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Search term: Rv3566c

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namenat
Rv numberRv3566c
Synonym(s)nhoA
TypeCDS
FunctionCould have a role in acetylating, and hence inactivating, the antitubercular drug isoniazid [catalytic activity: acetyl-CoA + arylamine = CoA + N-acetylarylamine].
ProductArylamine N-acetyltransferase Nat (arylamine acetylase)
CommentsRv3566c, (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).
Molecular mass (Da)31029.2
Isoelectric point5.3613
Gene length (bp)852
Protein length283
Location (kb)4007.33


Functional categoryintermediary metabolism and respiration


ProteomicsIdentified 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).
MutationNon-essential gene for in vitro growth of H37Rv, by sequencing of Himar1-based 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
OperonRv3566A and Rv3566c are co-transcribed in M. bovis BCG, by RT-PCR (See Anderton et al., 2006).


Coordinates
TypeStartEndOrientation
CDS40073314008182-


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv3566c|nat
MALDLTAYFDRINYRGATDPTLDVLQDLVTVHSRTIPFENLDPLLGVPVDDLSPQALADK
LVLRRRGGYCFEHNGLMGYVLAELGYRVRRFAARVVWKLAPDAPLPPQTHTLLGVTFPGS
GGCYLVDVGFGGQTPTSPLRLETGAVQPTTHEPYRLEDRVDGFVLQAMVRDTWQTLYEFT
TQTRPQIDLKVASWYASTHPASKFVTGLTAAVITDDARWNLSGRDLAVHRAGGTEKIRLA
DAAAVVDTLSERFGINVADIGERGALETRIDELLARQPGADAP
Blastp: Pre-computed results
TransMembrane prediction using Hidden Markov Models: TMHMM
Genomic sequence

Add extra bases upstream (5') and downstream (3')



Structural information
Protein Data BankNo structure available
PFAMP0A5L8


Orthologs/Cross-references
CDC1551MT3671
Enzyme Classification2.3.1.5
Gene Ontologyarylamine N-acetyltransferase activity
cytoplasm
metabolic process
M. bovisMb3596c
M. marinumMMAR_5055
M. smegmatisMSMEG_0306
UniProtP0A5L8
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv3566c
Drug Resistance MutationsIsoniazid


Expression Data
TBDBRv3566c


Bibliography
Sim E, Payton M, Noble M, Minchin R,
An update on genetic, structural and functional studies of arylamine N-acetyltransferases in eucaryotes and procaryotes
Hum Mol Genet (2000) 9(16):2435-41
Cited for: Review
Upton AM, Mushtaq A, Victor TC, Sampson SL, Sandy J, Smith DM, van Helden PV, Sim E,
Arylamine N-acetyltransferase of Mycobacterium tuberculosis is a polymorphic enzyme and a site of isoniazid metabolism
Mol Microbiol (2001) 42(2):309-17
Cited for: Product/Sequence/Mutant
Payton M, Gifford C, Schartau P, Hagemeier C, Mushtaq A, Lucas S, Pinter K, Sim E,
Evidence towards the role of arylamine N-acetyltransferase in Mycobacterium smegmatis and development of a specific antiserum against the homologous enzyme of Mycobacterium tuberculosis
Microbiology (2001) 147(Pt 12):3295-302
Cited for: Homolog/Function/Regulation/Mutant
Sandy J, Mushtaq A, Kawamura A, Sinclair J, Sim E, Noble M,
The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis--an enzyme which inactivates the anti-tubercular drug, isoniazid
J Mol Biol (2002) 318(4):1071-83
Cited for: Homolog/Product/Structure
Bhakta S, Besra GS, Upton AM, Parish T, Sholto-Douglas-Vernon C, Gibson KJ, Knutton S, Gordon S, DaSilva RP, Anderton MC, Sim E,
Arylamine N-acetyltransferase is required for synthesis of mycolic acids and complex lipids in Mycobacterium bovis BCG and represents a novel drug target.
J Exp Med (2004) 199(9):1191-9
Cited for: Mutant
Mawuenyega KG, Forst CV, Dobos KM, Belisle JT, Chen J, Bradbury EM, Bradbury AR, Chen X,
Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling.
Mol Biol Cell (2005) 16(1):396-404
Cited for: Proteomics
Anderton MC, Bhakta S, Besra GS, Jeavons P, Eltis LD, Sim E,
Characterization of the putative operon containing arylamine N-acetyltransferase (nat) in Mycobacterium bovis BCG.
Mol Microbiol (2006) 59(1):181-92
Cited for: Operon
Malen H, Pathak S, Softeland T, de Souza GA, Wiker HG,
Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv.
BMC Microbiol (2010) 10:132
Cited for: Proteomics
de Souza GA, Arntzen MO, Fortuin S, Schurch AC, Malen H, McEvoy CR, van Soolingen D, Thiede B, Warren RM, Wiker HG,
Proteogenomic analysis of polymorphisms and gene annotation divergences in prokaryotes using a clustered mass spectrometry-friendly database.
Mol Cell Proteomics (2011) 10(1):M110.002527
Cited for: Proteomics/Sequence
de Souza GA, Leversen NA, Malen H, Wiker HG,
Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway.
J Proteomics (2011) 75(2):502-10
Cited for: Proteomics
Kelkar DS, Kumar D, Kumar P, Balakrishnan L, Muthusamy B, Yadav AK, Shrivastava P, Marimuthu A, Anand S, Sundaram H, Kingsbury R, Harsha HC, Nair B, Prasad TS, Chauhan DS, Katoch K, Katoch VM, Kumar P, Chaerkady R, Ramachandran S, Dash D, Pandey A,
Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry.
Mol Cell Proteomics (2011) 10(12):M111.011627
Cited for: Proteomics/Sequence
Griffin JE, Gawronski JD, Dejesus MA, Ioerger TR, Akerley BJ, Sassetti CM,
High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism.
PLoS Pathog (2011) 7(9):e1002251
Cited for: Mutant
Payton M, Auty R, Delgoda R, Everett M, Sim E,
Cloning and characterization of arylamine N-acetyltransferase genes from Mycobacterium smegmatis and Mycobacterium tuberculosis: increased expression results in isoniazid resistance
J Bacteriol (1999) 181(4):1343-7
Cited for: Product/Function