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Q88WV4 (FPG_LACPL) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 80. 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:lp_1509
OrganismLactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1) [Reference proteome] [HAMAP]
Taxonomic identifier220668 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

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_0000170831

Regions

Zinc finger239 – 27335FPG-type; degenerate 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 site2631Proton donor; for delta-elimination activity By similarity
Binding site921DNA By similarity
Binding site1111DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q88WV4 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 443C4379233F94C4

FASTA27430,892
        10         20         30         40         50         60 
MPELPEVETV RRGLNRLVSG ATIASIEVFW PKIINNDVDS FKQRLANQTI QTIDRRGKYL 

        70         80         90        100        110        120 
LFRFSNGLTM VSHLRMEGKY NVVPRGEDQG KHTHVIFHLT DDRDLLYNDT RKFGRMTLVP 

       130        140        150        160        170        180 
TGEENTVAGL RTIGPEPVAE QLTLAYMTAT FGKSKKMIKP LLLDQSKIAG IGNIYADETL 

       190        200        210        220        230        240 
WMSKIHPMRP ANSLTTDEIA TLRQNIIDEM AMAIKGHGTT VHSFSTAFGE AGQFQNHLHV 

       250        260        270 
YGREGEPCER CGTIIEKIKV AQRGTHFCPL EQRL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL935263 Genomic DNA. Translation: CCC78835.1.
RefSeqYP_004889349.1. NC_004567.2.

3D structure databases

ProteinModelPortalQ88WV4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220668.lp_1509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCC78835; CCC78835; lp_1509.
GeneID1063357.
KEGGlpl:lp_1509.
PATRIC22249253. VBILacPla27411_1269.

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020885.
KOK10563.
OMAGWIIVHL.
ProtClustDBPRK01103.

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_LACPL
AccessionPrimary (citable) accession number: Q88WV4
Secondary accession number(s): F9UNP6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 80 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