Q74IB5 (FPG_LACJO) 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:	mutM
Synonyms:	fpg
Ordered Locus Names:	LJ_1650

Organism

Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533) [Complete proteome] [HAMAP]

Taxonomic identifier

257314 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Lactobacillales › Lactobacillaceae › Lactobacillus › Lactobacillus johnsonii

Protein attributes

Sequence length	276 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. 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.
Subunit structure	Monomer By similarity.
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
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 – 276	275	Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103		PRO_0000228441
Regions
	Zinc finger	239 – 273	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	58	1	Proton donor; for beta-elimination activity By similarity
	Active site	263	1	Proton donor; for delta-elimination activity By similarity
	Binding site	92	1	DNA By similarity
	Binding site	111	1	DNA By similarity
	Binding site	154	1	DNA By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q74IB5 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 625D83B82E23ADDE	FASTA	276	31,484
	10 20 30 40 50 60 MPEMPEVETV RRTLTPLVKG KTIAKIIIWY PKIIVNNPDE FVEKLTNKKI LKIDRYGKYL 70 80 90 100 110 120 LFRFSDDLTM VSHLRMEGKY HLVTPDHPKG KHEHVEFVFT DGTALRYADV RKFGRMHLVE 130 140 150 160 170 180 TGTEKQTTGI RHLGPEPNTE EFSVEYFINA LSRKKKNIKN TLLDQTVVCG LGNIYVDEVL 190 200 210 220 230 240 WQSKIHPLSS AKSIPADKIV DLYHNINHTI TVATKERGTT VHTYLDANGD IGGYQNMLQV 250 260 270 YGHAGEECNN CGTILEKIKV NGRGTTFCPH CQVLYK

References

[1]

"The genome sequence of the probiotic intestinal bacterium Lactobacillus johnsonii NCC 533." Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C., Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R., Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A. Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CNCM I-1225 / La1 / NCC 533.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017198 Genomic DNA. Translation: AAS09423.1.
RefSeq	NP_965457.1. NC_005362.1.
3D structure databases
ProteinModelPortal	Q74IB5.
ModBase	Search...
Protein-protein interaction databases
STRING	257314.LJ1650.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2742963.
KEGG	ljo:LJ1650.
PATRIC	22239603. VBILacJoh1832_1476.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0266.
KO	K10563.
OMA	VLRYNDP.
ProtClustDB	PRK01103.
Enzyme and pathway databases
BioCyc	LJOH257314:GJN3-1469-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_LACJO

Accession

Primary (citable) accession number: Q74IB5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 72 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program