Reviewed, UniProtKB/Swiss-Prot B0VRV3 (FPG_ACIBS)

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:	ABSDF0616

Organism

Acinetobacter baumannii (strain SDF) [Complete proteome] [HAMAP]

Taxonomic identifier

509170 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

Protein attributes

Sequence length	274 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.
Catalytic activity	Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine. HAMAP 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 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 base lesion DNA N-glycosylase activity Inferred from electronic annotation. Source: HAMAP zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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 – 274	273	Formamidopyrimidine-DNA glycosylase HAMAP MF_00103		PRO_1000094025
Regions
	Zinc finger	233 – 267	35	FPG-type HAMAP MF_00103
Sites
	Active site	2	1	Schiff-base intermediate with DNA By similarity
	Active site	3	1	Proton donor By similarity
	Active site	56	1	Proton donor; for beta-elimination activity By similarity
	Active site	257	1	Proton donor; for delta-elimination activity By similarity
	Binding site	89	1	DNA By similarity
	Binding site	107	1	DNA By similarity
	Binding site	148	1	DNA By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0VRV3-1 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: F39A3B282DD6096E	FASTA	274	31,164
	10 20 30 40 50 60 MPELPEVETT KTSLFPLLNQ KVLSVEVRNP SLRWPIPDNV QKLVGQRLIG LNRRSKYILA 70 80 90 100 110 120 EFEQDQMLWH LGMSGSFRLC QPNDELRKHD HLIIQFEDQQ LRYHDPRRFG CILWLNPETQ 130 140 150 160 170 180 GKLIDTLGPE PLSTDFHAEY LASKLKNKSV GIKIALMDNH VVVGVGNIYA TESLFNVGIH 190 200 210 220 230 240 PAQPAGDLTM QQIEKLVVEI KRILKSAIDL GGSTLRDYSN AMGENGYFQQ TLLAYGRARE 250 260 270 MCVNCETTLE NLKLGQRASV FCPQCQPLKK LRKP

References

[1]

"Comparative analysis of Acinetobacters: three genomes for three lifestyles." Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S. PLoS ONE 3:E1805-E1805(2008) [PubMed: 18350144] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU468230 Genomic DNA. Translation: CAO99994.1.
RefSeq	YP_001706240.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5987178.
GenomeReviews	Gene locus ABSDF0616 in contig CU468230_GR.
KEGG	abm:ABSDF0616.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	ANESLFR.
Family and domain databases
HAMAP	MF_00103. [Tree]
InterPro	IPR015886. DNA_glyclase/AP_lyase_DNA-bd. IPR000214. DNA_glyclase/AP_lyase_Znf_dom. IPR015887. DNA_glyclase_Znf_dom_DNA_BS. IPR000191. DNA_glycosylase/AP_lyase. IPR012319. DNA_glycosylase/AP_lyase_cat. [Graphical view]
Pfam	PF01149. Fapy_DNA_glyco. 1 hit. PF06831. H2TH. 1 hit. [Graphical view]
ProDom	PD003680. Fapy_DNA_glyco. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00577. fpg. 1 hit.
PROSITE	PS51068. FPG_CAT. 1 hit. PS01242. ZF_FPG_1. False negative. PS51066. ZF_FPG_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FPG_ACIBS

Accession

Primary (citable) accession number: B0VRV3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	April 8, 2008
Last modified:	November 3, 2009
This is version 17 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)