Difference between revisions of "HisC"
Line 45: | Line 45: | ||
* '''Locus tag:''' BSU22620 | * '''Locus tag:''' BSU22620 | ||
+ | |||
+ | [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=hisC_2370415_2371497_-1 Expression] | ||
===Phenotypes of a mutant === | ===Phenotypes of a mutant === |
Revision as of 12:33, 25 January 2012
- 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 |
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids
This gene is a member of the following regulons
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
- Swiss prot entry: P17731
- KEGG entry: [3]
- E.C. number: 2.6.1.9
Additional information
Expression and regulation
- Operon:
- Regulatory mechanism:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. Mol Microbiol. 2011 81(6): 1459-1473. PubMed:21815947