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Search term: Rv3709c

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene nameask
Rv numberRv3709c
FunctionInvolved at the first step in the common biosynthetic pathway leading from asp to the cell wall precursor MESO-diaminopimelate, to LYS, to met, to ILE and to THR [catalytic activity: ATP + L-aspartate = ADP + 4-phospho-L-aspartate]. Possibly acts in tetramer configuration, tetramer consisting of two alpha (catalytic activity) and two beta (function not known) chains.
ProductAspartokinase Ask (aspartate kinase) [contains: aspartokinase alpha subunit (Ask-alpha); and aspartokinase beta subunit (Ask-beta)]
CommentsRv3709c, (MTV025.057c), len: 421 aa. Ask, aspartokinase (see citation below), equivalent to Q9CB77|ask|ML2323 from Mycobacterium leprae (421 aa), FASTA scores: opt: 2531, E(): 2e-140, (92.65% identity in 421 aa overlap); and P41403|AK_MYCSM|ask from Mycobacterium smegmatis (421 aa), FASTA scores: opt: 2423, E(): 4e-134, (88.1% identity in 421 aa overlap); and to several other organisms e.g. Q9RQ25|ASKA from Amycolatopsis mediterranei (421 aa), FASTA scores: opt: 2026, E(): 5.8e-111, (72.2% identity in 421 aa overlap). Contains PS00324 Aspartokinase signature. Belongs to the aspartokinase family. Alternative products: the alpha and beta subunits of aspartokinase are produced by the use of alternative initiation sites (by similarity).
Molecular mass (Da)44429.6
Isoelectric point4.774
Gene length (bp)1266
Protein length421
Location (kb)4152.22

Functional categoryintermediary metabolism and respiration

ProteomicsIdentified in the membrane fraction of M. tuberculosis H37Rv using 1D-SDS-PAGE and uLC-MS/MS (See Gu et al., 2003). 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).
Mutationessential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti 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|Rv3709c|ask
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

Enzyme Classification2.7.2.4
Gene Ontologyaspartate kinase activity
ATP binding
amino acid binding
diaminopimelate biosynthetic process
M. bovisMb3736c
M. lepraeML2323
M. marinumMMAR_5222
M. smegmatisMSMEG_6257
Multiple Sequences Alignment: between orthologs

Interacting Drugs/Compounds
TDR TargetsRv3709c

Expression Data

Sassetti CM, Boyd DH, Rubin EJ,
Genes required for mycobacterial growth defined by high density mutagenesis.
Mol Microbiol (2003) 48(1):77-84
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
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, 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
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
Cirillo JD, Weisbrod TR, Pascopella L, Bloom BR, Jacobs WR,
Isolation and characterization of the aspartokinase and aspartate semialdehyde dehydrogenase operon from mycobacteria
Mol Microbiol (1994) 11(4):629-39
Cited for: Sequence