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Q8P3C4 (FPG_XANCP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. 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:XCC4147
OrganismXanthomonas campestris pv. campestris (strain ATCC 33913 / NCPPB 528 / LMG 568) [Reference proteome] [HAMAP]
Taxonomic identifier190485 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas ›

Protein attributes

Sequence length271 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.

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 – 271270Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_0000170887

Regions

Zinc finger237 – 27135FPG-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 site2611Proton donor; for delta-elimination activity By similarity
Binding site921DNA By similarity
Binding site1111DNA By similarity
Binding site1521DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8P3C4 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B44DA6A70248B194

FASTA27129,783
        10         20         30         40         50         60 
MPELPEVETT LRGLAPHLVG QRIHGVILRR PDLRWPIAAQ IEQLLPGATI TDVRRRAKYL 

        70         80         90        100        110        120 
LIDTDAGGSA VLHLGMSGSL RVLPGDTPPR AHDHVDISLQ NGRVLRFNDP RRFGCLLWQR 

       130        140        150        160        170        180 
DCETHELLAS LGPEPLSAAF TGDYLHALAC GRRAAVKTFL MDQAVVVGVG NIYAAESLHR 

       190        200        210        220        230        240 
AGISPLREAG KVSRERYRRL ADAVKEILAY AIQRGGTTLR DFISPDGAPG YFEQELMVYG 

       250        260        270 
REGEACRHCG GELKHATIGQ RATVWCAACQ R

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE008922 Genomic DNA. Translation: AAM43368.1.
RefSeqNP_639486.1. NC_003902.1.

3D structure databases

ProteinModelPortalQ8P3C4.
SMRQ8P3C4. Positions 2-271.
ModBaseSearch...

Protein-protein interaction databases

STRING190485.XCC4147.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1001170.
KEGGxcc:XCC4147.
PATRIC24079538. VBIXanCam115730_4445.

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020881.
KOK10563.
OMARREKFMN.
ProtClustDBPRK01103.

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]
SUPFAMSSF81624. Form_DNAglyc_cat. 1 hit.
SSF46946. Ribosomal_H2TH. 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_XANCP
AccessionPrimary (citable) accession number: Q8P3C4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 78 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

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