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B0UR68 (FPG_METS4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Formamidopyrimidine-DNA glycosylase

Short name=Fapy-DNA glycosylase
EC=3.2.2.23
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase MutM
Short name=AP lyase MutM
EC=4.2.99.18
Gene names
Name:mutM
Synonyms:fpg
Ordered Locus Names:M446_6254
OrganismMethylobacterium sp. (strain 4-46) [Complete proteome] [HAMAP]
Taxonomic identifier426117 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesMethylobacteriaceaeMethylobacterium

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

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). 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 By similarity. HAMAP-Rule MF_00103

Catalytic activity

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine. HAMAP-Rule MF_00103

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. HAMAP-Rule MF_00103

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00103

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00103

Sequence similarities

Belongs to the FPG family.

Contains 1 FPG-type zinc finger.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 297296Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000094055

Regions

Zinc finger259 – 29537FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site581Proton donor; for beta-elimination activity By similarity
Active site2851Proton donor; for delta-elimination activity By similarity
Binding site1061DNA By similarity
Binding site1251DNA By similarity
Binding site1681DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
B0UR68 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: C92BE2A73A266B2C

FASTA29732,460
        10         20         30         40         50         60 
MPELPEVETV RRGLEPALVG ARFTTVHLAR PDLRFPLPAR FAARLTGQRV EALSRRAKYL 

        70         80         90        100        110        120 
VADLSSGDAL IMHLGMSGRF DVVFPDGRQL SPGEFYLEGA PGQAKHDHVV FALSNGARVT 

       130        140        150        160        170        180 
YNDVRRFGFM DLVRRAELET CRHFAGMGIE PLGSDLSGEA VARLFRGRRT PLKAALLDQR 

       190        200        210        220        230        240 
LIAGLGNIYV CEALHRARLH PEAAAGTLAD AAGRPTRAAA RLAQVIRDVL TEAVAAGGST 

       250        260        270        280        290 
LRDYAHTDGT QGAFQHRFRV YDREGLACTA RGCRGRVRRI VQAGRSTFYC ETCQPAP 

« Hide

References

[1]"Complete sequence of chromosome of Methylobacterium sp. 4-46."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Ivanova N., Marx C.J., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 4-46.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000943 Genomic DNA. Translation: ACA20520.1.
RefSeqYP_001772954.1. NC_010511.1.

3D structure databases

ProteinModelPortalB0UR68.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING426117.M446_6254.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACA20520; ACA20520; M446_6254.
GeneID6134707.
KEGGmet:M446_6254.
PATRIC22593797. VBIMetSp32184_6199.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020881.
KOK10563.
OMARCATPIE.
OrthoDBEOG6QP131.
ProtClustDBPRK01103.

Enzyme and pathway databases

BioCycMSP426117:GI2I-6329-MONOMER.

Family and domain databases

HAMAPMF_00103. Fapy_DNA_glycosyl.
InterProIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR000191. DNA_glycosylase/AP_lyase.
IPR012319. DNA_glycosylase/AP_lyase_cat.
IPR020629. Formamido-pyr_DNA_Glyclase.
IPR010979. Ribosomal_S13-like_H2TH.
IPR000214. Znf_DNA_glyclase/AP_lyase.
IPR010663. Znf_DNA_glyclase/IsotRNA_synth.
[Graphical view]
PfamPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
PF06827. zf-FPG_IleRS. 1 hit.
[Graphical view]
SMARTSM00898. Fapy_DNA_glyco. 1 hit.
[Graphical view]
SUPFAMSSF46946. SSF46946. 1 hit.
SSF81624. SSF81624. 1 hit.
TIGRFAMsTIGR00577. fpg. 1 hit.
PROSITEPS51068. FPG_CAT. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFPG_METS4
AccessionPrimary (citable) accession number: B0UR68
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families