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

Q5XDE4 (FPG_STRP6) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 74. 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:M6_Spy0434
OrganismStreptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394) [Complete proteome] [HAMAP]
Taxonomic identifier286636 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length275 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 – 275274Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_0000170873

Regions

Zinc finger238 – 27235FPG-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 site2621Proton donor; for delta-elimination activity By similarity
Binding site911DNA By similarity
Binding site1101DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5XDE4 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 49988D5194DAC59B

FASTA27530,717
        10         20         30         40         50         60 
MPELPEVETV RRGLKALVLG QEIVAVTLKV PKMVKTDLET FALTLPGQII QSVGRRGKYL 

        70         80         90        100        110        120 
LIDLGQLVLV SHLRMEGKYL LFPDEVPDNK HFHVFFELKN GSTLVYQDVR KFGTFDLIAK 

       130        140        150        160        170        180 
SQLSAFFAKR KLGPEPKKET FKLKTFEAVL LSSKKTIKPH LLDQTLVAGL GNIYVDEVLW 

       190        200        210        220        230        240 
AAKVHPETAS SRLNKAEIKR LHDETIRILA LGIEKGGSTV RTYRNTLGAD GTMQDYLQVY 

       250        260        270 
GQTGKPCPRC GQAIVKLKVG GRGTHICPKC QKKRP 

« Hide

References

[1]"Progress toward characterization of the group A Streptococcus metagenome: complete genome sequence of a macrolide-resistant serotype M6 strain."
Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E., Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.
J. Infect. Dis. 190:727-738(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-946 / MGAS10394.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000003 Genomic DNA. Translation: AAT86569.1.
RefSeqYP_059752.1. NC_006086.1.

3D structure databases

ProteinModelPortalQ5XDE4.
SMRQ5XDE4. Positions 2-273.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING286636.M6_Spy0434.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT86569; AAT86569; M6_Spy0434.
GeneID2941611.
KEGGspa:M6_Spy0434.
PATRIC19723005. VBIStrPyo30273_0452.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020885.
KOK10563.
OMARCATPIE.
OrthoDBEOG6QP131.
ProtClustDBPRK01103.

Enzyme and pathway databases

BioCycSPYO286636:GHNO-490-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_STRP6
AccessionPrimary (citable) accession number: Q5XDE4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 74 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