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Q12DZ5 (FPG_POLSJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:Bpro_1297
OrganismPolaromonas sp. (strain JS666 / ATCC BAA-500) [Complete proteome] [HAMAP]
Taxonomic identifier296591 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaePolaromonas

Protein attributes

Sequence length271 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 – 271270Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000008734

Regions

Zinc finger236 – 27035FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site561Proton donor; for beta-elimination activity By similarity
Active site2601Proton donor; for delta-elimination activity By similarity
Binding site891DNA By similarity
Binding site1071DNA By similarity
Binding site1511DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q12DZ5 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 098DEF6B121C54CC

FASTA27129,165
        10         20         30         40         50         60 
MPELPEVEVT RLSFAGRIAG ARIEAVSMGK PLRWPLGCSP QQLVGLRVLA VRRRGKYLLV 

        70         80         90        100        110        120 
DLSDGLLLIH LGMSGSVSFG SSLSSPGKHD HFDMVTSLGT LRLNDPRRFG AVVYAGDEHD 

       130        140        150        160        170        180 
AVAHKLLGRL GVEPLSDAFD AALFHQALKP RQTPIKQVLL GGEAVVGVGN IYASEALFLA 

       190        200        210        220        230        240 
GIRPTTKASR ISKPRAALLH RAIRQVLTQA VTKGGSTLRD FSNAQGEAGH FQLDAMVYDR 

       250        260        270 
AGMPCKVCGS PIKSIRQGQR STFYCVSCQK P 

« Hide

References

[1]"Complete sequence of chromosome of Polaromonas sp. JS666."
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., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Anderson I., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS666 / ATCC BAA-500.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000316 Genomic DNA. Translation: ABE43247.1.
RefSeqYP_548145.1. NC_007948.1.

3D structure databases

ProteinModelPortalQ12DZ5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING296591.Bpro_1297.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE43247; ABE43247; Bpro_1297.
GeneID4012191.
KEGGpol:Bpro_1297.
PATRIC22955704. VBIPolSp102244_1333.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020881.
KOK10563.
OMAGAHDHFE.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycPSP296591:GHI4-2018-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_POLSJ
AccessionPrimary (citable) accession number: Q12DZ5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: May 14, 2014
This is version 59 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