-glycosylase activity	PMID:10862773^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0019104	DNA N-glycosylase activity	PMID:1649454^[5]	ECO:0000269	experimental evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	PMID:8473347^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	PMID:1731864^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	PMID:8473347^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	PMID:2664776^[3]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	PMID:1731864^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004519	endonuclease activity	PMID:1649454^[5]	ECO:0000269	experimental evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003906	DNA-(apurinic or apyrimidinic site) endonuclease activity	PMID:8473347^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003906	DNA-(apurinic or apyrimidinic site) endonuclease activity	PMID:1731864^[6]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:10862773^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0008534	oxidized purine nucleobase lesion DNA N-glycosylase activity	PMID:1689309^[7]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0006285	base-excision repair, AP site formation	PMID:1689309^[7]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	PMID:8332499^[8]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0000703	oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity	PMID:8034633^[9]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004519	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004519	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004519	P	Seeded From UniProt	complete
involved_in	GO:0090305	nucleic acid phosphodiester bond hydrolysis	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004519	P	Seeded From UniProt	complete
enables	GO:0003676	nucleic acid binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR010979	F	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR015887	F	Seeded From UniProt	complete
enables	GO:0003684	damaged DNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012319 InterPro:IPR015886	F	Seeded From UniProt	complete
enables	GO:0003906	DNA-(apurinic or apyrimidinic site) endonuclease activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000214 InterPro:IPR012319 InterPro:IPR015886 InterPro:IPR015887 InterPro:IPR020629	F	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000214 InterPro:IPR015887 InterPro:IPR020629	P	Seeded From UniProt	complete
involved_in	GO:0006284	base-excision repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR012319	P	Seeded From UniProt	complete
involved_in	GO:0006289	nucleotide-excision repair	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR015886	P	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000214 InterPro:IPR012319 InterPro:IPR015886 InterPro:IPR015887 InterPro:IPR020629	F	Seeded From UniProt	complete
enables	GO:0008534	oxidized purine nucleobase lesion DNA N-glycosylase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR020629	F	Seeded From UniProt	complete
enables	GO:0016799	hydrolase activity, hydrolyzing N-glycosyl compounds	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000214 InterPro:IPR012319 InterPro:IPR015886 InterPro:IPR015887	F	Seeded From UniProt	complete
enables	GO:0140078	class I DNA-(apurinic or apyrimidinic site) endonuclease activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:4.2.99.18	F	Seeded From UniProt	complete
enables	GO:0008534	oxidized purine nucleobase lesion DNA N-glycosylase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.2.2.23	F	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000076501	P	Seeded From UniProt	complete
enables	GO:0003906	DNA-(apurinic or apyrimidinic site) endonuclease activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000076501	F	Seeded From UniProt	complete
enables	GO:0008270	zinc ion binding	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000076501	F	Seeded From UniProt	complete
enables	GO:0008534	oxidized purine nucleobase lesion DNA N-glycosylase activity	GO_REF:0000104	ECO:0000256	match to sequence model evidence used in automatic assertion	UniRule:UR000076501	F	Seeded From UniProt	complete
enables	GO:0016798	hydrolase activity, acting on glycosyl bonds	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0326	F	Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F	Seeded From UniProt	complete
involved_in	GO:0006281	DNA repair	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0234	P	Seeded From UniProt	complete
involved_in	GO:0008152	metabolic process	GO_REF:0000037 GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511 UniProtKB-KW:KW-0326	P	Seeded From UniProt	complete
enables	GO:0003677	DNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0238	F	Seeded From UniProt	complete
enables	GO:0003824	catalytic activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0511	F	Seeded From UniProt	complete
enables	GO:0016829	lyase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0456	F	Seeded From UniProt	complete
involved_in	GO:0006974	cellular response to DNA damage stimulus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0227	P	Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 O'Connor, TR et al. (1993) Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role. J. Biol. Chem. 268 9063-70 PubMed GONUTS page
↑ ^3.0 ^3.1 O'Connor, TR & Laval, J (1989) Physical association of the 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase of Escherichia coli and an activity nicking DNA at apurinic/apyrimidinic sites. Proc. Natl. Acad. Sci. U.S.A. 86 5222-6 PubMed GONUTS page
↑ ^4.0 ^4.1 Hazra, TK et al. (2000) Characterization of a novel 8-oxoguanine-DNA glycosylase activity in Escherichia coli and identification of the enzyme as endonuclease VIII. J. Biol. Chem. 275 27762-7 PubMed GONUTS page
↑ ^5.0 ^5.1 Michaels, ML et al. (1991) MutM, a protein that prevents G.C----T.A transversions, is formamidopyrimidine-DNA glycosylase. Nucleic Acids Res. 19 3629-32 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Boiteux, S et al. (1992) Substrate specificity of the Escherichia coli Fpg protein (formamidopyrimidine-DNA glycosylase): excision of purine lesions in DNA produced by ionizing radiation or photosensitization. Biochemistry 31 106-10 PubMed GONUTS page
↑ ^7.0 ^7.1 Boiteux, S et al. (1990) Homogeneous Escherichia coli FPG protein. A DNA glycosylase which excises imidazole ring-opened purines and nicks DNA at apurinic/apyrimidinic sites. J. Biol. Chem. 265 3916-22 PubMed GONUTS page
↑ Castaing, B et al. (1993) Cleavage and binding of a DNA fragment containing a single 8-oxoguanine by wild type and mutant FPG proteins. Nucleic Acids Res. 21 2899-905 PubMed GONUTS page
↑ Hatahet, Z et al. (1994) New substrates for old enzymes. 5-Hydroxy-2'-deoxycytidine and 5-hydroxy-2'-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2'-deoxyuridine is a substrate for uracil DNA N-glycosylase. J. Biol. Chem. 269 18814-20 PubMed GONUTS page

[PMID:21873635-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:8473347-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 O'Connor, TR et al. (1993) Fpg protein of Escherichia coli is a zinc finger protein whose cysteine residues have a structural and/or functional role. J. Biol. Chem. 268 9063-70 PubMed GONUTS page

[PMID:2664776-3] 3.0 ^3.1 O'Connor, TR & Laval, J (1989) Physical association of the 2,6-diamino-4-hydroxy-5N-formamidopyrimidine-DNA glycosylase of Escherichia coli and an activity nicking DNA at apurinic/apyrimidinic sites. Proc. Natl. Acad. Sci. U.S.A. 86 5222-6 PubMed GONUTS page

[PMID:10862773-4] 4.0 ^4.1 Hazra, TK et al. (2000) Characterization of a novel 8-oxoguanine-DNA glycosylase activity in Escherichia coli and identification of the enzyme as endonuclease VIII. J. Biol. Chem. 275 27762-7 PubMed GONUTS page

[PMID:1649454-5] 5.0 ^5.1 Michaels, ML et al. (1991) MutM, a protein that prevents G.C----T.A transversions, is formamidopyrimidine-DNA glycosylase. Nucleic Acids Res. 19 3629-32 PubMed GONUTS page

[PMID:1731864-6] 6.0 ^6.1 ^6.2 Boiteux, S et al. (1992) Substrate specificity of the Escherichia coli Fpg protein (formamidopyrimidine-DNA glycosylase): excision of purine lesions in DNA produced by ionizing radiation or photosensitization. Biochemistry 31 106-10 PubMed GONUTS page

[PMID:1689309-7] 7.0 ^7.1 Boiteux, S et al. (1990) Homogeneous Escherichia coli FPG protein. A DNA glycosylase which excises imidazole ring-opened purines and nicks DNA at apurinic/apyrimidinic sites. J. Biol. Chem. 265 3916-22 PubMed GONUTS page

[PMID:8332499-8] Castaing, B et al. (1993) Cleavage and binding of a DNA fragment containing a single 8-oxoguanine by wild type and mutant FPG proteins. Nucleic Acids Res. 21 2899-905 PubMed GONUTS page

[PMID:8034633-9] Hatahet, Z et al. (1994) New substrates for old enzymes. 5-Hydroxy-2'-deoxycytidine and 5-hydroxy-2'-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA N-glycosylase, while 5-hydroxy-2'-deoxyuridine is a substrate for uracil DNA N-glycosylase. J. Biol. Chem. 269 18814-20 PubMed GONUTS page

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ECOLI:FPG

Contents

Annotations

Notes

References

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