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P19210 (FPG_BACFI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 87. 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
OrganismBacillus firmus
Taxonomic identifier1399 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length274 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 – 274273Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_0000170809

Regions

Zinc finger240 – 27435FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site601Proton donor; for beta-elimination activity By similarity
Active site2641Proton donor; for delta-elimination activity By similarity
Binding site931DNA By similarity
Binding site1121DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
P19210 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D5B074711E5AD33F

FASTA27431,114
        10         20         30         40         50         60 
MPELPEVETV KRTLTELVIG KTIAGITVKW ANIIKEPADV LEFETLLMNQ TIRSIRRRGK 

        70         80         90        100        110        120 
FLLFEFDDIV MVSHLRMEGR YGLYEKEEPL PPHTHVIFHF TDGEELRYQD VRKFGTMHLF 

       130        140        150        160        170        180 
PKGSEEKVLP LAHLGVEPFS EQFTSELLMN AFQKTNRKIK VALLDQKTVV GLGNIYVDEA 

       190        200        210        220        230        240 
LFRARIHPER LAHSLSKEEM AVLHKAIVST LEEAVEMGGS SIKSYVNGQG EMGMFQQKLG 

       250        260        270 
VYGRKNEPCR QCGTDILKTV VGGRGTHFCP NCQL 

« Hide

References

[1]"Nucleotide sequence of a gene from alkaliphilic Bacillus firmus RAB that is homologous to the fpg gene of Escherichia coli."
Ivey D.M.
Nucleic Acids Res. 18:5882-5882(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RAB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53930 Genomic DNA. Translation: CAA37877.1.
PIRS11489.

3D structure databases

ProteinModelPortalP19210.
SMRP19210. Positions 2-273.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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_BACFI
AccessionPrimary (citable) accession number: P19210
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 87 of the entry and version 3 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