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Search term: Rv1294

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namethrA
Rv numberRv1294
TypeCDS
FunctionInvolved in the conversion of L-aspartate to homoserine (third step). Homoserine participates in the biosynthesis of threonine and then isoleucine and in the biosynthesis of methionine [catalytic activity: L-homoserine + NAD(P)(+) = L-aspartate 4-semialdehyde + NAD(P)H.]
ProductProbable homoserine dehydrogenase ThrA
CommentsRv1294, (MTCY373.14), len: 441 aa. Probable thrA (hom), homoserine dehydrogenase, highly similar to DHOM_MYCLE|P46806 from Mycobacterium leprae (441 aa), FASTA scores: opt: 2437, E():0, (89.5% identity in 438 aa overlap). Contains PS00017 ATP/GTP-binding site motif A; PS01042 Homoserine dehydrogenase signature. Belongs to the homoserine dehydrogenase family.
Molecular mass (Da)45520.7
Isoelectric point4.5009
Gene length (bp)1326
Protein length441
Location (kb)1449.38


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 whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate or membrane protein fraction (See de Souza et al., 2011). Translational start site supported by proteomics data (See de Souza et al., 2011) (See Kelkar 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


Coordinates
TypeStartEndOrientation
RBS14493651449371+
CDS14493751450700+


Protein sequence in FASTA format
>M. tuberculosis H37Rv|Rv1294|thrA
VPGDEKPVGVAVLGLGNVGSEVVRIIENSAEDLAARVGAPLVLRGIGVRRVTTDRGVPIE
LLTDDIEELVAREDVDIVVEVMGPVEPSRKAILGALERGKSVVTANKALLATSTGELAQA
AESAHVDLYFEAAVAGAIPVIRPLTQSLAGDTVLRVAGIVNGTTNYILSAMDSTGADYAS
ALADASALGYAEADPTADVEGYDAAAKAAILASIAFHTRVTADDVYREGITKVTPADFGS
AHALGCTIKLLSICERITTDEGSQRVSARVYPALVPLSHPLAAVNGAFNAVVVEAEAAGR
LMFYGQGAGGAPTASAVTGDLVMAARNRVLGSRGPRESKYAQLPVAPMGFIETRYYVSMN
VADKPGVLSAVAAEFAKREVSIAEVRQEGVVDEGGRRVGARIVVVTHLATDAALSETVDA
LDDLDVVQGVSSVIRLEGTGL
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
PFAMP63629


Orthologs/Cross-references
CDC1551MT1333
Enzyme Classification1.1.1.3
Gene Ontologyhomoserine dehydrogenase activity
methionine biosynthetic process
threonine biosynthetic process
isoleucine biosynthetic process
amino acid binding
NADP or NADPH binding
oxidation reduction
M. bovisMb1326
M. lepraeML1129
M. marinumMMAR_4103
M. smegmatisMSMEG_4957
UniProtP63629
Multiple Sequences Alignment: between orthologs


Interacting Drugs/Compounds
TDR TargetsRv1294


Expression Data
TBDBRv1294


Bibliography
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
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