HisC

From SubtiWiki
Jump to: navigation, search
  • 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
HisC context.gif
Expression at a glance   PubMed
HisC expression.png















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

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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:

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • 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:

Labs working on this gene/protein

Your additional remarks

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] (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] (P p)