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Q726D5 (FPG_DESVH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 79. 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:DVU_3256
OrganismDesulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) [Reference proteome] [HAMAP]
Taxonomic identifier882 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length365 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 – 365364Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_0000228431

Regions

Zinc finger331 – 36535FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site611Proton donor; for beta-elimination activity By similarity
Active site3551Proton donor; for delta-elimination activity By similarity
Binding site1861DNA By similarity
Binding site2051DNA By similarity
Binding site2461DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q726D5 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: C48C4F917965C4E8

FASTA36539,011
        10         20         30         40         50         60 
MPELPEVETI ACGLRPALSG RRIVGVTVHN PGTLEGPLCT PAAFTEAVQG QRIADVGRRG 

        70         80         90        100        110        120 
KLLLVAFASL PPVGHAGQPR PEGLSSSTVR DFLVTHGFHA AGCATSVHAC APLLADGQQT 

       130        140        150        160        170        180 
RGRLAGHGDG MDGTSRTGST LPGTGGTENS DAVAVADDDT VLGLAFHLKM TGRLFIHPPA 

       190        200        210        220        230        240 
TPAGIHTRVV FDLEGGTRLF FDDARKFGYV RCITRRSLAL WPFWRDLGPE PLETEARGFA 

       250        260        270        280        290        300 
ARLARRRGRI KALLLDQKVV AGVGNIYADE SLFRAGIRPD TQAHTLTPER LFALHGHLQD 

       310        320        330        340        350        360 
VLRESIAECG SSIRDYRDAH GDAGAFQNSF RVYGRGGQPC RHCGTTLATA QVAGRTTVFC 


PQCQR 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017285 Genomic DNA. Translation: AAS97726.1.
RefSeqYP_012466.1. NC_002937.3.

3D structure databases

ProteinModelPortalQ726D5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING882.DVU3256.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS97726; AAS97726; DVU_3256.
GeneID2793859.
KEGGdvu:DVU3256.
PATRIC32066056. VBIDesVul119526_2961.

Phylogenomic databases

eggNOGCOG0266.
KOK10563.
OMAIYCSESL.
OrthoDBEOG6QP131.
PhylomeDBQ726D5.

Enzyme and pathway databases

BioCycDVUL882:GJIL-3341-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. 2 hits.
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_DESVH
AccessionPrimary (citable) accession number: Q726D5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 79 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