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C1AG40 (FPG_MYCBT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 37. 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:JTY_2941
OrganismMycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019) [Complete proteome] [HAMAP]
Taxonomic identifier561275 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length289 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 – 289288Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103
PRO_1000118896

Regions

Zinc finger251 – 28535FPG-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 site2751Proton donor; for delta-elimination activity By similarity
Binding site1001DNA By similarity
Binding site1191DNA By similarity
Binding site1651DNA By similarity

Sequences

Sequence LengthMass (Da)Tools
C1AG40 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: E00B94A70DC2904E

FASTA28931,951
        10         20         30         40         50         60 
MPELPEVEVV RRGLQAHVTG RTITEVRVHH PRAVRRHDAG PADLTARLRG ARINGTDRRG 

        70         80         90        100        110        120 
KYLWLTLNTA GVHRPTDTAL VVHLGMSGQM LLGAVPCAAH VRISALLDDG TVLSFADQRT 

       130        140        150        160        170        180 
FGGWLLADLV TVDGSVVPVP VAHLARDPLD PRFDCDAVVK VLRRKHSELK RQLLDQRVVS 

       190        200        210        220        230        240 
GIGNIYADEA LWRAKVNGAH VAATLRCRRL GAVLHAAADV MREALAKGGT SFDSLYVNVN 

       250        260        270        280 
GESGYFERSL DAYGREGENC RRCGAVIRRE RFMNRSSFYC PRCQPRPRK 

« Hide

References

[1]"Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains."
Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.
Vaccine 27:1710-1716(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BCG / Tokyo 172 / ATCC 35737 / TMC 1019.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP010918 Genomic DNA. Translation: BAH27219.1.
RefSeqYP_002645987.1. NC_012207.1.

3D structure databases

ProteinModelPortalC1AG40.
SMRC1AG40. Positions 2-284.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561275.JTY_2941.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH27219; BAH27219; JTY_2941.
GeneID7563821.
KEGGmbt:JTY_2941.
PATRIC18025685. VBIMycBov85238_3208.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0266.
HOGENOMHOG000020884.
KOK10563.
OMARCATPIE.
OrthoDBEOG6QP131.
ProtClustDBPRK01103.

Enzyme and pathway databases

BioCycMBOV561275:GHDN-2974-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_MYCBT
AccessionPrimary (citable) accession number: C1AG40
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: February 19, 2014
This is version 37 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