Difference between revisions of "TrpA"
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* '''Locus tag:''' BSU22630 | * '''Locus tag:''' BSU22630 | ||
+ | |||
+ | [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=trpA_2371508_2372311_-1 Expression] | ||
===Phenotypes of a mutant === | ===Phenotypes of a mutant === |
Revision as of 12:34, 25 January 2012
- Description: tryptophan synthase (alpha subunit)
Gene name | trpA |
Synonyms | |
Essential | no |
Product | tryptophan synthase (alpha subunit) |
Function | biosynthesis of tryptophan |
Interactions involving this protein in SubtInteract: TrpA | |
Metabolic function and regulation of this protein in SubtiPathways: Phe, Tyr, Trp | |
MW, pI | 29 kDa, 4.817 |
Gene length, protein length | 801 bp, 267 aa |
Immediate neighbours | hisC, trpB |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
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: BSU22630
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O (according to Swiss-Prot)
- Protein family: UPF0403 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
- UniProt: P07601
- KEGG entry: [3]
- E.C. number: 4.2.1.20
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
Reviews
Original publications
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