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B4TZX7 (FPG_SALSV) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 38. 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:SeSA_A3925
OrganismSalmonella schwarzengrund (strain CVM19633) [Complete proteome] [HAMAP]
Taxonomic identifier439843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length269 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 – 269268Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000094077

Regions

Zinc finger235 – 26935FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site571Proton donor; for beta-elimination activity By similarity
Active site2591Proton donor; for delta-elimination activity By similarity
Binding site901DNA By similarity
Binding site1091DNA By similarity
Binding site1501DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
B4TZX7 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 72BC9945527AC3E9

FASTA26930,223
        10         20         30         40         50         60 
MPELPEVETS RRGIEPHLVG ATILHAHIRN GRLRWPVSDE IYRLSDTPVL SVQRRAKYLL 

        70         80         90        100        110        120 
LELPDGWIII HLGMSGSLRI LSEALPAEKH DHVDLVMSNG KILRYTDPRR FGAWLWTKEL 

       130        140        150        160        170        180 
EGHNVLAHLG PEPLSDEFNG EYLQQKCAKK KTAIKPWLMD NKLVVGVGNI YASESLFAAG 

       190        200        210        220        230        240 
IHPDRLASSL STEECDLLAR VIKAVLLRSI EQGGTTLKDF LQSDGKPGYF AQELQVYGRK 

       250        260 
GEPCRVCGTP IVATKHAQRA TFYCRHCQK 

« Hide

References

[1]"Comparative genomics of 28 Salmonella enterica isolates: evidence for CRISPR-mediated adaptive sublineage evolution."
Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G., Leclerc J.E., Ravel J., Cebula T.A.
J. Bacteriol. 193:3556-3568(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CVM19633.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001127 Genomic DNA. Translation: ACF89194.1.
RefSeqYP_002116661.1. NC_011094.1.

3D structure databases

ProteinModelPortalB4TZX7.
SMRB4TZX7. Positions 2-269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439843.SeSA_A3925.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF89194; ACF89194; SeSA_A3925.
PATRIC32376427. VBISalEnt87589_3920.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020881.
OMADHVDLKL.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycSENT439843:GHHR-590-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_SALSV
AccessionPrimary (citable) accession number: B4TZX7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 38 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