Reviewed, UniProtKB/Swiss-Prot Q0VLB7 (FPG_ALCBS)

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:	ABO_2583

Organism

Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573) [Complete proteome] [HAMAP]

Taxonomic identifier

393595 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Oceanospirillales › Alcanivoracaceae › Alcanivorax

Protein attributes

Sequence length	269 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 – 269	268	Formamidopyrimidine-DNA glycosylase HAMAP MF_00103		PRO_1000008672
Regions
	Zinc finger	235 – 269	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	57	1	Proton donor; for beta-elimination activity By similarity
	Active site	259	1	Proton donor; for delta-elimination activity By similarity
	Binding site	90	1	DNA By similarity
	Binding site	109	1	DNA By similarity
	Binding site	150	1	DNA By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q0VLB7-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 155B4CF37AE56CFA	FASTA	269	29,903
	10 20 30 40 50 60 MPELPEVETT LRGIRPHLQG RILKSVTVRE PRLRWPVSEA IYALRDCPVV ALRRRAKYLL 70 80 90 100 110 120 IELEHGQLLI HLGMSGTLRV VDMDLPLRKH DHVDLLLDSG KVLRFNDPRR FGSVLFQGGD 130 140 150 160 170 180 QPHSLLQSLG PEPLSDSFNG QWLFARSRGR KVAVKSFIMD NATVVGVGNI YAQESLFMAG 190 200 210 220 230 240 IHPSRAAGRI SLARYQALAE AIKRVLAQAI EAGGTTLKDF TRADGQPGYF AQSLNVYGRA 250 260 GQPCVQCDAI LKADRHGQRS TAYCPQCQR

References

[1]

"Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium Alcanivorax borkumensis." Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B., McHardy A.C., Meyer F. , Nechitaylo T., Puehler A., Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N. Nat. Biotechnol. 24:997-1004(2006) [PubMed: 16878126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM286690 Genomic DNA. Translation: CAL18031.1.
RefSeq	YP_694303.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	4211249.
GenomeReviews	Gene locus ABO_2583 in contig AM286690_GR.
KEGG	abo:ABO_2583.
NMPDR	fig|393595.12.peg.2590.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0VLB7.
OMA	Q0VLB7. RMTGQLL.
Enzyme and pathway databases
BioCyc	ABOR393595:ABO_2583-MON.
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_ALCBS

Accession

Primary (citable) accession number: Q0VLB7

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	June 16, 2009
This is version 26 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)