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B8EKR5 (FPG_METSB) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 36. 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:Msil_3033
OrganismMethylocella silvestris (strain BL2 / DSM 15510 / NCIMB 13906) [Complete proteome] [HAMAP]
Taxonomic identifier395965 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBeijerinckiaceaeMethylocella

Protein attributes

Sequence length292 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 – 292291Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000118895

Regions

Zinc finger256 – 29237FPG-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 site2821Proton donor; for delta-elimination activity By similarity
Binding site1031DNA By similarity
Binding site1221DNA By similarity
Binding site1651DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
B8EKR5 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 03660146B8556187

FASTA29231,790
        10         20         30         40         50         60 
MPELPEVETV RRGLEPVMVG ARILSVDQRR PDLRFPFPDR FPERLAGRRI LALGRRAKYL 

        70         80         90        100        110        120 
LADLDDGDVL IMHLGMSGSF RVEQAGPAKT LSPRGAPPKN AAHDHVVFTL TSGGRIVYND 

       130        140        150        160        170        180 
PRRFGFMQIA ARADLAAHPL FRSLGVEPLG NELSGAALAR LFAGKTTSLK AALLDQSLVA 

       190        200        210        220        230        240 
GLGNIYVCEA LHRAGLSPLR QAGSLTKKSG RPTERANRLA DTIREVLEEA VAAGGSSLRD 

       250        260        270        280        290 
HRQTNGALGY FQHNFRVYDR ALHPCPTPGC KGEISRITQG GRSSFFCSMC QK 

« Hide

References

[1]"Complete sequence of Methylocella silvestris BL2."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Forester B., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Dunfield P.F., Dedysh S.N., Liesack W. expand/collapse author list , Stott M.B., Smirnova A.V., Alam M., Chen Y., Murrell J.C., Richardson P.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BL2 / DSM 15510 / NCIMB 13906.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001280 Genomic DNA. Translation: ACK51943.1.
RefSeqYP_002363305.1. NC_011666.1.

3D structure databases

ProteinModelPortalB8EKR5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395965.Msil_3033.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACK51943; ACK51943; Msil_3033.
GeneID7092710.
KEGGmsl:Msil_3033.
PATRIC22601838. VBIMetSil55537_3270.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020881.
KOK10563.
OMAFHHARSK.
OrthoDBEOG6QP131.
ProtClustDBPRK01103.

Enzyme and pathway databases

BioCycMSIL395965:GCND-3084-MONOMER.

Family and domain databases

HAMAPMF_00103. Fapy_DNA_glycosyl.
InterProIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
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.
PS01242. ZF_FPG_1. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFPG_METSB
AccessionPrimary (citable) accession number: B8EKR5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: February 19, 2014
This is version 36 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