Formamidopyrimidine-DNA glycosylase 1 - Mycobacterium tuberculosis

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P64150 (FPG1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Formamidopyrimidine-DNA glycosylase 1
Short name=Fapy-DNA glycosylase 1
EC=3.2.2.23

Alternative name(s):
DNA-(apurinic or apyrimidinic site) lyase MutM 1
Short name=AP lyase MutM 1
EC=4.2.99.18

Gene names

Name:	fpg1
Synonyms:	mutM
Ordered Locus Names:	Rv2924c, MT2994
ORF Names:	MTCY338.13c

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	289 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) when paired with C, G or T, as well as methyl-faPy (formanidopyrimidine residues) in poly(dG-dC) and spiroiminodihydantoin:C base pairs. Unlike its E.coli ortholog has no activity on 8-oxoG:A. 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. Cleaves ssDNA containing an AP site. Complements the H₂O₂ sensitivity of an M.smegmatis fpg disruption mutant; upon expression in M.smegmatis excises 8-oxoG from dsDNA. Ref.3 Ref.4 Ref.5
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
Induction	Expressed in mid-log phase. Ref.4
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 Reference proteome
Gene Ontology (GO)
Biological_process	base-excision repair Inferred from direct assay Ref.4. Source: MTBBASE nucleotide-excision repair Inferred from electronic annotation. Source: InterPro response to oxidative stress Inferred from direct assay Ref.4 Ref.5. Source: MTBBASE
Cellular_component	plasma membrane Inferred from direct assay PubMed 15525680. Source: MTBBASE
Molecular_function	8-oxo-7,8-dihydroguanine DNA N-glycosylase activity Inferred from direct assay Ref.4. Source: MTBBASE damaged DNA binding Inferred from electronic annotation. Source: InterPro double-stranded DNA binding Inferred from direct assay Ref.5. Source: MTBBASE 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

Removed By similarity

Chain

2 – 289

288

Formamidopyrimidine-DNA glycosylase 1 HAMAP-Rule MF_00103

PRO_0000170840

Regions

Zinc finger

251 – 285

FPG-type HAMAP-Rule MF_00103

Sites

Active site

Schiff-base intermediate with DNA By similarity

Active site

Proton donor By similarity

Active site

Proton donor; for beta-elimination activity By similarity

Active site

275

Proton donor; for delta-elimination activity By similarity

Binding site

100

DNA By similarity

Binding site

119

DNA By similarity

Binding site

165

DNA By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P64150 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E00B94A70DC2904E
Show »

FASTA

289

31,951

        10         20         30         40         50         60 
MPELPEVEVV RRGLQAHVTG RTITEVRVHH PRAVRRHDAG PADLTARLRG ARINGTDRRG 

        70         80         90        100        110        120 
KYLWLTLNTA GVHRPTDTAL VVHLGMSGQM LLGAVPCAAH VRISALLDDG TVLSFADQRT 

       130        140        150        160        170        180 
FGGWLLADLV TVDGSVVPVP VAHLARDPLD PRFDCDAVVK VLRRKHSELK RQLLDQRVVS 

       190        200        210        220        230        240 
GIGNIYADEA LWRAKVNGAH VAATLRCRRL GAVLHAAADV MREALAKGGT SFDSLYVNVN 

       250        260        270        280 
GESGYFERSL DAYGREGENC RRCGAVIRRE RFMNRSSFYC PRCQPRPRK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"A distinct role of formamidopyrimidine DNA glycosylase (MutM) in down-regulation of accumulation of G, C mutations and protection against oxidative stress in mycobacteria." Jain R., Kumar P., Varshney U. DNA Repair 6:1774-1785(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: ATCC 25618 / H37Rv.
[4]	"Characterization of the major formamidopyrimidine-DNA glycosylase homolog in Mycobacterium tuberculosis and its linkage to variable tandem repeats." Olsen I., Balasingham S.V., Davidsen T., Debebe E., Rodland E.A., van Soolingen D., Kremer K., Alseth I., Tonjum T. FEMS Immunol. Med. Microbiol. 56:151-161(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBSTRATES, INDUCTION. Strain: ATCC 25618 / H37Rv.
[5]	"The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit different substrate preferences from their Escherichia coli counterparts." Guo Y., Bandaru V., Jaruga P., Zhao X., Burrows C.J., Iwai S., Dizdaroglu M., Bond J.P., Wallace S.S. DNA Repair 9:177-190(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBSTRATES, DNA-BINDING. Strain: ATCC 25618 / H37Rv.
[6]	"Base excision and nucleotide excision repair pathways in mycobacteria." Kurthkoti K., Varshney U. Tuberculosis 91:533-543(2011) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000516 Genomic DNA. Translation: AAK47321.1. AL123456 Genomic DNA. Translation: CCP45727.1.
PIR	D70748.
RefSeq	NP_217440.1. NC_000962.3. NP_337507.1. NC_002755.2. YP_006516378.1. NC_018143.1.
3D structure databases
ProteinModelPortal	P64150.
SMR	P64150. Positions 2-284.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv2924c.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000000824; EBMYCP00000000824; EBMYCG00000000824. EBMYCT00000072433; EBMYCP00000070492; EBMYCG00000072428.
GeneID	13317718. 887438. 925264.
KEGG	mtc:MT2994. mtu:Rv2924c.
PATRIC	18128350. VBIMycTub22151_3274.
Organism-specific databases
TubercuList	Rv2924c.
Phylogenomic databases
eggNOG	COG0266.
HOGENOM	HOG000020884.
KO	K10563.
OMA	RREKFMN.
ProtClustDB	PRK01103.
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

FPG1_MYCTU

Accession

Primary (citable) accession number: P64150
Secondary accession number(s): L0TDY9, Q10959

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 72 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents