Q6G0L3 (FPG_BARQU) 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:	BQ02370

Organism

Bartonella quintana (strain Toulouse) (Rochalimaea quintana) [Complete proteome] [HAMAP]

Taxonomic identifier

283165 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella › Bartonella quintana

Protein attributes

Sequence length	291 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 – 291	290	Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103		PRO_0000228417
Regions
	Zinc finger	257 – 291	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	281	1	Proton donor; for delta-elimination activity By similarity
	Binding site	100	1	DNA By similarity
	Binding site	123	1	DNA By similarity
	Binding site	166	1	DNA By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6G0L3 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E1E27C324ECB5C27	FASTA	291	33,117
	10 20 30 40 50 60 MPELPEVETV RRGLEPVITG AKIISITLNR RDLRFPFPEA FSERLVGRTI MELGRRGKYL 70 80 90 100 110 120 LFHLSQNETI LSHLGMSGSW RIEDDLLRKT YSAAGKFVKH DHFLMDIQAK DGKVYHLTYN 130 140 150 160 170 180 DVRRFGFMLL LDTNRIYEHP LLKKLGLEPL SNEFSGRYLQ EAFVNKKISL KGVLLDQSII 190 200 210 220 230 240 AGLGNIYVCE ALWRSRLSPQ RGAFTLALKT VCAREFADSL AQNIRNVIAE AISFGGSTLR 250 260 270 280 290 DYIRTDGSLG YFQHSFSVYG REGKECFQCG IPITRISQSG RSSFYCSQCQ K

References

[1]

"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Toulouse.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX897700 Genomic DNA. Translation: CAF25740.1.
RefSeq	YP_031941.1. NC_005955.1.
3D structure databases
ProteinModelPortal	Q6G0L3.
ModBase	Search...
Protein-protein interaction databases
STRING	283165.BQ02370.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2866609.
KEGG	bqu:BQ02370.
PATRIC	31951677. VBIBarQui58630_0278.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0266.
HOGENOM	HOG000020881.
KO	K10563.
OMA	VLRYNDP.
ProtClustDB	PRK01103.
Enzyme and pathway databases
BioCyc	BQUI283165:GHZA-425-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_BARQU

Accession

Primary (citable) accession number: Q6G0L3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 66 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program