Reviewed, UniProtKB/Swiss-Prot B0C5D4 (FPG_ACAM1)

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:	AM1_2501

Organism

Acaryochloris marina (strain MBIC 11017) [Complete proteome] [HAMAP]

Taxonomic identifier

329726 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Acaryochloris

Protein attributes

Sequence length	284 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 MF_00103
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. HAMAP MF_00103
Subunit structure	Monomer By similarity. HAMAP MF_00103
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 – 284	283	Formamidopyrimidine-DNA glycosylase HAMAP MF_00103		PRO_1000075691
Regions
	Zinc finger	248 – 282	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	272	1	Proton donor; for delta-elimination activity By similarity
	Binding site	99	1	DNA By similarity
	Binding site	118	1	DNA By similarity
	Binding site	163	1	DNA By similarity

Sequences

	Sequence		Length	Mass (Da)
	B0C5D4-1 [UniParc]. Last modified February 26, 2008. Version 1. Checksum: 7BB706D202E548C7	FASTA	284	32,098
	10 20 30 40 50 60 MPELPEVETV RLGLEKVTVG MQIMGGEVLY PRTIAHPQSP QVFIQGLQDA TFLSWMRRGK 70 80 90 100 110 120 YLLSQLSFST QQPSGWLGVH LRMTGQLLWV AQDEPVQKHT RVRLFFVNNR ELRFVDQRTF 130 140 150 160 170 180 GQMWWVAPTE DPKQVISGLQ KLGPEPFSEE FSVDYFWESL QGRKRSIKSA LLDQALVAGV 190 200 210 220 230 240 GNIYADEALF MSEIRPTTAC HQLQTEQVQR LRTAIIEVLS TSIGAGGTTF SDFRDLKGVN 250 260 270 280 GNYGGMAWVY GRQGQPCRTC GQTIERIKLV GRSTHFCPQC QPES

References

[1]

"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina." Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L. , Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W. Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008) [PubMed: 18252824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000828 Genomic DNA. Translation: ABW27510.1.
RefSeq	YP_001516824.1.
3D structure databases
SMR	B0C5D4. Positions 2-283.
ModBase	Search...
Genome annotation databases
GeneID	5681314.
GenomeReviews	Gene locus AM1_2501 in contig CP000828_GR.
KEGG	amr:AM1_2501.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG690070.
OMA	LHDPRRF.
Family and domain databases
HAMAP	MF_00103. Fapy-DNA_glycosyl. [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. IPR020629. Formamido-pyr_DNA_Glyclase. IPR010979. Ribosomal_S13-like_H2TH. [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]
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_ACAM1

Accession

Primary (citable) accession number: B0C5D4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	February 26, 2008
Last modified:	February 9, 2010
This is version 18 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)