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C0MAN8 (C0MAN8_STRE4) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 36. 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:SEQ_1610 EMBL CAW94602.1
OrganismStreptococcus equi subsp. equi (strain 4047) [Complete proteome] [HAMAP] EMBL CAW94602.1
Taxonomic identifier553482 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length297 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 SAAS000214

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 SAAS000214

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 SAAS000214

Cofactor

Binds 1 zinc ion per subunit By similarity. HAMAP-Rule MF_00103 SAAS SAAS000214

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00103 SAAS SAAS000214

Sequence similarities

Belongs to the FPG family. HAMAP-Rule MF_00103

Contains 1 FPG-type zinc finger. HAMAP-Rule MF_00103 SAAS SAAS000214

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Zinc finger262 – 29635FPG-type By similarity HAMAP-Rule MF_00103

Sites

Active site261Schiff-base intermediate with DNA By similarity HAMAP-Rule MF_00103
Active site271Proton donor By similarity HAMAP-Rule MF_00103
Active site821Proton donor; for beta-elimination activity By similarity HAMAP-Rule MF_00103
Active site2861Proton donor; for delta-elimination activity By similarity HAMAP-Rule MF_00103
Binding site1151DNA By similarity HAMAP-Rule MF_00103
Binding site1341DNA By similarity HAMAP-Rule MF_00103

Sequences

Sequence LengthMass (Da)Tools
C0MAN8 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: A53799720C138B42

FASTA29733,342
        10         20         30         40         50         60 
MLKLAGSAGF GYVVSLLARL VSLIMPELPE VETVRRGLER LVVGKQIAAV TVRVPKMVKT 

        70         80         90        100        110        120 
DLEHFVMTIP GQQVQGVDRR GKYLLFDFGQ LVMISHLRME GKYLLFPDTV PEHKHFHVFL 

       130        140        150        160        170        180 
TMTDGSTLVY QDVRKFGTFD LLPKAELAAF FQKRQLGPEP TKQTFQLKTF EAALLASKKT 

       190        200        210        220        230        240 
IKPHLLDQTL VAGLGNIYVD EVLWAARVHP ERRSASLKKA EIKRIHDETI RILQLGIEKG 

       250        260        270        280        290 
GSTVRTYQNT LGMNGSMQHY LMVYGQTGKP CQRCGTSIVK LKVGGRGTHV CPRCQKQ

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References

[1]"Genomic evidence for the evolution of Streptococcus equi: host restriction, increased virulence, and genetic exchange with human pathogens."
Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A. expand/collapse author list , Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J., Waller A.S.
PLoS Pathog. 5:e1000346-e1000346(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 4047 EMBL CAW94602.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM204883 Genomic DNA. Translation: CAW94602.1.
RefSeqYP_002746858.1. NC_012471.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING553482.SEQ_1610.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW94602; CAW94602; SEQ_1610.
GeneID7697031.
KEGGseu:SEQ_1610.
PATRIC19648051. VBIStrEqu13040_1640.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020885.
KOK10563.
OMARREKFMN.
ProtClustDBPRK01103.

Enzyme and pathway databases

BioCycSEQU553482:GJOY-1593-MONOMER.

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]
SUPFAMSSF81624. Form_DNAglyc_cat. 1 hit.
SSF46946. Ribosomal_H2TH. 1 hit.
TIGRFAMsTIGR00577. fpg. 1 hit.
PROSITEPS51068. FPG_CAT. 1 hit.
PS51066. ZF_FPG_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameC0MAN8_STRE4
AccessionPrimary (citable) accession number: C0MAN8
Entry history
Integrated into UniProtKB/TrEMBL: May 5, 2009
Last sequence update: May 5, 2009
Last modified: May 1, 2013
This is version 36 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