LeuC

• Description: 3-isopropylmalate dehydratase (large subunit)
  
  

Gene name	leuC
Synonyms
Essential	no
Product	3-isopropylmalate dehydratase (large subunit)
Function	biosynthesis of leucine
Gene expression levels in SubtiExpress: leuC
Metabolic function and regulation of this protein in SubtiPathways: leuC
MW, pI	52 kDa, 6.127
Gene length, protein length	1416 bp, 472 aa
Immediate neighbours	leuD, leuB
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

CcpA regulon, CodY regulon, FsrA regulon, T-box, TnrA regulon

The gene

Basic information

• Locus tag: BSU28260

Database entries

• BsubCyc: BSU28260

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: (2R,3S)-3-isopropylmalate = (2S)-2-isopropylmaleate + H₂O (according to Swiss-Prot)

• Protein family: LeuC type 1 subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-81 PubMed

• Cofactors: contains an iron-sulfur cluster

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU28260

• Structure:

• UniProt: P80858

• KEGG entry: [3]

• E.C. number: 4.2.1.33

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon: ilvB-ilvH-ilvC-leuA-leuB-leuC-leuD PubMed

• Expression browser: leuC PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • for a complete overview on the regulation of the ilv operon, see Brinsmade et al.
  • repressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
  • repressed during growth in the presence of branched chain amino acids (CodY) PubMed
  • repressed by casamino acids PubMed
  • expression is stimulated in the presence of glucose PubMed
  • less expressed under conditions of extreme iron limitation (FsrA) PubMed

• Regulatory mechanism:
  • TnrA: transcription repression PubMed
  • CodY: transcription repression PubMed
  • glucose regulation: CcpA PubMed
  • repression by BCAA: tRNA-controlled RNA switch (T-box) that mediates termination/antitermination
  • FsrA: translational repression PubMed

• Additional information:
  • subject to Clp-dependent proteolysis upon glucose starvation PubMed
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 751 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 360 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1636 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 1150 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 741 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody: