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Q9KVC5 (FPG_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 87. 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:VC_0221
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

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_0000170882

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
Q9KVC5 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 677A73179E5F8887

FASTA26930,037
        10         20         30         40         50         60 
MPELPEVEVS RLGISPHLVG GTIQSLVLRT PKLRWPIPQE LKQLEGQTIL AIHRRAKYLI 

        70         80         90        100        110        120 
IETAVGSAIV HLGMSGSLRI LDGDFPAAKH DHVDLVMTSG KRLRYNDPRR FGAWLWCAPD 

       130        140        150        160        170        180 
ESHEVLGRLG PEPLTEAFNA EYMMDKARNK RIAVKAFIMD NAAVVGVGNI YANESLFTSR 

       190        200        210        220        230        240 
LHPLRPAHSL SLEEWQTLVA NIKQVLQVAI KQGGTTLKDF TQSDGKPGYF AQELQVYGKA 

       250        260 
KQPCPHCGEP LCEQKIAQRN TFFCPQCQH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF93397.1.
PIRG82347.
RefSeqNP_229878.1. NC_002505.1.

3D structure databases

ProteinModelPortalQ9KVC5.
SMRQ9KVC5. Positions 2-269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC0221.

Protocols and materials databases

DNASU2614281.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF93397; AAF93397; VC_0221.
GeneID2614281.
KEGGvch:VC0221.
PATRIC20079488. VBIVibCho83274_0203.

Phylogenomic databases

eggNOGCOG0266.
KOK10563.
OMADHVDLKL.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycVCHO:VC0221-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_VIBCH
AccessionPrimary (citable) accession number: Q9KVC5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 87 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