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A1BAN2 (FPG_PARDP) 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:Pden_4512
OrganismParacoccus denitrificans (strain Pd 1222) [Complete proteome] [HAMAP]
Taxonomic identifier318586 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeParacoccus

Protein attributes

Sequence length281 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 – 281280Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000008730

Regions

Zinc finger245 – 28137FPG-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 site2711Proton donor; for delta-elimination activity By similarity
Binding site1001DNA By similarity
Binding site1191DNA By similarity
Binding site1601DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
A1BAN2 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 11C161FC68CF6D44

FASTA28130,669
        10         20         30         40         50         60 
MPELPEVETV RRGLQPHLEG RVIARAEARR PDLRWPLPPD LVQVLTGARV VALRRRSKYI 

        70         80         90        100        110        120 
LAELEDRGSL LLHLGMSGRM LIEGESQGDF HRDPAILPRH DHVVLWNDQG TRITFNDARR 

       130        140        150        160        170        180 
FGMVDLVPPG AEHPLLAHLG PEPLSDAFTA EALAAAFAGR RMPVKAALLD QRIVAGLGNI 

       190        200        210        220        230        240 
YVSEALYRAG IDPRRLAGAV TAPEVAALVG HVRAVLEEAI AAGGSSLRDH RQATGELGYF 

       250        260        270        280 
QHSFRVYGRE GAPCPTPGCT GTVQRIVQSG RSSFFCPLCQ Q 

« Hide

References

[1]"Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222."
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., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pd 1222.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000490 Genomic DNA. Translation: ABL72576.1.
RefSeqYP_918272.1. NC_008687.1.

3D structure databases

ProteinModelPortalA1BAN2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING318586.Pden_4512.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL72576; ABL72576; Pden_4512.
GeneID4583062.
KEGGpde:Pden_4512.
PATRIC22860246. VBIParDen97112_4475.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020884.
KOK10563.
OMAIYCSESL.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycPDEN318586:GCVQ-4555-MONOMER.

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_PARDP
AccessionPrimary (citable) accession number: A1BAN2
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