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Search term: Rv1596

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namenadC
Rv numberRv1596
Functionde novo biosynthesis of NAD and NADP [catalytic activity: nicotinate D-ribonucleotide + diphosphate + CO(2) = pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1-diphosphate]
ProductProbable nicotinate-nucleotide pyrophosphatase NadC
CommentsRv1596, (MTCY336.08c), len: 285 aa. Probable nadC, nicotinate-nucleotide pyrophosphatase O06594. Similar to many e.g. ADC_MYCLE|P46714 from Mycobacterium leprae (284 aa), FASTA results: opt: 1418, E(): 0,(79.2% identity in 283 aa overlap). Belongs to the NADC/MODD family.
Molecular mass (Da)29951.1
Isoelectric point4.8783
Gene length (bp)858
Protein length285
Location (kb)1797.39

Functional categoryintermediary metabolism and respiration

ProteomicsThe product of this CDS corresponds to spot 3_266 identified by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany (see citations below). Identified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). Identified in the membrane fraction of M. tuberculosis H37Rv using nanoLC-MS/MS (See Xiong 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 by Himar1-based transposon mutagenesis in CDC1551 strain (see Lamichhane et al., 2003). Essential gene for in vitro growth of H37Rv, by sequencing of Himar1-based transposon mutagenesis (See Griffin et al., 2011). Check for mutants available at TARGET website


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv1596|nadC
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 Bank1QPN 1QPO 1QPQ 1QPR

Enzyme Classification2.4.2.19
Gene Ontologynicotinate-nucleotide diphosphorylase (carboxylating) activity
NAD biosynthetic process
M. bovisMb1622
M. lepraeML1227
M. marinumMMAR_2393
M. smegmatisMSMEG_3201
Multiple Sequences Alignment: between orthologs

Interacting Drugs/Compounds
TDR TargetsRv1596

Expression Data

Jungblut PR, Schaible UE, Mollenkopf HJ, Zimny-Arndt U, Zimny -Arndt U, Raupach B, Mattow J, Halada P, Lamer S, Hagens K, Kaufmann SH,
Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens
Mol Microbiol (1999) 33(6):1103-17
Cited for: Proteomics
Mattow J, Jungblut PR, Schaible UE, Mollenkopf HJ, Lamer S, Zimny-Arndt U, Zimny -Arndt U, Hagens K, Muller EC, Kaufmann SH,
Identification of proteins from Mycobacterium tuberculosis missing in attenuated Mycobacterium bovis BCG strains
Electrophoresis (2001) 22(14):2936-46
Cited for: Proteomics
Lamichhane G, Zignol M, Blades NJ, Geiman DE, Dougherty A, Grosset J, Broman KW, Bishai WR,
A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis.
Proc Natl Acad Sci U S A (2003) 100(12):7213-8
Cited for: Mutant
Gu S, Chen J, Dobos KM, Bradbury EM, Belisle JT, Chen X,
Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain.
Mol Cell Proteomics (2003) 2(12):1284-96
Cited for: Proteomics
Xiong Y, Chalmers MJ, Gao FP, Cross TA, Marshall AG,
Identification of Mycobacterium tuberculosis H37Rv integral membrane proteins by one-dimensional gel electrophoresis and liquid chromatography electrospray ionization tandem mass spectrometry.
J Proteome Res (2005) 4(3):855-61
Cited for: Proteomics
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
Sharma V, Grubmeyer C, Sacchettini JC,
Crystal structure of quinolinic acid phosphoribosyltransferase from Mmycobacterium tuberculosis: a potential TB drug target.
Structure (1998) 6(12):1587-99
Cited for: Structure