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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) and its derivatives such as guanidinohydantoin:C and spiroiminodihydantoin:C, however it also acts on thymine glycol:G, 5,6-dihydrouracil:G and 5-hydroxyuracil:G. Has AP (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA strand. Cleaves the DNA backbone by beta-delta elimination to generate a single-strand break at the site of the removed base with both 3'- and 5'-phosphates. Cleaves ssDNA containing an AP site.2 Publications

Catalytic activityi

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei2Schiff-base intermediate with DNA1
Active sitei3Proton donorCurated1
Active sitei57Proton donor; for beta-elimination activityCurated1
Binding sitei90DNA1 Publication1
Binding sitei109DNA1 Publication1
Binding sitei150DNA1 Publication1
Active sitei259Proton donor; for delta-elimination activityCurated1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri235 – 269FPG-typeAdd BLAST35

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Glycosidase, Hydrolase, Lyase, Multifunctional enzyme
Biological processDNA damage, DNA repair
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10329-MONOMER
MetaCyc:EG10329-MONOMER
BRENDAi3.2.2.23 2026

Names & Taxonomyi

Protein namesi
Recommended name:
Formamidopyrimidine-DNA glycosylase (EC:3.2.2.23)
Short name:
Fapy-DNA glycosylase
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase MutM (EC:4.2.99.18)
Short name:
AP lyase MutM
Gene namesi
Name:mutM
Synonyms:fpg
Ordered Locus Names:b3635, JW3610
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10329 mutM

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi3E → Q: Strong decrease of glycosylase activity; slight decrease of AP lyase activity. 1 Publication1
Mutagenesisi6E → Q: Decrease of glycosylase activity; no effect on AP lyase activity. 1 Publication1
Mutagenesisi90H → A: Increase of substrate affinity and decrease of activity. 1 Publication1
Mutagenesisi107D → N: No effect on glycosylase and AP lyase activity. 1 Publication1
Mutagenesisi109R → A: Over 100-fold decrease of activity. 1 Publication1
Mutagenesisi110R → A: Over 100-fold increase of substrate affinity and decrease of activity. 1 Publication1
Mutagenesisi132E → Q: Decrease of glycosylase activity; slight decrease of AP lyase activity. 1 Publication1
Mutagenesisi160D → N: No effect on glycosylase and AP lyase activity. 1 Publication1
Mutagenesisi174E → Q: Strong decrease of glycosylase activity; slight decrease of AP lyase activity. 1 Publication1
Mutagenesisi218K → T: Slight increase of substrate affinity and decrease of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001708222 – 269Formamidopyrimidine-DNA glycosylaseAdd BLAST268

Proteomic databases

PaxDbiP05523
PRIDEiP05523

Interactioni

Subunit structurei

Monomer.2 Publications

Protein-protein interaction databases

BioGridi4262563, 118 interactors
DIPiDIP-10286N
IntActiP05523, 12 interactors
STRINGi316385.ECDH10B_3817

Structurei

Secondary structure

1269
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP05523
SMRiP05523
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05523

Family & Domainsi

Domaini

The zinc-finger is necessary for DNA binding.

Sequence similaritiesi

Belongs to the FPG family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri235 – 269FPG-typeAdd BLAST35

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4105ERD Bacteria
COG0266 LUCA
HOGENOMiHOG000020881
InParanoidiP05523
KOiK10563
PhylomeDBiP05523

Family and domain databases

Gene3Di3.20.190.10, 1 hit
HAMAPiMF_00103 Fapy_DNA_glycosyl, 1 hit
InterProiView protein in InterPro
IPR015886 DNA_glyclase/AP_lyase_DNA-bd
IPR015887 DNA_glyclase_Znf_dom_DNA_BS
IPR020629 Formamido-pyr_DNA_Glyclase
IPR012319 FPG_cat
IPR035937 MutM-like_N-ter
IPR010979 Ribosomal_S13-like_H2TH
IPR000214 Znf_DNA_glyclase/AP_lyase
IPR010663 Znf_FPG/IleRS
PfamiView protein in Pfam
PF01149 Fapy_DNA_glyco, 1 hit
PF06831 H2TH, 1 hit
PF06827 zf-FPG_IleRS, 1 hit
SMARTiView protein in SMART
SM00898 Fapy_DNA_glyco, 1 hit
SM01232 H2TH, 1 hit
SUPFAMiSSF46946 SSF46946, 1 hit
SSF81624 SSF81624, 1 hit
TIGRFAMsiTIGR00577 fpg, 1 hit
PROSITEiView protein in PROSITE
PS51068 FPG_CAT, 1 hit
PS01242 ZF_FPG_1, 1 hit
PS51066 ZF_FPG_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05523-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPELPEVETS RRGIEPHLVG ATILHAVVRN GRLRWPVSEE IYRLSDQPVL
60 70 80 90 100
SVQRRAKYLL LELPEGWIII HLGMSGSLRI LPEELPPEKH DHVDLVMSNG
110 120 130 140 150
KVLRYTDPRR FGAWLWTKEL EGHNVLTHLG PEPLSDDFNG EYLHQKCAKK
160 170 180 190 200
KTAIKPWLMD NKLVVGVGNI YASESLFAAG IHPDRLASSL SLAECELLAR
210 220 230 240 250
VIKAVLLRSI EQGGTTLKDF LQSDGKPGYF AQELQVYGRK GEPCRVCGTP
260
IVATKHAQRA TFYCRQCQK
Length:269
Mass (Da):30,290
Last modified:January 23, 2007 - v3
Checksum:i01826F7E0E4686EC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86305 Genomic DNA Translation: AAA03747.1
X06036 Genomic DNA Translation: CAA29431.1
L10328 Genomic DNA Translation: AAA61988.1
U00039 Genomic DNA Translation: AAB18612.1
U00096 Genomic DNA Translation: AAC76659.1
AP009048 Genomic DNA Translation: BAE77657.1
M60670 Genomic DNA Translation: AAA24045.1
PIRiA30254 DGECFP
RefSeqiNP_418092.1, NC_000913.3
WP_001114543.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC76659; AAC76659; b3635
BAE77657; BAE77657; BAE77657
GeneIDi946765
KEGGiecj:JW3610
eco:b3635
PATRICifig|1411691.4.peg.3071

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86305 Genomic DNA Translation: AAA03747.1
X06036 Genomic DNA Translation: CAA29431.1
L10328 Genomic DNA Translation: AAA61988.1
U00039 Genomic DNA Translation: AAB18612.1
U00096 Genomic DNA Translation: AAC76659.1
AP009048 Genomic DNA Translation: BAE77657.1
M60670 Genomic DNA Translation: AAA24045.1
PIRiA30254 DGECFP
RefSeqiNP_418092.1, NC_000913.3
WP_001114543.1, NZ_LN832404.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K82X-ray2.10A/B/C/D2-269[»]
ProteinModelPortaliP05523
SMRiP05523
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262563, 118 interactors
DIPiDIP-10286N
IntActiP05523, 12 interactors
STRINGi316385.ECDH10B_3817

Proteomic databases

PaxDbiP05523
PRIDEiP05523

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76659; AAC76659; b3635
BAE77657; BAE77657; BAE77657
GeneIDi946765
KEGGiecj:JW3610
eco:b3635
PATRICifig|1411691.4.peg.3071

Organism-specific databases

EchoBASEiEB0325
EcoGeneiEG10329 mutM

Phylogenomic databases

eggNOGiENOG4105ERD Bacteria
COG0266 LUCA
HOGENOMiHOG000020881
InParanoidiP05523
KOiK10563
PhylomeDBiP05523

Enzyme and pathway databases

BioCyciEcoCyc:EG10329-MONOMER
MetaCyc:EG10329-MONOMER
BRENDAi3.2.2.23 2026

Miscellaneous databases

EvolutionaryTraceiP05523
PROiPR:P05523

Family and domain databases

Gene3Di3.20.190.10, 1 hit
HAMAPiMF_00103 Fapy_DNA_glycosyl, 1 hit
InterProiView protein in InterPro
IPR015886 DNA_glyclase/AP_lyase_DNA-bd
IPR015887 DNA_glyclase_Znf_dom_DNA_BS
IPR020629 Formamido-pyr_DNA_Glyclase
IPR012319 FPG_cat
IPR035937 MutM-like_N-ter
IPR010979 Ribosomal_S13-like_H2TH
IPR000214 Znf_DNA_glyclase/AP_lyase
IPR010663 Znf_FPG/IleRS
PfamiView protein in Pfam
PF01149 Fapy_DNA_glyco, 1 hit
PF06831 H2TH, 1 hit
PF06827 zf-FPG_IleRS, 1 hit
SMARTiView protein in SMART
SM00898 Fapy_DNA_glyco, 1 hit
SM01232 H2TH, 1 hit
SUPFAMiSSF46946 SSF46946, 1 hit
SSF81624 SSF81624, 1 hit
TIGRFAMsiTIGR00577 fpg, 1 hit
PROSITEiView protein in PROSITE
PS51068 FPG_CAT, 1 hit
PS01242 ZF_FPG_1, 1 hit
PS51066 ZF_FPG_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiFPG_ECOLI
AccessioniPrimary (citable) accession number: P05523
Secondary accession number(s): Q2M7U9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: November 7, 2018
This is version 174 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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