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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
FunctionFunction unknown, but involved in lipid degradation [catalytic activity: acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA].
ProductProbable acetyl-CoA acyltransferase FadA2 (3-ketoacyl-CoA thiolase) (beta-ketothiolase)
CommentsRv0243, (MTV034.09), len: 440 aa. Probable fadA2, acetyl-CoA acyltransferase (3-acyl-CoA thiolase), equivalent, but shorter 17 aa, to AL022486|MLCB1883_14T44879 acetyltransferase from Mycobacterium leprae (457 aa), FASTA scores: opt: 250 7, E(): 0, (87.6% identity in 435 aa overlap). Also highly similar to many e.g. G83046|PA478 probable acyl-CoA thiolase from Pseudomonas aeruginosa (425 aa); AB77293.1|AL160312 putative ketoacyl CoA thiolase from Streptomyces coelicolor (428 aa); P76503|7449731|YFCY_ECOLI|D65007|B2342 probable 3-ketoacyl-CoA thiolase (acetyl-CoA acyltransferase) (beta-ketothiolase) from Escherichia coli strain K-12 (436 aa), FASTA scores: opt: 914, E(): 0, (38.2% identity in 434 aa overlap); P55084|ECHB_HUMAN mitochondrial trifunctonal enzyme (474 aa), FASTA scores: opt: 881, E(): 0, (37.7 identity in 451 aa overlap). Contains PS00099 Thiolases active site. Belongs to the thiolase family.
Functional categoryLipid metabolism
ProteomicsIdentified in Triton X-114 extracts of M. tuberculosis H37Rv membranes using 2DGE and MALDI-MS (See Sinha et al., 2002). 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 culture supernatant of M. tuberculosis H37Rv using mass spectrometry (See Mattow et al., 2003). Identified in the cytosol and cell membrane fraction of M. tuberculosis H37Rv using 2DLC/MS (See Mawuenyega et al., 2005). Identified in the membrane fraction of M. tuberculosis H37Rv using nanoLC-MS/MS (See Xiong et al., 2005). Identified in the detergent phase of Triton X-114 extracts of M. tuberculosis H37Rv membranes using 1-DGE and MALDI-TOF-MS (See Sinha 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).
MutantNon-essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Non-essential gene for in vitro growth of H37Rv, by analysis of saturated Himar1 transposon libraries (see DeJesus et al. 2017). Non essential gene by Himar1 transposon mutagenesis in H37Rv and CDC1551 strains (see Sassetti et al., 2003 and Lamichhane et al., 2003).
Check for mutants available at TARGET website
Coordinates
TypeStartEndOrientation
CDS292171293493+
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv0243|fadA2
VAPAAKNTSQTRRRVAVLGGNRIPFARSDGAYADASNQDMFTAALSGLVDRFGLAGERLDMVVGGAVLKHSRDFNLMRECVLGSELSPYTPAFDLQQACGTGLQAAIAAADGIAAGRYEVAAAGGVDTTSDPPIGLGDDLRRTLLKLRRSRSNVQRLKLVGTLPASLGVEIPANSEPRTGLSMGEHAAVTAKQMGIKRVDQDELAAASHRNMADAYDRGFFDDLVSPFLGLYRDDNLRPNSSVEKLATLRPVFGVKAGDATMTAGNSTPLTDGASVALLASEQWAEAHSLAPLAYLVDAETAAVDYVNGNDGLLMAPTYAVPRLLARNGLSLQDFDFYEIHEAFASVVLAHLAAWESEEYCKRRLGLDAALGSIDRSKLNVNGSSLAAGHPFAATGGRILAQTAKQLAEKKAAKKGGGPLRGLISICAAGGQGVAAILEA
      
Bibliography