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B1VG60 (FPG_CORU7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 46. 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:cu0789
OrganismCorynebacterium urealyticum (strain ATCC 43042 / DSM 7109) [Complete proteome] [HAMAP]
Taxonomic identifier504474 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length289 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 – 289288Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000094039

Regions

Zinc finger254 – 28835FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site611Proton donor; for beta-elimination activity By similarity
Active site2781Proton donor; for delta-elimination activity By similarity
Binding site971DNA By similarity
Binding site1191DNA By similarity
Binding site1681DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
B1VG60 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: EAAA95AF3195B06F

FASTA28931,437
        10         20         30         40         50         60 
MPELPEVEVV RRGLEEHLSD GVIHDVDVRH PRAVRAQPGG AAELVALLDG ARIQSIERRG 

        70         80         90        100        110        120 
KYMWLVLNNG RALFVHLGMS GQMLIHEASD PALPTTHVRI SARVDVGEKD LVLSFVDQRT 

       130        140        150        160        170        180 
FGQWQVTPVV ADPHGGFTGV PVPVAHIAPD PFEAVFDPAV VARRLRAKKT DVKRAILDQT 

       190        200        210        220        230        240 
LVSGIGNIYA DEALWAAGVA PSRRTRGMRQ RDAVAVLEQA GAVMRRALAQ GGTSFDSLYV 

       250        260        270        280 
NVNGASGYFA RSLNAYGRAG KPCPRCGEPI VRVQWTNRSS HFCPQCQSS 

« Hide

References

[1]"The lifestyle of Corynebacterium urealyticum derived from its complete genome sequence established by pyrosequencing."
Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A., Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J., Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M., Puehler A.
J. Biotechnol. 136:11-21(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43042 / DSM 7109.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM942444 Genomic DNA. Translation: CAQ04749.1.
RefSeqYP_001800183.1. NC_010545.1.

3D structure databases

ProteinModelPortalB1VG60.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING504474.cur_0789.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAQ04749; CAQ04749; cu0789.
GeneID6185823.
KEGGcur:cur_0789.
PATRIC21521304. VBICorUre58120_0788.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
KOK10563.
OMADHVDLKL.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycCURE504474:GJ8Y-805-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_CORU7
AccessionPrimary (citable) accession number: B1VG60
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 46 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