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Search term: Rv0131c

General annotation | Coordinates | Sequence | Structural information | Orthologs/Cross-references | Interacting Drugs/Compounds | Bibliography
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General annotation
Gene namefadE1
Rv numberRv0131c
FunctionFunction unknown, but involved in lipid degradation.
ProductProbable acyl-CoA dehydrogenase FadE1
CommentsRv0131c, (MTCI5.05c), len: 447 aa. Probable fadE1, acyl-CoA dehydrogenase, similar to many e.g. ACDS_HUMAN|P16219 acyl-CoA dehydrogenase short-chain specific precursor (412 aa), FASTA scores: opt: 522, E(): 1.4e-23, (30.1% identity in 425 aa overlap). Also highly similar to MTCI5_28 from Mycobacterium tuberculosis.
Molecular mass (Da)50223.6
Isoelectric point7.8523
Gene length (bp)1344
Protein length447
Location (kb)158.315

Functional categorylipid metabolism

ProteomicsIdentified in the cytosol 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 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).
TranscriptomemRNA identified by microarray analysis and up-regulated after 24h and 96h of starvation (see Betts et al., 2002).
Mutationnon essential gene by Himar1-based transposon mutagenesis in H37Rv strain (see Sassetti et al., 2003). Non-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|Rv0131c|fadE1
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 Classification1.3.99.-
Gene Ontologyacyl-CoA dehydrogenase activity
FAD binding
oxidation reduction
M. bovisMb0136c
M. marinumMMAR_0331
Multiple Sequences Alignment: between orthologs

Interacting Drugs/Compounds
TDR TargetsRv0131c

Expression Data

Betts JC, Lukey PT, Robb LC, McAdam RA, Duncan K,
Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling
Mol Microbiol (2002) 43(3):717-31
Cited for: Transcriptome
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
Mawuenyega KG, Forst CV, Dobos KM, Belisle JT, Chen J, Bradbury EM, Bradbury AR, Chen X,
Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling.
Mol Biol Cell (2005) 16(1):396-404
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, 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