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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 + ETF = 2,3-dehydroacyl-CoA + reduced ETF].
ProductProbable acyl-CoA dehydrogenase FadE25
CommentsRv3274c, (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 categoryLipid metabolism
ProteomicsIdentified 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).
TranscriptomicsDNA 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).
MutantNon-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
TypeStartEndOrientation
CDS36569203658089-
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv3274c|fadE25
MVGWAGNPSFDLFKLPEEHDEMRSAIRALAEKEIAPHAAEVDEKARFPEEALVALNSSGFNAVHIPEEYGGQGADSVATCIVIEEVARVDASASLIPAVNKLGTMGLILRGSEELKKQVLPALAAEGAMASYALSEREAGSDAASMRTRAKADGDHWILNGAKCWITNGGKSTWYTVMAVTDPDRGANGISAFMVHKDDEGFTVGPKERKLGIKGSPTTELYFENCRIPGDRIIGEPGTGFKTALATLDHTRPTIGAQAVGIAQGALDAAIAYTKDRKQFGESISTFQAVQFMLADMAMKVEAARLMVYSAAARAERGEPDLGFISAASKCFASDVAMEVTTDAVQLFGGAGYTTDFPVERFMRDAKITQIYEGTNQIQRVVMSRALLR
      
Bibliography