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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 supposedly involved in lipid degradation (beta oxidation).
ProductProbable beta-ketoacyl CoA thiolase FadA3
CommentsRv1074c, (MTV017.27c), len: 405 aa. Probable fadA3, beta-ketoacyl CoA thiolase, highly similar to many involved in beta-oxidation e.g. CAB89028.1|AL353870 beta-ketoadipyl-CoA thiolase from Streptomyces coelicolor (395 aa); P77525|PAAJ_ECOLI probable beta-ketoadipyl CoA thiolase from Escherichia coli (401 aa), FASTA scores: opt: 1034, E(): 5.4e-56, (43.5% identity in 416 aa overlap) and X97452 acetyl-CoA acetyltransferase (thiolase) from Escherichia coli (401 aa), FASTA scores: opt: 1043, E(): 0, (43.4% identity in 415 aa overlap); Q43935|CATF_ACICA beta-ketoadipyl CoA thiolase from Acinetobacter calcoaceticus (401 aa), FASTA scores: opt: 992, E(): 0, (41.5% identity in 415 aa overlap); etc. Contains PS00737 Thiolases signature 2, and PS00445 FGGY family of carbohydrate kinases signature 2, although this is probably fortuitous. Belongs to the thiolase family.
Functional categoryLipid metabolism
ProteomicsThe product of this CDS corresponds to spot 1_18 identified in culture supernatant by proteomics at the Max Planck Institute for Infection Biology, Berlin, Germany (see citations below). 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 culture filtrates of M. tuberculosis H37Rv (See Malen et al., 2007). 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).
MutantNon-essential gene for in vitro growth of H37Rv in a MtbYM rich medium, by Himar1 transposon mutagenesis (see Minato et al. 2019). Disruption of this gene provides a growth advantage 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 strain (see Sassetti et al., 2003). Non-essential gene for in vitro growth of H37Rv, by Himar1 transposon mutagenesis (See Griffin et al., 2011).
Check for mutants available at TARGET website
Coordinates
TypeStartEndOrientation
CDS11981561199373-
Genomic sequence
Feature type Upstream flanking region (bp) Downstream flanking region (bp) Update
       
Protein sequence
>Mycobacterium tuberculosis H37Rv|Rv1074c|fadA3
MPEAVIVSTARSPIGRAMKGSLVGMRPDDLAVQMVRAALDKVPALNPHQIDDLMMGCGLPGGESGFNIARVVAVALGYDFLPGTTVNRYCSSSLQTTRMAFHAIKAGEGDAFISAGVETVSRFAKGNSDSWPDTKNPLFDGAQERSAAAAAGADEWHDPRTDQKLPDIYIAMGQTAENVAIMTGISREEQDRWGVRSQNRAEEAIKNGFFEREITPVTLPDGTTVSTDDGPRPGTTYEKVSELKPAFRPNGTVTAGNACPLNDGAAAVVITSDTKAKELGLTPLARIVSTGVSGLSPEIMGLGPIEASKKALERAGMAITDIDLVEINEAFAVQVLGSARELGIDEDKLNISGGAIALGHPFGMTGARITTTLLNNLQTYDKTFGLETMCVGGGQGMAMVIERLA
      
Bibliography