Q5KWC3 (FPG_GEOKA) 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:	GK2728

Organism

Geobacillus kaustophilus (strain HTA426) [Complete proteome] [HAMAP]

Taxonomic identifier

235909 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Geobacillus › Geobacillus kaustophilus

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. 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.
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 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 – 274	273	Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103		PRO_0000228434
Regions
	Zinc finger	240 – 274	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	60	1	Proton donor; for beta-elimination activity By similarity
	Active site	264	1	Proton donor; for delta-elimination activity By similarity
	Binding site	93	1	DNA By similarity
	Binding site	112	1	DNA By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5KWC3 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 92BACFC57FC5C86A	FASTA	274	30,619
	10 20 30 40 50 60 MPELPEVETI RRTLLPLIVG KTIEDVRIFW PNIIRHPRDP EAFAARMIGQ TVRGLERRGK 70 80 90 100 110 120 FLKFLLDRDA LISHLRMEGR YAVASALEPL EPHTHVVFCF TDGSELRYRD VRKFGTMHVY 130 140 150 160 170 180 AKEEADRRPP LAELGPEPLS PAFSPAVLAE RAVKTKRSVK ALLLDQTVVA GFGNIYVDES 190 200 210 220 230 240 LFRAGILPGR PAASLSSKEI ERLHEEMVAT IGEAVMKGGS TVRTYVNTQG EAGAFQHSLF 250 260 270 VYGRKGEPCK RCGTPIEKTV VAGRGTHYCP RCQR

References

[1]

"Thermoadaptation trait revealed by the genome sequence of thermophilic Geobacillus kaustophilus." Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., Matsui S., Uchiyama I. Nucleic Acids Res. 32:6292-6303(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HTA426.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000043 Genomic DNA. Translation: BAD77013.1.
RefSeq	YP_148581.1. NC_006510.1.
3D structure databases
ProteinModelPortal	Q5KWC3.
SMR	Q5KWC3. Positions 2-274.
ModBase	Search...
Protein-protein interaction databases
STRING	235909.GK2728.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3185785.
KEGG	gka:GK2728.
PATRIC	21966927. VBIGeoKau81518_2912.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0266.
HOGENOM	HOG000020885.
KO	K10563.
OMA	VLRYNDP.
ProtClustDB	PRK01103.
Enzyme and pathway databases
BioCyc	GKAU235909:GJO7-2823-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_GEOKA

Accession

Primary (citable) accession number: Q5KWC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 67 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program