Difference between revisions of "HisC"
Line 78: | Line 78: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' | + | * '''[[SubtInteract|Interactions]]:''' |
− | * '''Localization:''' | + | * '''[[Localization]]:''' |
=== Database entries === | === Database entries === | ||
Line 104: | Line 104: | ||
* '''Regulation:''' | * '''Regulation:''' | ||
− | ** induction by tryptophan ([[MtrB| TRAP]]) {{PubMed|1551827}} | + | ** induction by tryptophan ([[MtrB|TRAP]]) {{PubMed|1551827}} |
* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
− | ** [[MtrB| TRAP]]: binding to the mRNA in the presence of tryptophan, this results in transcription termination {{PubMed|8419914}} | + | ** [[MtrB|TRAP]]: binding to the mRNA in the presence of tryptophan, this results in transcription termination {{PubMed|8419914}} |
* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** the mRNA is substantially stabilized upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}} | ||
=Biological materials = | =Biological materials = | ||
Line 130: | Line 131: | ||
=References= | =References= | ||
+ | <big>''Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J'' </big> | ||
+ | <big>'''RNA processing in ''Bacillus subtilis'': identification of targets of the essential RNase Y.''' </big> | ||
+ | <big>Mol Microbiol. 2011 81(6): 1459-1473. </big> | ||
+ | [http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947] | ||
<pubmed> 4431, 824269 11518529 3924737 6436812 1551827 8419914</pubmed> | <pubmed> 4431, 824269 11518529 3924737 6436812 1551827 8419914</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 18:29, 19 November 2011
- 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