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
Metabolic function and regulation of this protein in SubtiPathways: Phe, Tyr, Trp, His
MW, pI	39 kDa, 5.005
Gene length, protein length	1080 bp, 360 aa
Immediate neighbours	tyrA, trpA
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context

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

• 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

• 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)

• 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:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)