fpg



Type
protein_coding
Name
fpg
Locus Name

Rv2924c

Product

Probable formamidopyrimidine-DNA glycosylase Fpg (FAPY-DNA glycosylase)

Functional Category

Information pathways

Location
3238601..3239470 (- strand)
Gene Length
869 bp
Nucleotides
ATGCCCGAGCTGCCCGAAGTCGAGGTGGTGCGGCGCGGCTTGCAGGCTCACGTGACCGGCCGGACCATCACCGAGGTTCGGGTGCACCACCCCCGCGCTGTGCGCCGCCACGATGCCGGGCCCGCGGATCTGACGGCGCGGCTGCGGGGAGCGCGGATCAACGGAACCGATCGGCGCGGCAAGTACCTGTGGTTGACACTCAATACGGCTGGGGTCCATAGGCCGACGGACACCGCACTCGTGGTGCACCTGGGCATGAGTGGGCAGATGCTGCTCGGGGCGGTGCCGTGTGCCGCTCACGTCCGGATTTCCGCGCTGCTCGACGACGGGACCGTGCTGAGCTTCGCTGACCAACGGACCTTCGGAGGGTGGCTGCTTGCCGACCTGGTGACGGTGGACGGCAGCGTGGTACCGGTGCCGGTCGCCCACCTGGCGCGCGACCCGCTTGACCCGCGGTTCGATTGTGACGCTGTAGTTAAAGTGTTGCGGCGCAAGCATTCCGAACTCAAGCGCCAGCTGCTGGATCAGCGGGTGGTGTCGGGAATCGGCAACATCTATGCCGATGAGGCGCTGTGGCGGGCCAAGGTGAACGGCGCCCACGTCGCCGCCACACTAAGGTGCCGGCGTCTGGGAGCGGTCCTGCATGCCGCCGCCGACGTGATGCGCGAAGCGCTGGCGAAAGGTGGCACCTCGTTCGACTCTTTGTATGTCAACGTCAACGGCGAGTCGGGCTACTTCGAGCGGTCGCTGGACGCTTATGGCCGCGAAGGCGAAAACTGTCGGCGCTGCGGCGCGGTGATACGCCGGGAGAGGTTTATGAACCGCTCGTCGTTCTACTGCCCGCGATGCCAGCCGCGGCCCCGAAAGTA
Drug Resistance

Check for drug resistance association at TBDREAMDB

Mutations

Check for mutants available at TARGET


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 H(2)O(2) sensitivity of an M.smegmatis fpg disruption mutant; upon expression in M.smegmatis excises 8-oxoG from dsDNA. {ECO:0000269|PubMed:17698424, ECO:0000269|PubMed:19496823, ECO:0000269|PubMed:20031487}.
Family

FPG family

GO
InterPro

UniProt
P9WNC3
GenBank
Rv2924c
EnsemblBacteria
Rv2924c
Mycobrowser
Rv2924c


Summary
Name
Formamidopyrimidine-DNA glycosylase 1 (Fapy-DNA glycosylase 1) (EC 3.2.2.23) (DNA-(apurinic or apyrimidinic site) lyase MutM 1) (AP lyase MutM 1) (EC 4.2.99.18)
Family
FPG family
Protein Sequence
MPELPEVEVVRRGLQAHVTGRTITEVRVHHPRAVRRHDAGPADLTARLRGARINGTDRRGKYLWLTLNTAGVHRPTDTALVVHLGMSGQMLLGAVPCAAHVRISALLDDGTVLSFADQRTFGGWLLADLVTVDGSVVPVPVAHLARDPLDPRFDCDAVVKVLRRKHSELKRQLLDQRVVSGIGNIYADEALWRAKVNGAHVAATLRCRRLGAVLHAAADVMREALAKGGTSFDSLYVNVNGESGYFERSLDAYGREGENCRRCGAVIRRERFMNRSSFYCPRCQPRPRK
Mass
31,951 Da
Length
289 Aa

Rv2924c doesn't seem to be a targeted by any drug.



Base excision and nucleotide excision repair pathways in mycobacteria.
Tuberculosis (Edinb). 2011 Nov;91(6):533-43. doi: 10.1016/j.tube.2011.06.005. Epub 2011 Jul 18.
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol Cell Proteomics. 2011 Dec;10(12):M111.011627. doi: 10.1074/mcp.M111.011445. Epub 2011 Oct 3.
The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit different substrate preferences from their Escherichia coli counterparts.
DNA Repair (Amst). 2010 Feb 4;9(2):177-90. doi: 10.1016/j.dnarep.2009.11.008. Epub 2009 Dec 23.
Characterization of the major formamidopyrimidine-DNA glycosylase homolog in Mycobacterium tuberculosis and its linkage to variable tandem repeats.
FEMS Immunol Med Microbiol. 2009 Jul;56(2):151-61. doi: 10.1111/j.1574-695X.2009.00562.x. Epub 2009 Jun 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.
DNA Repair (Amst). 2007 Dec 1;6(12):1774-85. doi: 10.1016/j.dnarep.2007.06.009. Epub 2007 Aug 16.
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence.
Nature. 1998 Jun 11;393(6685):537-44. doi: 10.1038/31159.