O50606 (FPG_THET8) 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:	TTHA1806

Organism

Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]

Taxonomic identifier

300852 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › Thermus thermophilus

Protein attributes

Sequence length	267 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

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.
Subunit structure	Monomer.
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	3D-structure Complete proteome Multifunctional enzyme Reference proteome
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 HAMAP-Rule MF_00103

Chain

2 – 267

266

Formamidopyrimidine-DNA glycosylase HAMAP-Rule MF_00103

PRO_0000170880

Regions

Zinc finger

230 – 264

35

FPG-type HAMAP-Rule MF_00103

Sites

Active site

2

1

Schiff-base intermediate with DNA Probable

Active site

3

1

Proton donor Probable

Active site

53

1

Proton donor; for beta-elimination activity Probable

Active site

254

1

Proton donor; for delta-elimination activity Probable

Binding site

82

1

DNA By similarity

Binding site

100

1

DNA By similarity

Secondary structure

1

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267

Helix Strand Turn

Details...

Helix

4 – 18

15

Beta strand

22 – 27

6

Turn

31 – 33

3

Beta strand

34 – 36

3

Helix

37 – 40

4

Beta strand

43 – 51

9

Beta strand

54 – 59

6

Turn

60 – 62

3

Beta strand

63 – 68

6

Turn

70 – 72

3

Beta strand

74 – 78

5

Beta strand

83 – 91

9

Beta strand

93 – 97

5

Beta strand

104 – 109

6

Helix

118 – 121

4

Helix

133 – 141

9

Helix

147 – 153

7

Beta strand

154 – 157

4

Helix

162 – 171

10

Beta strand

176 – 179

4

Helix

180 – 182

3

Helix

185 – 204

20

Helix

226 – 228

3

Turn

240 – 242

3

Beta strand

247 – 253

7

Beta strand

255 – 258

4

Turn

260 – 264

5

Sequences

	Sequence		Length	Mass (Da)
	O50606 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: CDEAEAB2BED893EA	FASTA	267	29,915
	10 20 30 40 50 60 MPELPEVETT RRRLRPLVLG QTLRQVVHRD PARYRNTALA EGRRILEVDR RGKFLLFALE 70 80 90 100 110 120 GGVELVAHLG MTGGFRLEPT PHTRAALVLE GRTLYFHDPR RFGRLFGVRR GDYREIPLLL 130 140 150 160 170 180 RLGPEPLSEA FAFPGFFRGL KESARPLKAL LLDQRLAAGV GNIYADEALF RARLSPFRPA 190 200 210 220 230 240 RSLTEEEARR LYRALREVLA EAVELGGSTL SDQSYRQPDG LPGGFQTRHA VYGREGLPCP 250 260 ACGRPVERRV VAGRGTHFCP TCQGEGP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Thermostable repair enzyme for oxidative DNA damage from extremely thermophilic bacterium, Thermus thermophilus HB8." Mikawa T., Kato R., Sugahara M., Kuramitsu S. Nucleic Acids Res. 26:903-910(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
[2]	"Complete genome sequence of Thermus thermophilus HB8." Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S. Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB8 / ATCC 27634 / DSM 579.
[3]	"Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8." Sugahara M., Mikawa T., Kumasaka T., Yamamoto M., Kato R., Fukuyama K., Inoue Y., Kuramitsu S. EMBO J. 19:3857-3869(2000) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB008520 Genomic DNA. Translation: BAA24892.1.
AP008226 Genomic DNA. Translation: BAD71629.1.

RefSeq

YP_145072.1. NC_006461.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EE8	X-ray	1.90	A/B	2-267	[»]

ProteinModelPortal

O50606.

SMR

O50606. Positions 2-267.

ModBase

Search...

Protein-protein interaction databases

STRING

300852.TTHA1806.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3169771.

KEGG

ttj:TTHA1806.

PATRIC

23958581. VBITheThe93045_1777.

Phylogenomic databases

eggNOG

COG0266.

HOGENOM

HOG000020884.

KO

K10563.

OMA

RREKFMN.

ProtClustDB

PRK14811.

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...

Other

EvolutionaryTrace

O50606.

Entry information

Entry name

FPG_THET8

Accession

Primary (citable) accession number: O50606
Secondary accession number(s): Q5SHC4

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program