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Protein

Formamidopyrimidine-DNA glycosylase

Gene

mutM

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  • damaged DNA binding Source: EcoliWiki
  • DNA-(apurinic or apyrimidinic site) lyase activity Source: EcoliWiki
  • DNA N-glycosylase activity Source: EcoliWiki
  • endonuclease activity Source: EcoliWiki
  • metal ion binding Source: EcoliWiki
  • oxidized purine nucleobase lesion DNA N-glycosylase activity Source: EcoCyc
  • oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity Source: EcoCyc
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

  • base-excision repair, AP site formation Source: EcoCyc
  • cellular response to DNA damage stimulus Source: EcoliWiki
  • nucleotide-excision repair Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10329-MONOMER.
ECOL316407:JW3610-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. 107 interactors.
DIPiDIP-10286N.
IntActiP05523. 12 interactors.
STRINGi511145.b3635.

Structurei

Secondary structure

1269
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 18Combined sources15
Beta strandi22 – 29Combined sources8
Beta strandi32 – 36Combined sources5
Helixi39 – 43Combined sources5
Beta strandi46 – 49Combined sources4
Beta strandi51 – 55Combined sources5
Beta strandi58 – 62Combined sources5
Beta strandi67 – 71Combined sources5
Turni73 – 75Combined sources3
Beta strandi77 – 84Combined sources8
Beta strandi93 – 97Combined sources5
Beta strandi102 – 106Combined sources5
Beta strandi113 – 118Combined sources6
Beta strandi120 – 123Combined sources4
Helixi124 – 126Combined sources3
Helixi140 – 147Combined sources8
Helixi154 – 158Combined sources5
Turni161 – 163Combined sources3
Helixi169 – 179Combined sources11
Helixi187 – 189Combined sources3
Helixi192 – 211Combined sources20
Helixi231 – 233Combined sources3
Turni245 – 247Combined sources3
Beta strandi252 – 256Combined sources5
Beta strandi259 – 263Combined sources5
Turni265 – 267Combined sources3

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...

Miscellaneous databases

EvolutionaryTraceiP05523.

Family & Domainsi

Domaini

The zinc-finger is necessary for DNA binding.

Sequence similaritiesi

Belongs to the FPG family.Curated
Contains 1 FPG-type zinc finger.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.
OMAiDGWIIVH.
PhylomeDBiP05523.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl. 1 hit.
InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR012319. FPG_cat.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_FPG/IleRS.
[Graphical view]
PfamiPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
SMARTiSM00898. Fapy_DNA_glyco. 1 hit.
SM01232. H2TH. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsiTIGR00577. fpg. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]

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.
PATRICi32122757. VBIEscCol129921_3755.

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. 107 interactors.
DIPiDIP-10286N.
IntActiP05523. 12 interactors.
STRINGi511145.b3635.

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.
PATRICi32122757. VBIEscCol129921_3755.

Organism-specific databases

EchoBASEiEB0325.
EcoGeneiEG10329. mutM.

Phylogenomic databases

eggNOGiENOG4105ERD. Bacteria.
COG0266. LUCA.
HOGENOMiHOG000020881.
InParanoidiP05523.
KOiK10563.
OMAiDGWIIVH.
PhylomeDBiP05523.

Enzyme and pathway databases

BioCyciEcoCyc:EG10329-MONOMER.
ECOL316407:JW3610-MONOMER.
MetaCyc:EG10329-MONOMER.
BRENDAi3.2.2.23. 2026.

Miscellaneous databases

EvolutionaryTraceiP05523.
PROiP05523.

Family and domain databases

HAMAPiMF_00103. Fapy_DNA_glycosyl. 1 hit.
InterProiIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR012319. FPG_cat.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_FPG/IleRS.
[Graphical view]
PfamiPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
SMARTiSM00898. Fapy_DNA_glyco. 1 hit.
SM01232. H2TH. 1 hit.
[Graphical view]
SUPFAMiSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsiTIGR00577. fpg. 1 hit.
PROSITEiPS51068. FPG_CAT. 1 hit.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFPG_ECOLI
AccessioniPrimary (citable) accession number: P05523
Secondary accession number(s): Q2M7U9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.