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A1AV29 (FPG_PELPD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. 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:Ppro_3608
OrganismPelobacter propionicus (strain DSM 2379) [Complete proteome] [HAMAP]
Taxonomic identifier338966 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter

Protein attributes

Sequence length267 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 – 267266Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000008732

Regions

Zinc finger233 – 26735FPG-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 site2571Proton donor; for delta-elimination activity By similarity
Binding site911DNA By similarity
Binding site1101DNA By similarity
Binding site1521DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
A1AV29 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: C08B22C273E14CD5

FASTA26729,718
        10         20         30         40         50         60 
MPELPEVELT RRRLERDITG KQVQQVLVRA PKLRLPVPPE LEEALKGRTV RAVERRGKYL 

        70         80         90        100        110        120 
LLECEAGWLI VHLGMTGFLR LLHTPQLPGK HDHVDIVFTD GSVLRFHDPR KFGTIAWTTD 

       130        140        150        160        170        180 
SLDKHPLLAG IGPEPLTAAF SGAYLFRVSR TRRVVVKLLI MNMAIVAGVG NIYANEALFR 

       190        200        210        220        230        240 
AGIRPDRAAS SLSRTECERL AVTIREVLQE SIDLGSTYRV EEGTVTYHPL AFDVYGRGHG 

       250        260 
TCTSCGGALE AVRLGNRSTV FCPRCQQ 

« Hide

References

[1]"Complete sequence of chromosome of Pelobacter propionicus DSM 2379."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000482 Genomic DNA. Translation: ABL01200.1.
RefSeqYP_903257.1. NC_008609.1.

3D structure databases

ProteinModelPortalA1AV29.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING338966.Ppro_3608.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL01200; ABL01200; Ppro_3608.
GeneID4574536.
KEGGppd:Ppro_3608.
PATRIC22900347. VBIPelPro64470_3758.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020881.
KOK10563.
OMADHVDLKL.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycPPRO338966:GHL0-3667-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_PELPD
AccessionPrimary (citable) accession number: A1AV29
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 54 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