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Reviewed, UniProtKB/Swiss-Prot Q0A598 (FPG_ALHEH)

Last modified June 16, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: Mlg_2649
OrganismAlkalilimnicola ehrlichei (strain MLHE-1) [Complete proteome] [HAMAP]
Taxonomic identifier187272 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaChromatialesEctothiorhodospiraceaeAlkalilimnicola

Protein attributes

Sequence length277 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.

Catalytic activity

Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine. HAMAP 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 MF_00103

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Monomer By similarity.

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 – 277276Formamidopyrimidine-DNA glycosylase HAMAP MF_00103
PRO_1000008673

Regions

Zinc finger243 – 27735FPG-type HAMAP 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 site2671Proton donor; for delta-elimination activity By similarity
Binding site971DNA By similarity
Binding site1161DNA By similarity
Binding site1581DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0A598-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 9DD01C45EF06DE1B

FASTA27730,392
        10         20         30         40         50         60 
MPELPEVETT RRGLAPLLEG RRVTGMTVRQ ARLRWPVPAG LPDAITGQTI RAVDRRAKYL 

        70         80         90        100        110        120 
LFRTPAGTLI LHLGMSGSLR VIPGQQAGAC AVPPGRHDHV DLRLADGSCL RYTDPRRFGS 

       130        140        150        160        170        180 
LHWCTGEPEA HWLLHRLGPE PFDTAFDGDR LHRLSRGRRT SVKAFIMDSG IVVGVGNIYA 

       190        200        210        220        230        240 
SESLFRAGIH PGRPAGRVGL ARYRRLAGAV REVLAEAIAA GGTTLRDFTA SDGRPGYFAQ 

       250        260        270 
TLNVYGRAGA PCPRCGRSIR QRRIAQRSTW YCPGCQR 

« Hide

References

[1]"Complete sequence of Alkalilimnicola ehrilichei MLHE-1."
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., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000453 Genomic DNA. Translation: ABI57989.1.
RefSeqYP_743479.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4268539.
GenomeReviewsGene locus Mlg_2649 in contig CP000453_GR.
KEGGaeh:Mlg_2649.
NMPDRfig|187272.6.peg.2526.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ0A598.
OMAQ0A598. SSARFLH.

Family and domain databases

HAMAPMF_00103.
[Tree]
InterProIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
IPR000214. DNA_glyclase/AP_lyase_Znf_dom.
IPR015887. DNA_glyclase_Znf_dom_DNA_BS.
IPR000191. DNA_glycosylase/AP_lyase.
IPR012319. DNA_glycosylase/AP_lyase_cat.
[Graphical view]
PfamPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 1 hit.
[Graphical view]
ProDomPD003680. Fapy_DNA_glyco. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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_ALHEH
AccessionPrimary (citable) accession number: Q0A598
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: June 16, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents