HisC

• Description: histidinol-phosphate aminotransferase / tyrosine and phenylalanine aminotransferase
  
  

Gene name	hisC
Synonyms	aroJ
Essential	no
Product	histidinol-phosphate aminotransferase / tyrosine and phenylalanine aminotransferase
Function	biosynthesis of aromatic amino acids
Gene expression levels in SubtiExpress: hisC
Metabolic function and regulation of this protein in SubtiPathways: hisC
MW, pI	39 kDa, 5.005
Gene length, protein length	1080 bp, 360 aa
Immediate neighbours	tyrA, trpA
Sequences	Protein DNA DNA_with_flanks
Genetic context
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

This gene is a member of the following regulons

TRAP regulon

The gene

Basic information

• Locus tag: BSU22620

Database entries

• BsubCyc: BSU22620

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: L-histidinol phosphate + 2-oxoglutarate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate (according to Swiss-Prot)

• Protein family: bacterial solute-binding protein 3 family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU22620

• Structure: 1UU0 (the enzyme from E. coli) PubMed

• Swiss prot entry: P17731

• KEGG entry: [3]

• E.C. number: 2.6.1.9

Expression and regulation

• Operon:
  • aroF-aroB-aroH-trpE-trpD-trpC-trpF-trpB-trpA-hisC-tyrA-aroE (according to DBTBS)
  • trpE-trpD-trpC-trpF-trpB-trpA-hisC-tyrA-aroE PubMed
  • hisC-tyrA-aroE (according to DBTBS)

• Expression browser: hisC PubMed

• Sigma factor:
  • trpE: SigA PubMed

• Regulation:
  • induction by tryptophan (TRAP) PubMed

• Regulatory mechanism:
  • TRAP: binding to the mRNA in the presence of tryptophan, this results in transcription termination PubMed

• Additional information:
  • the mRNA is substantially stabilized upon depletion of RNase Y PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 2715 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 2096 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4023 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2507 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 6242 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Martin Bommer, John M Ward
A 1-step microplate method for assessing the substrate range of l-α-amino acid aminotransferase.
Enzyme Microb Technol: 2013, 52(4-5);218-25
[PubMed:23540922] [WorldCat.org] [DOI] (I p)

Martin Lehnik-Habrink, Marc Schaffer, Ulrike Mäder, Christine Diethmaier, Christina Herzberg, Jörg Stülke
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y.
Mol Microbiol: 2011, 81(6);1459-73
[PubMed:21815947] [WorldCat.org] [DOI] (I p)

J Sivaraman, Y Li, R Larocque, J D Schrag, M Cygler, A Matte
Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate.
J Mol Biol: 2001, 311(4);761-76
[PubMed:11518529] [WorldCat.org] [DOI] (P p)

J Otridge, P Gollnick
MtrB from Bacillus subtilis binds specifically to trp leader RNA in a tryptophan-dependent manner.
Proc Natl Acad Sci U S A: 1993, 90(1);128-32
[PubMed:8419914] [WorldCat.org] [DOI] (P p)

P Babitzke, P Gollnick, C Yanofsky
The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis.
J Bacteriol: 1992, 174(7);2059-64
[PubMed:1551827] [WorldCat.org] [DOI] (P p)

D J Henner, L Band, H Shimotsu
Nucleotide sequence of the Bacillus subtilis tryptophan operon.
Gene: 1985, 34(2-3);169-77
[PubMed:3924737] [WorldCat.org] [DOI] (P p)

H Shimotsu, D J Henner
Characterization of the Bacillus subtilis tryptophan promoter region.
Proc Natl Acad Sci U S A: 1984, 81(20);6315-9
[PubMed:6436812] [WorldCat.org] [DOI] (P p)

D A Weigent, E W Nester
Regulation of histidinol phosphate aminotransferase synthesis by tryptophan in Bacillus subtilis.
J Bacteriol: 1976, 128(1);202-11
[PubMed:824269] [WorldCat.org] [DOI] (P p)

E W Nester, A L Montoya
An enzyme common to histidine and aromatic amino acid biosynthesis in Bacillus subtilis.
J Bacteriol: 1976, 126(2);699-705
[PubMed:4431] [WorldCat.org] [DOI] (P p)