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O50606 (FPG_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:TTHA1806
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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.

Subunit structure

Monomer.

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 HAMAP-Rule MF_00103
Chain2 – 267266Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_0000170880

Regions

Zinc finger230 – 26435FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA Probable
Active site31Proton donor Probable
Active site531Proton donor; for beta-elimination activity Probable
Active site2541Proton donor; for delta-elimination activity Probable
Binding site821DNA By similarity
Binding site1001DNA By similarity

Secondary structure

................................................. 267
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O50606 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CDEAEAB2BED893EA

FASTA26729,915
        10         20         30         40         50         60 
MPELPEVETT RRRLRPLVLG QTLRQVVHRD PARYRNTALA EGRRILEVDR RGKFLLFALE 

        70         80         90        100        110        120 
GGVELVAHLG MTGGFRLEPT PHTRAALVLE GRTLYFHDPR RFGRLFGVRR GDYREIPLLL 

       130        140        150        160        170        180 
RLGPEPLSEA FAFPGFFRGL KESARPLKAL LLDQRLAAGV GNIYADEALF RARLSPFRPA 

       190        200        210        220        230        240 
RSLTEEEARR LYRALREVLA EAVELGGSTL SDQSYRQPDG LPGGFQTRHA VYGREGLPCP 

       250        260 
ACGRPVERRV VAGRGTHFCP TCQGEGP 

« Hide

References

« Hide 'large scale' references
[1]"Thermostable repair enzyme for oxidative DNA damage from extremely thermophilic bacterium, Thermus thermophilus HB8."
Mikawa T., Kato R., Sugahara M., Kuramitsu S.
Nucleic Acids Res. 26:903-910(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[3]"Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8."
Sugahara M., Mikawa T., Kumasaka T., Yamamoto M., Kato R., Fukuyama K., Inoue Y., Kuramitsu S.
EMBO J. 19:3857-3869(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB008520 Genomic DNA. Translation: BAA24892.1.
AP008226 Genomic DNA. Translation: BAD71629.1.
RefSeqYP_145072.1. NC_006461.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EE8X-ray1.90A/B2-267[»]
ProteinModelPortalO50606.
SMRO50606. Positions 2-267.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA1806.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71629; BAD71629; BAD71629.
GeneID3169771.
KEGGttj:TTHA1806.
PATRIC23958581. VBITheThe93045_1777.

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020884.
KOK10563.
OMAIYCSESL.
OrthoDBEOG6QP131.
PhylomeDBO50606.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-1851-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...

Other

EvolutionaryTraceO50606.

Entry information

Entry nameFPG_THET8
AccessionPrimary (citable) accession number: O50606
Secondary accession number(s): Q5SHC4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references