Gene Rv3274c
in Mycobacterium tuberculosis H37Rv
General annotation
Type | CDS |
Function | Function unknown, but involved in lipid degradation [catalytic activity: acyl-CoA + ETF = 2,3-dehydroacyl-CoA + reduced ETF]. |
Product | Probable acyl-CoA dehydrogenase FadE25 |
Comments | Rv3274c, (MTCY71.14c), len: 389 aa. Probable fadE25, Acyl-CoA Dehydrogenase, equivalent to P46703|ACDP_MYCLE|FADE25|ACD|ML0737|B1308_F1_34 probable acyl-CoA dehydrogenase FADE25 from Mycobacterium leprae (389 aa), FASTA scores: opt: 2394, E(): 3.8e-143, (92.05% identity in 389 aa overlap). Also similar to many e.g. Q9RIQ5|fade fatty acid acyl-CoA dehydrogenase from Streptomyces lividans (385 aa), FASTA scores: opt: 1692, E(): 4.9e-99, (67.35% identity in 383 aa overlap); P45867|ACDA_BACSU|ACD from Bacillus subtilis (379 aa), FASTA scores: opt: 1212, E(): 7.2e-69, (51.85% identity in 376 aa overlap); Q9K6D1|ACDA|BH3798 from Bacillus halodurans (380 aa), FASTA scores: opt: 1209, E(): 1.1e-68, (51.7% identity in 377 aa overlap); P52042|ACDS_CLOAB|BCD from Clostridium acetobutylicum (379 aa), FASTA scores: opt: 1056, E(): 4.6e-59, (44.6% identity in 379 aa overlap); etc. Contains PS00072 Acyl-CoA dehydrogenases signature 1, PS00073 Acyl-CoA dehydrogenases signature 2. Belongs to the acyl-CoA dehydrogenases family. |
Functional category | Lipid metabolism |
Proteomics | Identified by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany (See Jungblut et al., 1999). 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 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 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 de Souza et al., 2011) (See Kelkar et al., 2011). |
Transcriptomics | DNA microarrays detect expression in M. tuberculosis H37Rv in vivo (in BALB/c and SCID mice) but not in vitro (in 7H9 medium) (See Talaat et al., 2004). |
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). Non essential gene by Himar1 transposon mutagenesis in CDC1551 strain (see Lamichhane et al., 2003). Non-essential gene for in vitro growth of H37Rv, but essential for in vitro growth on cholesterol; by sequencing of Himar1-based transposon mutagenesis (See Griffin et al., 2011). Check for mutants available at TARGET website |
Coordinates
Type | Start | End | Orientation |
---|---|---|---|
CDS | 3656920 | 3658089 | - |
Genomic sequence
Feature type
Upstream flanking region (bp)
Downstream flanking region (bp)
Update
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3274c|fadE25 MVGWAGNPSFDLFKLPEEHDEMRSAIRALAEKEIAPHAAEVDEKARFPEEALVALNSSGFNAVHIPEEYGGQGADSVATCIVIEEVARVDASASLIPAVNKLGTMGLILRGSEELKKQVLPALAAEGAMASYALSEREAGSDAASMRTRAKADGDHWILNGAKCWITNGGKSTWYTVMAVTDPDRGANGISAFMVHKDDEGFTVGPKERKLGIKGSPTTELYFENCRIPGDRIIGEPGTGFKTALATLDHTRPTIGAQAVGIAQGALDAAIAYTKDRKQFGESISTFQAVQFMLADMAMKVEAARLMVYSAAARAERGEPDLGFISAASKCFASDVAMEVTTDAVQLFGGAGYTTDFPVERFMRDAKITQIYEGTNQIQRVVMSRALLR
Bibliography
- Jungblut PR, Schaible UE, Mollenkopf HJ, Zimny-Arndt U, Raupach B, Mattow J, Halada P, Lamer S, Hagens K and Kaufmann SH [1999]. Comparative proteome analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG strains: towards functional genomics of microbial pathogens. Proteomics
- Gu S et al. [2003]. Comprehensive proteomic profiling of the membrane constituents of a Mycobacterium tuberculosis strain. Proteomics
- Lamichhane G et al. [2003]. A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis. Mutant
- Talaat AM et al. [2004]. The temporal expression profile of Mycobacterium tuberculosis infection in mice. Transcriptome
- Xiong Y, Chalmers MJ, Gao FP, Cross TA and Marshall AG [2005]. Identification of Mycobacterium tuberculosis H37Rv integral membrane proteins by one-dimensional gel electrophoresis and liquid chromatography electrospray ionization tandem mass spectrometry. Proteomics
- Mawuenyega KG et al. [2005]. Mycobacterium tuberculosis functional network analysis by global subcellular protein profiling. 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
- Griffin JE et al. [2011]. High-resolution phenotypic profiling defines genes essential for mycobacterial growth and cholesterol catabolism. Mutant
- de Souza GA et al. [2011]. Proteogenomic analysis of polymorphisms and gene annotation divergences in prokaryotes using a clustered mass spectrometry-friendly database. Proteomics Sequence
- 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