Gene Rv3566c (nhoA)
in Mycobacterium tuberculosis H37Rv
General annotation
| Type | CDS |
| Function | Could have a role in acetylating, and hence inactivating, the antitubercular drug isoniazid [catalytic activity: acetyl-CoA + arylamine = CoA + N-acetylarylamine]. |
| Product | Arylamine N-acetyltransferase Nat (arylamine acetylase) |
| Comments | Rv3566c, (MT3671, MTCY06G11.13c), len: 283 aa. Nat (alternate gene name: nhoA), arylamine N-acetyltransferase (see citations below), highly similar to O86309|NAT_MYCSM arylamine N-acetyltransferase from Mycobacterium smegmatis (see citation below) (275 aa), FASTA scores: opt: 1114, E(): 3e-66, (60.95% identity in 274 aa overlap). Also highly similar to others e.g. Q98D42|BAB51429|MLR4870 from Rhizobium loti (Mesorhizobium loti) (278 aa), FASTA scores: opt: 697, E(): 1.1e-38, (44.1% identity in 272 aa overlap); P77567|NHOA_ECOLI|B1463 from Escherichia coli strain K12 (281 aa), FASTA scores: opt: 537, E(): 4.4e-28, (38.85% identity in 273 aa overlap); Q00267|NHOA_SALTY from Salmonella typhimurium (281 aa), FASTA scores: opt: 507, E(): 4.3e-26, (34.8% identity in 273 aa overlap); etc. Belongs to the arylamine N-acetyltransferase family. Note that previously known as nhoA (332 aa) and that nucleotide 4007874 has been changed since first submission (G deleted). |
| Functional category | Intermediary metabolism and respiration |
| Proteomics | Identified in the cell membrane fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified by mass spectrometry in Triton X-114 extracts of M. tuberculosis H37Rv (See Malen et al., 2010). Identified by mass spectrometry in the membrane protein fraction and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza et al., 2011). Translational start site supported by proteomics data (See de Souza et al., 2011) (See Kelkar et al., 2011). |
| Operon | Rv3566A and Rv3566c are co-transcribed in M. bovis BCG, by RT-PCR (See Anderton et al., 2006). |
| Mutant | Non-essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Non-essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Non-essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011). Deletion of nat from M. bovis BCG Pasteur reduces biosynthesis of mycolic acids and other complex lipids (See Bhakta et al., 2004). Check for mutants available at TARGET website |
Coordinates
| Type | Start | End | Orientation |
|---|---|---|---|
| CDS | 4007331 | 4008182 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3566c|nat
MALDLTAYFDRINYRGATDPTLDVLQDLVTVHSRTIPFENLDPLLGVPVDDLSPQALADKLVLRRRGGYCFEHNGLMGYVLAELGYRVRRFAARVVWKLAPDAPLPPQTHTLLGVTFPGSGGCYLVDVGFGGQTPTSPLRLETGAVQPTTHEPYRLEDRVDGFVLQAMVRDTWQTLYEFTTQTRPQIDLKVASWYASTHPASKFVTGLTAAVITDDARWNLSGRDLAVHRAGGTEKIRLADAAAVVDTLSERFGINVADIGERGALETRIDELLARQPGADAP
Bibliography
- Payton M et al. [1999]. Cloning and characterization of arylamine N-acetyltransferase genes from Mycobacterium smegmatis and Mycobacterium tuberculosis: increased expression results in isoniazid resistance. Product Function
- Sim E et al. [2000]. An update on genetic, structural and functional studies of arylamine N-acetyltransferases in eucaryotes and procaryotes. Review
- Payton M et al. [2001]. Evidence towards the role of arylamine N-acetyltransferase in Mycobacterium smegmatis and development of a specific antiserum against the homologous enzyme of Mycobacterium tuberculosis. Homolog Function Regulation Mutant
- Upton AM et al. [2001]. Arylamine N-acetyltransferase of Mycobacterium tuberculosis is a polymorphic enzyme and a site of isoniazid metabolism. Product Sequence Mutant
- Sandy J et al. [2002]. The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis--an enzyme which inactivates the anti-tubercular drug, isoniazid. Homolog Product Structure
- Bhakta S et al. [2004]. Arylamine N-acetyltransferase is required for synthesis of mycolic acids and complex lipids in Mycobacterium bovis BCG and represents a novel drug target. Mutant
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. Proteomics
- Anderton MC et al. [2006]. Characterization of the putative operon containing arylamine N-acetyltransferase (nat) in Mycobacterium bovis BCG. Operon
- Målen H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- Kelkar DS et al. [2011]. Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Proteomics Sequence
- Griffin JE et al. [2011]. High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. Mutant
- de Souza GA et al. [2011]. Proteogenomic analysis of polymorphisms and gene annotation divergences in prokaryotes using a clustered mass spectrometry-friendly database. Proteomics Sequence
- DeJesus MA et al. [2017]. Comprehensive Essentiality Analysis of the Mycobacterium tuberculosis Genome via Saturating Transposon Mutagenesis. Mutant
- Minato Y et al. [2019]. Genomewide Assessment of Mycobacterium tuberculosis Conditionally Essential Metabolic Pathways. Mutant
