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Q73VL9 (FPG_MYCPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. 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:MAP_2994c
OrganismMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) [Complete proteome] [HAMAP]
Taxonomic identifier262316 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length283 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 – 283282Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_0000228448

Regions

Zinc finger245 – 27935FPG-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 site2691Proton donor; for delta-elimination activity By similarity
Binding site941DNA By similarity
Binding site1131DNA By similarity
Binding site1591DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
Q73VL9 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: EC0B7AD3B2B4AEE2

FASTA28331,164
        10         20         30         40         50         60 
MPELPEVEVV RRGLHAHVVG KTIGAVRVHH PRAVRRHEAG PADLTARLLG ARITGTDRRG 

        70         80         90        100        110        120 
KYLWLLLDGC DTALVVHLGM SGQMLLGAVP RAEHVRISAL LDDGTVLSFA DQRTFGGWML 

       130        140        150        160        170        180 
ADLLEVDGSI LPRPVAHLAR DPLDPRFDAA AVVKVLRRKH SEIKRQLLDQ QVVSGIGNIY 

       190        200        210        220        230        240 
ADEALWRAKV HGARIAATMT GRQLTAVLDA AAEVMRDALA QGGTSFDSLY VNVNGESGYF 

       250        260        270        280 
DRSLDAYGRE GESCRRCGAV MRREKFMNRS SFYCPKCQPR PRL 

« Hide

References

[1]"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-968 / K-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016958 Genomic DNA. Translation: AAS05311.1.
RefSeqNP_961928.1. NC_002944.2.

3D structure databases

ProteinModelPortalQ73VL9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262316.MAP2994c.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS05311; AAS05311; MAP_2994c.
GeneID2721442.
KEGGmpa:MAP2994c.
PATRIC17998722. VBIMycAvi108102_3171.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
KOK10563.
OMAREGESCR.
OrthoDBEOG6QP131.

Enzyme and pathway databases

BioCycMAVI262316:GCQR-3034-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_MYCPA
AccessionPrimary (citable) accession number: Q73VL9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 77 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