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virulence, detoxification, adaptation
information pathways
cell wall and cell processes
stable RNAs
insertion seqs and phages
PE/PPE
intermediary metabolism and respiration
unknown
regulatory proteins
conserved hypotheticals
lipid metabolism
pseudogenes
General annotation
TypeCDS
FunctionInvolved in leucine biosynthesis (at the first step). Catalyzes condensation of acetyl-CoA and 2-oxoisovalerate to form 2-isopropylmalate synthase [catalytic activity: 3-carboxy-3-hydroxy-4-methylpentanoate + CoA = acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O].
Product2-isopropylmalate synthase LeuA (alpha-isopropylmalate synthase) (alpha-IPM synthetase) (IPMS)
CommentsRv3710, (MTV025.058), len: 644 aa. LeuA, alpha-isopropylmalate synthase (see citations below), equivalent to Q9CB76|LEUA|ML2324 2-isopropylmalate synthase from Mycobacterium leprae (607 aa), FASTA scores: opt: 3291, E(): 3.7e-192, (80.7% identity in 642 aa overlap). Also highly similar to many e.g. P42455|LEU1_CORGL|LEUA from Corynebacterium glutamicum (Brevibacterium flavum) (616 aa), FASTA scores: opt: 2547, E(): 5.3e-147, (63.25% identity in 645 aa overlap); O31046|LEU1_STRCO|LEUA from Streptomyces coelicolor (573 aa), FASTA scores: opt: 2226, E(): 1.5e-127, (57.8% identity in 616 aa overlap); BAB49833|Q98HN3|MLR2792 from Rhizobium loti (Mesorhizobium loti) (588 aa), FASTA scores: opt: 1849, E(): 1.1e-104, (58.0% identity in 536 aa overlap); etc. Equivalent to AAK48181 from Mycobacterium tuberculosis strain CDC1551 (659 aa) but shorter 15 aa. Contains PS00815 and PS00816 Alpha-isopropylmalate and homocitrate synthases signatures 1 and 2. Belongs to the alpha-IPM synthetase / homocitrate synthase family. K+ is likely the physiological activator; Zn2+ and Cd2+ are inhibitors.
Functional categoryIntermediary metabolism and respiration
ProteomicsThe product of this CDS corresponds to spot 1_186 identified by proteomics at the Max Planck Institute for Infection Biology, Berlin (Germany) and the Statens Serum Institute (Denmark) (see proteomics citations). Identified in culture filtrates of M. tuberculosis H37Rv (See Malen et al., 2007). 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 M. tuberculosis H37Rv-infected guinea pig lungs at 90 days but not 30 days (See Kruh et al., 2010). Identified by mass spectrometry in the culture filtrate, membrane protein fraction, and whole cell lysates of M. tuberculosis H37Rv (See de Souza et al., 2011). Translational start site supported by proteomics data (See Kelkar et al., 2011).
MutantEssential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Essential gene by Himar1 transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011).
Check for mutants available at TARGET website
Coordinates
TypeStartEndOrientation
CDS41537404155674+
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3710|leuA
VTTSESPDAYTESFGAHTIVKPAGPPRVGQPSWNPQRASSMPVNRYRPFAEEVEPIRLRNRTWPDRVIDRAPLWCAVDLRDGNQALIDPMSPARKRRMFDLLVRMGYKEIEVGFPSASQTDFDFVREIIEQGAIPDDVTIQVLTQCRPELIERTFQACSGAPRAIVHFYNSTSILQRRVVFRANRAEVQAIATDGARKCVEQAAKYPGTQWRFEYSPESYTGTELEYAKQVCDAVGEVIAPTPERPIIFNLPATVEMTTPNVYADSIEWMSRNLANRESVILSLHPHNDRGTAVAAAELGFAAGADRIEGCLFGNGERTGNVCLVTLGLNLFSRGVDPQIDFSNIDEIRRTVEYCNQLPVHERHPYGGDLVYTAFSGSHQDAINKGLDAMKLDADAADCDVDDMLWQVPYLPIDPRDVGRTYEAVIRVNSQSGKGGVAYIMKTDHGLSLPRRLQIEFSQVIQKIAEGTAGEGGEVSPKEMWDAFAEEYLAPVRPLERIRQHVDAADDDGGTTSITATVKINGVETEISGSGNGPLAAFVHALADVGFDVAVLDYYEHAMSAGDDAQAAAYVEASVTIASPAQPGEAGRHASDPVTIASPAQPGEAGRHASDPVTSKTVWGVGIAPSITTASLRAVVSAVNRAAR
      
Bibliography