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C6BUX8 (FPG_DESAD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 32. 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:Desal_0043
OrganismDesulfovibrio salexigens (strain ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763) [Complete proteome] [HAMAP]
Taxonomic identifier526222 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfovibrionalesDesulfovibrionaceaeDesulfovibrio

Protein attributes

Sequence length274 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 – 274273Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000202822

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
C6BUX8 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: CF79EA1EF0FF42DC

FASTA27430,222
        10         20         30         40         50         60 
MPELPEVEVI SRGLAESLEG KTIESVKILN HSSVKMPWYL FSSRVAGEKI TRIHRRAKLL 

        70         80         90        100        110        120 
IMDLGDDLHI TFHLKMTGRV LAHEGPTTPE PHTRIVFGLT DGGSIEFHDT RKFGEVRALN 

       130        140        150        160        170        180 
NEELQEWDFY KNLGPEPLEV TAEELAERIT GRKAQIKGLL LNQSVVAGCG NIYADESLFR 

       190        200        210        220        230        240 
SGIHPKAKAS DLSNESLVKL FTELQAVLKQ AIQENGSSIR DYVDAGGDAG GFQNSFKVYG 

       250        260        270 
KKGEPCPDCG KIFEGATVAG RTSTFCSNCQ KMKD 

« Hide

References

[1]"Complete sequence of Desulfovibrio salexigens DSM 2638."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Anderson I. expand/collapse author list , Wall J.D., Arkin A.P., Dehal P., Chivian D., Giles B., Hazen T.C.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 14822 / DSM 2638 / NCIB 8403 / VKM B-1763.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001649 Genomic DNA. Translation: ACS78115.1.
RefSeqYP_002989654.1. NC_012881.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING526222.Desal_0043.

Proteomic databases

PRIDEC6BUX8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS78115; ACS78115; Desal_0043.
GeneID8092184.
KEGGdsa:Desal_0043.
PATRIC21755519. VBIDesSal121003_0044.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020885.
KOK10563.
OMAIYCSESL.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycDSAL526222:GHES-45-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_DESAD
AccessionPrimary (citable) accession number: C6BUX8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: May 14, 2014
This is version 32 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