A0QV21 (FPG_MYCS2) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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:	fpg
Synonyms:	mutM
Ordered Locus Names:	MSMEG_2419, MSMEI_2358

Organism

Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Reference proteome] [HAMAP]

Taxonomic identifier

246196 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium smegmatis

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred 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. Acts on oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) when paired with C, G or T. 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. Ref.4
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.
Subunit structure	Monomer By similarity.
Disruption phenotype	Loss of excision of 8-oxoG from dsDNA. No significant growth in the presence of 3 mM H2O2. 4-fold increase in mutation frequency upon plating on rifampicin (mutator phenotype); an increase in A to G and C to G mutations is seen. Ref.4
Sequence similarities	Belongs to the FPG family. Contains 1 FPG-type zinc finger.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Glycosidase Hydrolase Lyase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	base-excision repair Inferred from electronic annotation. Source: InterPro nucleotide-excision repair Inferred from electronic annotation. Source: InterPro
Molecular_function	damaged DNA binding Inferred from electronic annotation. Source: InterPro oxidized purine nucleobase lesion DNA N-glycosylase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 285	284	Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103		PRO_1000008719
Regions
	Zinc finger	244 – 278	35	FPG-type HAMAP-Rule MF_00103
Sites
	Active site	2	1	Schiff-base intermediate with DNA By similarity
	Active site	3	1	Proton donor By similarity
	Active site	61	1	Proton donor; for beta-elimination activity By similarity
	Active site	268	1	Proton donor; for delta-elimination activity By similarity
	Binding site	93	1	DNA By similarity
	Binding site	112	1	DNA By similarity
	Binding site	158	1	DNA By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0QV21 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: E4D4A1C572CCBC99	FASTA	285	31,669
	10 20 30 40 50 60 MPELPEVEVV RRGLAEHVTG KTITGVRVHH PRAVRRHEAG PADLTARLLD VRITGTGRRG 70 80 90 100 110 120 KYLWLTLDDS AALVVHLGMS GQMLLGPIRD TRHLRIAAVL DDGTALSFVD QRTFGGWQLT 130 140 150 160 170 180 EMVTVDGTDV PEPVAHIARD PLDPLFDRDR VVTVLRGKHS EIKRQLLDQT VVSGIGNIYA 190 200 210 220 230 240 DEALWRTKIN GARIAAALPR RRLAELLDAA AEVMTDALGQ GGTSFDSLYV NVNGESGYFD 250 260 270 280 RSLDAYGREG EPCRRCGAIM RREKFMNRSS FYCPRCQPRP RVPRV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155.
[2]	"Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?" Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M. Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155.
[3]	"Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol." Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O. Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700084 / mc(2)155.
[4]	"A distinct role of formamidopyrimidine DNA glycosylase (MutM) in down-regulation of accumulation of G, C mutations and protection against oxidative stress in mycobacteria." Jain R., Kumar P., Varshney U. DNA Repair 6:1774-1785(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE. Strain: ATCC 700084 / mc(2)155.
[5]	"Base excision and nucleotide excision repair pathways in mycobacteria." Kurthkoti K., Varshney U. Tuberculosis 91:533-543(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000480 Genomic DNA. Translation: ABK72450.1. CP001663 Genomic DNA. Translation: AFP38826.1.
RefSeq	YP_006567121.1. NC_018289.1. YP_886759.1. NC_008596.1.
3D structure databases
ProteinModelPortal	A0QV21.
ModBase	Search...
Protein-protein interaction databases
STRING	246196.MSMEG_2419.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000043728; EBMYCP00000042065; EBMYCG00000043723.
GeneID	13428875. 4537159.
KEGG	msg:MSMEI_2358. msm:MSMEG_2419.
PATRIC	18077264. VBIMycSme59918_2384.
Phylogenomic databases
eggNOG	COG0266.
HOGENOM	HOG000020884.
KO	K10563.
OMA	RREKFMN.
ProtClustDB	PRK01103.
Enzyme and pathway databases
BioCyc	MSME246196:GJ4Y-2419-MONOMER.
Family and domain databases
HAMAP	MF_00103. Fapy-DNA_glycosyl.
InterPro	IPR015886. 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]
Pfam	PF01149. Fapy_DNA_glyco. 1 hit. PF06831. H2TH. 1 hit. PF06827. zf-FPG_IleRS. 1 hit. [Graphical view]
SMART	SM00898. Fapy_DNA_glyco. 1 hit. [Graphical view]
SUPFAM	SSF81624. Form_DNAglyc_cat. 1 hit. SSF46946. Ribosomal_H2TH. 1 hit.
TIGRFAMs	TIGR00577. fpg. 1 hit.
PROSITE	PS51068. FPG_CAT. 1 hit. PS01242. ZF_FPG_1. 1 hit. PS51066. ZF_FPG_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FPG_MYCS2

Accession

Primary (citable) accession number: A0QV21
Secondary accession number(s): I7G6H6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 9, 2007
Last modified:	May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program