Reviewed, UniProtKB/Swiss-Prot Q3MDP1 (FPG_ANAVT)

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:	Ava_1271

Organism

Anabaena variabilis (strain ATCC 29413 / PCC 7937) [Complete proteome] [HAMAP]

Taxonomic identifier

240292 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Nostocales › Nostocaceae › Anabaena

Protein attributes

Sequence length	277 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 – 277	276	Formamidopyrimidine-DNA glycosylase HAMAP MF_00103		PRO_1000008674
Regions
	Zinc finger	243 – 277	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	60	1	Proton donor; for beta-elimination activity By similarity
	Active site	267	1	Proton donor; for delta-elimination activity By similarity
	Binding site	94	1	DNA By similarity
	Binding site	113	1	DNA By similarity
	Binding site	158	1	DNA By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q3MDP1-1 [UniParc]. Last modified October 25, 2005. Version 1. Checksum: 3D67C43773CD2D78	FASTA	277	30,933
	10 20 30 40 50 60 MPELPEVETV RRGLNQLTLN RKITGGDVLL HRTIAHPFSV GDFLNGITGD SISAWHRRGK 70 80 90 100 110 120 YLLASTTSAA WLGVHLRMTG QLLWLNQDEP LHKHTRVRIF FEDQQELRFV DQRTFGQMWW 130 140 150 160 170 180 VSSGMAVESV ITGLAKLAVD PFSPEFTVEY LANKLHNRRR PIKTALLDQS VVAGLGNIYA 190 200 210 220 230 240 DEALFKSGVL PETLCTEVQL KQIELLRTAI IQVLETSIEA GGTTFSNFLN VKGVNGNYGG 250 260 270 VAWVYNRAGE PCKVCGDVIQ RIKLGGRSSH FCRQCQV

References

[1]

"Complete sequence of Anabaena variabilis ATCC 29413." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000117 Genomic DNA. Translation: ABA20895.1.
RefSeq	YP_321790.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	3683170.
GenomeReviews	Gene locus Ava_1271 in contig CP000117_GR.
KEGG	ava:Ava_1271.
NMPDR	fig|240292.3.peg.1955.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q3MDP1.
OMA	Q3MDP1. RMTGQLL.
Enzyme and pathway databases
BioCyc	AVAR240292:AVA_1271-MON.
Family and domain databases
HAMAP	MF_00103. [Tree]
InterPro	IPR015886. DNA_glyclase/AP_lyase_DNA-bd. IPR000214. DNA_glyclase/AP_lyase_Znf_dom. IPR010663. DNA_glyclase/IsotRNA_synth_Znf. 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. PF06827. zf-FPG_IleRS. 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. 1 hit. PS51066. ZF_FPG_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FPG_ANAVT

Accession

Primary (citable) accession number: Q3MDP1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	October 25, 2005
Last modified:	June 16, 2009
This is version 28 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)