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A7HZC4 (FPG_PARL1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:Plav_3659
OrganismParvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966) [Complete proteome] [HAMAP]
Taxonomic identifier402881 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhodobiaceaeParvibaculum

Protein attributes

Sequence length293 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 – 293292Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000071310

Regions

Zinc finger257 – 29337FPG-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 site2831Proton donor; for delta-elimination activity By similarity
Binding site1101DNA By similarity
Binding site1291DNA By similarity
Binding site1721DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
A7HZC4 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: B458D39B29C3B439

FASTA29331,903
        10         20         30         40         50         60 
MPELPEVETV RRGLAPALEG RRIVHVTQRR PDLRFPLPEL FAKRLTGRRV IRLERRAKYI 

        70         80         90        100        110        120 
LVYMEPAKSG GAEDVLIMHL GMSGRFTVHG PSGSSAPGLF HLGMPGGETH DHIVFDMEDG 

       130        140        150        160        170        180 
TRVVYADHRR FGFMDLVAEP ELASSRHLAA LGPEPLGNEF SALVLAERLK GRRAPIKSAL 

       190        200        210        220        230        240 
LDQRTVAGLG NIYVCEALYR AGISPLRTAA SIGPARVERL TAAIRAVLQD AIAAGGSTLR 

       250        260        270        280        290 
DYAATDGELG YFQHAFAVYG REGEACSKPG CGGTVRRIVQ SARSTFYCPA CQR 

« Hide

References

[1]"Complete genome sequence and annotation of Parvibaculum lavamentivorans DS-1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DS-1 / DSM 13023 / NCIMB 13966.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000774 Genomic DNA. Translation: ABS65257.1.
RefSeqYP_001414914.1. NC_009719.1.

3D structure databases

ProteinModelPortalA7HZC4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING402881.Plav_3659.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABS65257; ABS65257; Plav_3659.
GeneID5456284.
KEGGpla:Plav_3659.
PATRIC22869125. VBIParLav90819_3766.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020884.
KOK10563.
OMARCATPIE.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycPLAV402881:GHQA-3705-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_PARL1
AccessionPrimary (citable) accession number: A7HZC4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: September 11, 2007
Last modified: February 19, 2014
This is version 43 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