Difference between revisions of "TrpA"
Line 56: | Line 56: | ||
=== Additional information=== | === Additional information=== | ||
− | |||
− | |||
Line 82: | Line 80: | ||
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
− | * '''Interactions:''' [[TrpA]]-[[TrpB]] | + | * '''[[SubtInteract|Interactions]]:''' [[TrpA]]-[[TrpB]] |
− | * '''Localization:''' | + | * '''[[Localization]]:''' |
=== Database entries === | === Database entries === | ||
Line 113: | Line 111: | ||
* '''Additional information:''' | * '''Additional information:''' | ||
+ | ** the mRNA is substantially stabilized upon depletion of [[Rny|RNase Y]] {{PubMed|21815947}} | ||
=Biological materials = | =Biological materials = | ||
Line 136: | Line 135: | ||
<pubmed> 18486479 11893063 11163353 7900177 19387555 </pubmed> | <pubmed> 18486479 11893063 11163353 7900177 19387555 </pubmed> | ||
==Original publications== | ==Original publications== | ||
+ | <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> 14976255, 3924737, 6436812,2422155,8419914, 1551827 </pubmed> | <pubmed> 14976255, 3924737, 6436812,2422155,8419914, 1551827 </pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 18:29, 19 November 2011
- 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
Samanta Raboni, Stefano Bettati, Andrea Mozzarelli
Tryptophan synthase: a mine for enzymologists.
Cell Mol Life Sci: 2009, 66(14);2391-403
[PubMed:19387555]
[WorldCat.org]
[DOI]
(I p)
Michael F Dunn, Dimitri Niks, Huu Ngo, Thomas R M Barends, Ilme Schlichting
Tryptophan synthase: the workings of a channeling nanomachine.
Trends Biochem Sci: 2008, 33(6);254-64
[PubMed:18486479]
[WorldCat.org]
[DOI]
(P p)
E W Miles
Tryptophan synthase: a multienzyme complex with an intramolecular tunnel.
Chem Rec: 2001, 1(2);140-51
[PubMed:11893063]
[WorldCat.org]
[DOI]
(P p)
N K Nagradova
Interdomain interactions in oligomeric enzymes: creation of asymmetry in homo-oligomers and role in metabolite channeling between active centers of hetero-oligomers.
FEBS Lett: 2001, 487(3);327-32
[PubMed:11163353]
[WorldCat.org]
[DOI]
(P p)
E W Miles
Tryptophan synthase. Structure, function, and protein engineering.
Subcell Biochem: 1995, 24;207-54
[PubMed:7900177]
[WorldCat.org]
(P p)
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