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B0VRV3 (FPG_ACIBS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. 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:ABSDF0616
OrganismAcinetobacter baumannii (strain SDF) [Complete proteome] [HAMAP]
Taxonomic identifier509170 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacterAcinetobacter calcoaceticus/baumannii complex

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_1000094025

Regions

Zinc finger233 – 26735FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site561Proton donor; for beta-elimination activity By similarity
Active site2571Proton donor; for delta-elimination activity By similarity
Binding site891DNA By similarity
Binding site1071DNA By similarity
Binding site1481DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
B0VRV3 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: F39A3B282DD6096E

FASTA27431,164
        10         20         30         40         50         60 
MPELPEVETT KTSLFPLLNQ KVLSVEVRNP SLRWPIPDNV QKLVGQRLIG LNRRSKYILA 

        70         80         90        100        110        120 
EFEQDQMLWH LGMSGSFRLC QPNDELRKHD HLIIQFEDQQ LRYHDPRRFG CILWLNPETQ 

       130        140        150        160        170        180 
GKLIDTLGPE PLSTDFHAEY LASKLKNKSV GIKIALMDNH VVVGVGNIYA TESLFNVGIH 

       190        200        210        220        230        240 
PAQPAGDLTM QQIEKLVVEI KRILKSAIDL GGSTLRDYSN AMGENGYFQQ TLLAYGRARE 

       250        260        270 
MCVNCETTLE NLKLGQRASV FCPQCQPLKK LRKP 

« Hide

References

[1]"Comparative analysis of Acinetobacters: three genomes for three lifestyles."
Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S.
PLoS ONE 3:E1805-E1805(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SDF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU468230 Genomic DNA. Translation: CAO99994.1.
RefSeqYP_001706240.1. NC_010400.1.

3D structure databases

ProteinModelPortalB0VRV3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING509170.ABSDF0616.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAO99994; CAO99994; ABSDF0616.
GeneID5987178.
KEGGabm:ABSDF0616.
PATRIC20732181. VBIAciBau88365_0622.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020881.
KOK10563.
OMAGKYHLTT.
OrthoDBEOG6QP131.
ProtClustDBCLSK707047.

Family and domain databases

HAMAPMF_00103. Fapy_DNA_glycosyl.
InterProIPR015886. DNA_glyclase/AP_lyase_DNA-bd.
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.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFPG_ACIBS
AccessionPrimary (citable) accession number: B0VRV3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: April 8, 2008
Last modified: February 19, 2014
This is version 46 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