Skip Header

Contribute Send feedback
Read comments (?) or add your own

G2S8V3 (G2S8V3_ENTAL) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 11. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

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:Entas_0113 EMBL AEN62868.1
OrganismEnterobacter asburiae (strain LF7a) [Complete proteome] [HAMAP]
Taxonomic identifier640513 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Enterobacter › Enterobacter cloacae complex ›

Protein attributes

Sequence length269 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 SAAS015886

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 SAAS015886

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 SAAS015886

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00103 SAAS SAAS015886

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00103 SAAS SAAS015886

Sequence similarities

Belongs to the FPG family. HAMAP-Rule MF_00103

Contains 1 FPG-type zinc finger. HAMAP-Rule MF_00103 SAAS SAAS015886

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Zinc finger235 – 26935FPG-type By similarity HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity HAMAP-Rule MF_00103
Active site31Proton donor By similarity HAMAP-Rule MF_00103
Active site571Proton donor; for beta-elimination activity By similarity HAMAP-Rule MF_00103
Active site2591Proton donor; for delta-elimination activity By similarity HAMAP-Rule MF_00103
Binding site901DNA By similarity HAMAP-Rule MF_00103
Binding site1091DNA By similarity HAMAP-Rule MF_00103
Binding site1501DNA By similarity HAMAP-Rule MF_00103

Sequences

Sequence LengthMass (Da)Tools
G2S8V3 [UniParc].

Last modified November 16, 2011. Version 1.
Checksum: 6E4B3EB1E1BE1A6E

FASTA26930,129
        10         20         30         40         50         60 
MPELPEVETS RRGIEPHLVG ATILHAVVRN GRLRWPVSDE IHALSDKPIL SVQRRAKYLL 

        70         80         90        100        110        120 
LELPDGWIII HLGMSGSLRI LSEELPAEKH DHVDLVMSNG KVLRYTDPRR FGAWLWTKEL 

       130        140        150        160        170        180 
EGHSVLAHLG PEPLSDAFNA DYLKEKCAKK KTPIKPWLMD NKLVVGVGNI YASESLFAAG 

       190        200        210        220        230        240 
IHPDRLASSL SPQECELLVR VIKAVLLRSI EQGGTTLKDF LQSDGKPGYF AQELQVYGRK 

       250        260 
GEPCRVCGTP IIATKHAQRA TFYCRQCQK

« Hide

References

[1]"Complete sequence of chromosome of Enterobacter asburiae LF7a."
Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., van der Lelie D., Woyke T.
Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LF7a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP003026 Genomic DNA. Translation: AEN62868.1.
RefSeqYP_004826653.1. NC_015968.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEN62868; AEN62868; Entas_0113.
GeneID11111665.
KEGGeas:Entas_0113.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK10563.
OMAVLRYNDP.

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 nameG2S8V3_ENTAL
AccessionPrimary (citable) accession number: G2S8V3
Entry history
Integrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: May 1, 2013
This is version 11 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info