Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q117D2 (FPG_TRIEI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Tery_1015
OrganismTrichodesmium erythraeum (strain IMS101) [Complete proteome] [HAMAP]
Taxonomic identifier203124 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeOscillatorialesTrichodesmium

Protein attributes

Sequence length300 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 – 300299Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000008787

Regions

Zinc finger266 – 30035FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site601Proton donor; for beta-elimination activity By similarity
Active site2901Proton donor; for delta-elimination activity By similarity
Binding site1081DNA By similarity
Binding site1361DNA By similarity
Binding site1811DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q117D2 [UniParc].

Last modified August 22, 2006. Version 1.
Checksum: 627B960F42068282

FASTA30033,875
        10         20         30         40         50         60 
MPELPEVEIV KQGLNQLTLN KRILGGEVLL ERTLAYPISV ADFLRGLEGK AIAQWHRQGK 

        70         80         90        100        110        120 
YLLAQLYKWG KKNSKLQEYE NEDGWLGVHL RMTGQLLWVN PEESLHKHTR VRLFFGHNSS 

       130        140        150        160        170        180 
GDKDSSNYEL RFVDQRTFGK MWGVPPGKEI SKVITGLQQL GLEPFSPEFS PKYLNKKLYK 

       190        200        210        220        230        240 
RHRPIKTALL DQTTIAGLGN IYADEALFLS GIRPTTICKD LTEKQIEQLH LAILKVLQTA 

       250        260        270        280        290        300 
INAGGTTFSN FLNVKGVNGN YGGVAWVYSR AGQPCRICNT PLEKIKLAGR STHFCPQCQK 

« Hide

References

[1]"Complete sequence of Trichodesmium erythraeum IMS101."
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., Kiss H., Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: IMS101.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000393 Genomic DNA. Translation: ABG50392.1.
RefSeqYP_720865.1. NC_008312.1.

3D structure databases

ProteinModelPortalQ117D2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING203124.Tery_1015.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG50392; ABG50392; Tery_1015.
GeneID4243094.
KEGGter:Tery_1015.
PATRIC23985616. VBITriEry99848_1247.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020885.
KOK10563.
OMAAKIHPEK.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycTERY203124:GJDR-1022-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_TRIEI
AccessionPrimary (citable) accession number: Q117D2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 22, 2006
Last modified: May 14, 2014
This is version 63 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