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C9R209 (C9R209_AGGAD) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103

Short name=Fapy-DNA glycosylase HAMAP-Rule MF_00103
EC=3.2.2.23 HAMAP-Rule MF_00103
Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase MutM HAMAP-Rule MF_00103
Gene names
Name:mutM HAMAP-Rule MF_00103
Synonyms:fpg HAMAP-Rule MF_00103
Ordered Locus Names:D11S_0435
OrganismAggregatibacter actinomycetemcomitans serotype C (strain D11S-1) (Actinobacillus actinomycetemcomitans) [Complete proteome] [HAMAP] EMBL ACX81845.1
Taxonomic identifier668336 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeAggregatibacter

Protein attributes

Sequence length285 AA.
Sequence statusComplete.
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 SAAS SAAS015887

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 SAAS SAAS015887

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 SAAS SAAS015887

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00103 SAAS SAAS015887

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00103 SAAS SAAS015887

Sequence similarities

Belongs to the FPG family. HAMAP-Rule MF_00103

Contains 1 FPG-type zinc finger. HAMAP-Rule MF_00103 SAAS SAAS015887

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Zinc finger249 – 28335FPG-type By similarity HAMAP-Rule MF_00103

Sites

Active site161Schiff-base intermediate with DNA By similarity HAMAP-Rule MF_00103
Active site171Proton donor By similarity HAMAP-Rule MF_00103
Active site711Proton donor; for beta-elimination activity By similarity HAMAP-Rule MF_00103
Active site2731Proton donor; for delta-elimination activity By similarity HAMAP-Rule MF_00103
Binding site1041DNA By similarity HAMAP-Rule MF_00103
Binding site1231DNA By similarity HAMAP-Rule MF_00103
Binding site1641DNA By similarity HAMAP-Rule MF_00103

Sequences

Sequence LengthMass (Da)Tools
C9R209 [UniParc].

Last modified November 24, 2009. Version 1.
Checksum: F6B215D9B015C127

FASTA28532,441
        10         20         30         40         50         60 
MYQYFPAPRI LEKEMPELPE VETAVRGVSP YLKDYVIEKI VVRQPKLRWA VSPELAELHH 

        70         80         90        100        110        120 
VKILDLTRRA KYLVIHTEQG YIIGHLGMSG TVRIVFHGSP IDKHDHLDIV VNNGKLLRYN 

       130        140        150        160        170        180 
DPRRFGAWLW TEKLDEFHLF LKLGPEPLSE EFNAEYLFKK LHKKTTALKT VLMDNTVVVG 

       190        200        210        220        230        240 
IGNIYANESL FLCGLHPLKL AANLTRKQCE RLVDTIKSVL AKAIEQGGTT LKDFLQPDGR 

       250        260        270        280 
PGYFAQELLV YGNKGKPCPK CGTKIESLVI GQRNSFYCPT CQKKG 

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References

[1]"Genome sequence of Aggregatibacter actinomycetemcomitans serotype c strain D11S-1."
Chen C., Kittichotirat W., Si Y., Bumgarner R.
J. Bacteriol. 191:7378-7379(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: D11S-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001733 Genomic DNA. Translation: ACX81845.1.
RefSeqYP_003255064.1. NC_013416.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING668336.D11S_0435.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACX81845; ACX81845; D11S_0435.
GeneID8536154.
KEGGaat:D11S_0435.
PATRIC31911649. VBIAggAct139153_0404.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020881.
KOK10563.
OMAVLRYNDP.

Enzyme and pathway databases

BioCycAACT668336:GJBF-434-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]
SUPFAMSSF81624. Form_DNAglyc_cat. 1 hit.
SSF46946. Ribosomal_H2TH. 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 nameC9R209_AGGAD
AccessionPrimary (citable) accession number: C9R209
Entry history
Integrated into UniProtKB/TrEMBL: November 24, 2009
Last sequence update: November 24, 2009
Last modified: May 1, 2013
This is version 30 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)