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A5D0T6 (FPG_PELTS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:PTH_1977
OrganismPelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI) [Complete proteome] [HAMAP]
Taxonomic identifier370438 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaePelotomaculum

Protein attributes

Sequence length276 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 – 276275Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000075704

Regions

Zinc finger240 – 27435FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site591Proton donor; for beta-elimination activity By similarity
Active site2641Proton donor; for delta-elimination activity By similarity
Binding site931DNA By similarity
Binding site1121DNA By similarity
Binding site1551DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
A5D0T6 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: 1F28EE10AE02C6A2

FASTA27631,388
        10         20         30         40         50         60 
MPELPEVETV RRTLQAKLPG LKITGVEVLL PKVIRSPELS EFKETIADKK ILKVGRRGKY 

        70         80         90        100        110        120 
LLINLSEGYT LAVHLRMTGR LVYCAGQDPP ARHTHVIFNL SNGCQLHFAD MRQFGRIWLV 

       130        140        150        160        170        180 
PTDALDGLKG IKELGVEPLE ELFTREFLKK ELRRRHARIK PLLLDQTFIA GLGNIYADEA 

       190        200        210        220        230        240 
LHRARINPER LATTLTPREI ARLYRAIRDL LQEGIENRGT TVRDFIDGNG QAGNYQEFLQ 

       250        260        270 
VYNREGKPCP RCGDKIAKKK VGGRSSYYCP TCQKVK 

« Hide

References

[1]"The genome of Pelotomaculum thermopropionicum reveals niche-associated evolution in anaerobic microbiota."
Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.
Genome Res. 18:442-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13744 / JCM 10971 / SI.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009389 Genomic DNA. Translation: BAF60158.1.
RefSeqYP_001212527.1. NC_009454.1.

3D structure databases

ProteinModelPortalA5D0T6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING370438.PTH_1977.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF60158; BAF60158; PTH_1977.
GeneID5138110.
KEGGpth:PTH_1977.
PATRIC22911275. VBIPelThe8413_2227.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020885.
KOK10563.
OMAQNTLGMN.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycPTHE370438:GCGQ-2028-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_PELTS
AccessionPrimary (citable) accession number: A5D0T6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: May 14, 2014
This is version 53 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