B7VHK6 (FPG_VIBSL) 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:	VS_0186

Organism

Vibrio splendidus (strain LGP32) (Vibrio splendidus (strain Mel32)) [Complete proteome] [HAMAP]

Taxonomic identifier

575788 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio › Vibrio splendidus

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. 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. HAMAP-Rule MF_00103
Subunit structure	Monomer By similarity. HAMAP-Rule 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 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 – 269	268	Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103		PRO_1000118906
Regions
	Zinc finger	235 – 269	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	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)
	B7VHK6 [UniParc]. Last modified February 10, 2009. Version 1. Checksum: DC635316CF8B6EAF	FASTA	269	30,122
	10 20 30 40 50 60 MPELPEVEVS RMGISPHLVG ETIKTLTFRT PKLRWDIPQE LKRLEGQVIR SISRRAKYLL 70 80 90 100 110 120 IETDTGTAIV HLGMSGSLRV LDADFPPAKH DHVDLKLTNG KILRYNDPRR FGAWLWSAPD 130 140 150 160 170 180 EIHTVLLGSG PEPLTDDFNA DYIAEKAEKR KVAVKQFIMD NKVVVGVGNI YANEALFSSR 190 200 210 220 230 240 INPLRSASKV TKQEWLLLTK EIKQVLATAI RQGGTTLKDF AQADGKPGYF AQELQVYGKA 250 260 GEQCPNCAEL IQELKIGQRN TFYCSSCQV

References

[1]	"Vibrio splendidus str. LGP32 complete genome." Mazel D., Le Roux F. Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: LGP32.

Cross-references

Sequence databases
EMBL GenBank DDBJ	FM954972 Genomic DNA. Translation: CAV17218.1.
RefSeq	YP_002415870.1. NC_011753.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	575788.VS_0186.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7159856.
KEGG	vsp:VS_0186.
PATRIC	20151094. VBIVibSpl48387_1574.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0266.
HOGENOM	HOG000020881.
KO	K10563.
OMA	VLRYNDP.
ProtClustDB	PRK01103.
Enzyme and pathway databases
BioCyc	VSPL575788:GH64-178-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_VIBSL

Accession

Primary (citable) accession number: B7VHK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	February 10, 2009
Last modified:	May 29, 2013
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program