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Q16DL0 (FPG_ROSDO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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:RD1_0204
OrganismRoseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp. (strain OCh 114)) (Roseobacter denitrificans) [Complete proteome] [HAMAP]
Taxonomic identifier375451 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodobacteralesRhodobacteraceaeRoseobacter

Protein attributes

Sequence length283 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 – 283282Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000008764

Regions

Zinc finger247 – 28337FPG-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 site2731Proton donor; for delta-elimination activity By similarity
Binding site1001DNA By similarity
Binding site1191DNA By similarity
Binding site1621DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q16DL0 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 6DAB1DAFD2E6C27D

FASTA28331,350
        10         20         30         40         50         60 
MPELPEVETV RRGLTPAMEG VVIARADVNR PDLRWPFPAD MAARLTGKRV ERLRRRSKYI 

        70         80         90        100        110        120 
LMDLDSGETL LVHLGMSGRM LVSGDPLGQF VHSHPAPEKH DHVVFHMANN ARITFNDPRR 

       130        140        150        160        170        180 
FGAMDLMETA SADTHKLLSV LGPEPLGNDF HESHLIEAFK NRNSPVKSVL LDQRIVSGLG 

       190        200        210        220        230        240 
NIYVCEALFR AKIHPIRKAG KISGARVATL VPIIREVLAE AIEAGGSSLR DFKQADGELG 

       250        260        270        280 
YFQHSFDVYG REGAPCKGEG CTGQIKRIVQ SGRSSFYCAQ CQR 

« Hide

References

[1]"The complete genome sequence of Roseobacter denitrificans reveals a mixotrophic rather than photosynthetic metabolism."
Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H., Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K., O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T., Touchman J.W.
J. Bacteriol. 189:683-690(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33942 / OCh 114.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000362 Genomic DNA. Translation: ABG29933.1.
RefSeqYP_680619.1. NC_008209.1.

3D structure databases

ProteinModelPortalQ16DL0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING375451.RD1_0204.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG29933; ABG29933; RD1_0204.
GeneID4198193.
KEGGrde:RD1_0204.
PATRIC23358587. VBIRosDen86677_0198.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020881.
KOK10563.
OMAGAHDHFE.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycRDEN375451:GJIZ-192-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.
[Graphical view]
PfamPF01149. Fapy_DNA_glyco. 1 hit.
PF06831. H2TH. 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_ROSDO
AccessionPrimary (citable) accession number: Q16DL0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 25, 2006
Last modified: May 14, 2014
This is version 61 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