Gene Rv1679
in Mycobacterium tuberculosis H37Rv
General annotation
Type | CDS |
Function | Function unknown, but involvement in lipid degradation. |
Product | Possible acyl-CoA dehydrogenase FadE16 |
Comments | Rv1679, (MTV047.14, MTCI125.01), len: 373 aa. Possible fadE16, acyl-CoA dehydrogenase, similar to acyl/butyryl-CoA dehydrogenases e.g. NP_244665.1|NC_002570 acyl-CoA dehydrogenase from Bacillus halodurans (380 aa); NP_000008.1|NM_000017 acyl-Coenzyme A dehydrogenase from Homo sapiens (412 aa); Z99113|BSUB0010_119 from Bacillus subtilis (380 aa), FASTA scores: opt: 439, E(): 3.4e-20, (29.6% identity in 287 aa overlap); etc. Weakly similar to many dehydrogenases and to P31571|CAIA_ECOLI probable carnitine operon oxidoreductase from Escherichia coli (380 aa), FASTA scores: opt: 109, E(): 0.0066, (28.6% identity in 98 aa overlap). |
Functional category | Lipid metabolism |
Proteomics | Identified by proteomics (See Rosenkrands et al., 2000). Identified 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 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 membrane protein fraction and whole cell lysates of M. tuberculosis H37Rv but not the culture filtrate (See de Souza et al., 2011). Translational start site supported by proteomics data (See Kelkar et al., 2011). |
Mutant | Non-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). Check for mutants available at TARGET website |
Coordinates
Type | Start | End | Orientation |
---|---|---|---|
CDS | 1903299 | 1904420 | + |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv1679|fadE16 MATPGVVQEVVSVAAEHAERVDTDCAFPAEAVDALRKTGLLGLVLPREIGGMGSGPVEFTEVVAQLSAACGSTAMIYLMHMAAAVTVAASPPPGLPDLLADMASGKQLGTLAFSEPGSRSHFWAPVSTASADGDGIAVRADKSWVTSAGFADVYVVSVGSADGAAGDVDLYAVPADTPGLRVAGTFTGMGLRGNASAPMAVDIRIPDSYRLGEAGGGFGIMMQTVLPWFNLGNAAVSLGLATAATGAAVKHVGTARLEHLGGSLAELPTIRAQIARMGTTLAAQKAYLEVAANSVSSPDDTTLTHVLGVKASVNDAALTITESAMRVCGGAAFSKHLPIERAFRDARAGSVMAPTADALYDFYGRAVTGLPLF
Bibliography
- Rosenkrands I et al. [2000]. Towards the proteome of Mycobacterium tuberculosis. Proteomics
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Kruh NA et al. [2010]. Portrait of a pathogen: the Mycobacterium tuberculosis proteome in vivo. Proteomics
- MÃ¥len H et al. [2010]. Definition of novel cell envelope associated proteins in Triton X-114 extracts of Mycobacterium tuberculosis H37Rv. Proteomics
- Kelkar DS et al. [2011]. Proteogenomic analysis of Mycobacterium tuberculosis by high resolution mass spectrometry. Proteomics Sequence
- de Souza GA et al. [2011]. Bacterial proteins with cleaved or uncleaved signal peptides of the general secretory pathway. Proteomics
- DeJesus MA et al. [2017]. Comprehensive Essentiality Analysis of the Mycobacterium tuberculosis Genome via Saturating Transposon Mutagenesis. Mutant
- Minato Y et al. [2019]. Genomewide Assessment of Mycobacterium tuberculosis Conditionally Essential Metabolic Pathways. Mutant