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A4FMJ7 (FPG_SACEN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. 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:SACE_6099
OrganismSaccharopolyspora erythraea (strain NRRL 23338) [Complete proteome] [HAMAP]
Taxonomic identifier405948 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPseudonocardineaePseudonocardiaceaeSaccharopolyspora

Protein attributes

Sequence length295 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 – 295294Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000008768

Regions

Zinc finger254 – 28835FPG-type HAMAP-Rule MF_00103

Sites

Active site21Schiff-base intermediate with DNA By similarity
Active site31Proton donor By similarity
Active site611Proton donor; for beta-elimination activity By similarity
Active site2781Proton donor; for delta-elimination activity By similarity
Binding site1021DNA By similarity
Binding site1221DNA By similarity
Binding site1681DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
A4FMJ7 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: 92237F8778B13061

FASTA29532,348
        10         20         30         40         50         60 
MPELPEVEVV RRGVAAHVVG RTVSEVEVLH PRSVRRHVPG PDDFATRLAG RCLTAARRRG 

        70         80         90        100        110        120 
KYMWLELGGG PEEVDAGEAV LAHLGMSGQL LVQPDEAPDE THLRVRFRFD DGGPQLRFVD 

       130        140        150        160        170        180 
QRTFGGLSLT ELVSVDGVAV PEPVAHIAPD PLEPVFDLEA AVARMRKRRT GVKRALLDQT 

       190        200        210        220        230        240 
LVSGIGNIYA DEALWRAKLH WARPTANLTR PQARTLLVAA VEVMQAALTA GGTSFDDLYV 

       250        260        270        280        290 
NVNGESGYFD RSLAVYGQAG LPCPRCGTPV RRDAFMNRSS YSCPRCQPTP RNPHY 

« Hide

References

[1]"Complete genome sequence of the erythromycin-producing bacterium Saccharopolyspora erythraea NRRL23338."
Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S., Haydock S.F., Leadlay P.F.
Nat. Biotechnol. 25:447-453(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NRRL 23338.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM420293 Genomic DNA. Translation: CAM05272.1.
RefSeqYP_001108197.1. NC_009142.1.

3D structure databases

ProteinModelPortalA4FMJ7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING405948.SACE_6099.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM05272; CAM05272; SACE_6099.
GeneID4945828.
KEGGsen:SACE_6099.
PATRIC23419566. VBISacEry28377_6073.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020884.
KOK10563.
OMARREKFMN.
OrthoDBEOG6QP131.
ProtClustDBPRK01103.

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_SACEN
AccessionPrimary (citable) accession number: A4FMJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: April 17, 2007
Last modified: February 19, 2014
This is version 53 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