TrpE
- Description: anthranilate synthase (subunit I)
Gene name | trpE |
Synonyms | |
Essential | no |
Product | anthranilate synthase (subunit I) |
Function | biosynthesis of tryptophan |
Metabolic function and regulation of this protein in SubtiPathways: Phe, Tyr, Trp | |
MW, pI | 57 kDa, 5.246 |
Gene length, protein length | 1545 bp, 515 aa |
Immediate neighbours | trpD, aroH |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU22680
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity: subject to feedback inhibtion by tryptophan PubMed
- Localization:
Database entries
- UniProt: P03963
- KEGG entry: [3]
- E.C. number: 4.1.3.27
Additional information
Expression and regulation
- Regulatory mechanism:
- Additional information:
- subject to feedback inhibtion by tryptophan PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
The trpE RNA switch
Alexander V Yakhnin, Paul Babitzke
Mechanism of NusG-stimulated pausing, hairpin-dependent pause site selection and intrinsic termination at overlapping pause and termination sites in the Bacillus subtilis trp leader.
Mol Microbiol: 2010, 76(3);690-705
[PubMed:20384694]
[WorldCat.org]
[DOI]
(I p)
Adam P McGraw, Ali Mokdad, François Major, Philip C Bevilacqua, Paul Babitzke
Molecular basis of TRAP-5'SL RNA interaction in the Bacillus subtilis trp operon transcription attenuation mechanism.
RNA: 2009, 15(1);55-66
[PubMed:19033375]
[WorldCat.org]
[DOI]
(I p)
Adam P McGraw, Philip C Bevilacqua, Paul Babitzke
TRAP-5' stem loop interaction increases the efficiency of transcription termination in the Bacillus subtilis trpEDCFBA operon leader region.
RNA: 2007, 13(11);2020-33
[PubMed:17881743]
[WorldCat.org]
[DOI]
(P p)
Paul Gollnick, Paul Babitzke, Alfred Antson, Charles Yanofsky
Complexity in regulation of tryptophan biosynthesis in Bacillus subtilis.
Annu Rev Genet: 2005, 39;47-68
[PubMed:16285852]
[WorldCat.org]
[DOI]
(P p)
Gintaras Deikus, Paul Babitzke, David H Bechhofer
Recycling of a regulatory protein by degradation of the RNA to which it binds.
Proc Natl Acad Sci U S A: 2004, 101(9);2747-51
[PubMed:14976255]
[WorldCat.org]
[DOI]
(P p)
Paul Babitzke, Janell Schaak, Alexander V Yakhnin, Philip C Bevilacqua
Role of RNA structure in transcription attenuation in Bacillus subtilis: the trpEDCFBA operon as a model system.
Methods Enzymol: 2003, 371;392-404
[PubMed:14712717]
[WorldCat.org]
[DOI]
(P p)
Janell E Schaak, Helen Yakhnin, Philip C Bevilacqua, Paul Babitzke
A Mg2+-dependent RNA tertiary structure forms in the Bacillus subtilis trp operon leader transcript and appears to interfere with trpE translation control by inhibiting TRAP binding.
J Mol Biol: 2003, 332(3);555-74
[PubMed:12963367]
[WorldCat.org]
[DOI]
(P p)
H Yakhnin, J E Babiarz, A V Yakhnin, P Babitzke
Expression of the Bacillus subtilis trpEDCFBA operon is influenced by translational coupling and Rho termination factor.
J Bacteriol: 2001, 183(20);5918-26
[PubMed:11566991]
[WorldCat.org]
[DOI]
(P p)
H Du, A V Yakhnin, S Dharmaraj, P Babitzke
trp RNA-binding attenuation protein-5' stem-loop RNA interaction is required for proper transcription attenuation control of the Bacillus subtilis trpEDCFBA operon.
J Bacteriol: 2000, 182(7);1819-27
[PubMed:10714985]
[WorldCat.org]
[DOI]
(P p)
E Merino, P Babitzke, C Yanofsky
trp RNA-binding attenuation protein (TRAP)-trp leader RNA interactions mediate translational as well as transcriptional regulation of the Bacillus subtilis trp operon.
J Bacteriol: 1995, 177(22);6362-70
[PubMed:7592410]
[WorldCat.org]
[DOI]
(P p)
P Babitzke, J T Stults, S J Shire, C Yanofsky
TRAP, the trp RNA-binding attenuation protein of Bacillus subtilis, is a multisubunit complex that appears to recognize G/UAG repeats in the trpEDCFBA and trpG transcripts.
J Biol Chem: 1994, 269(24);16597-604
[PubMed:7515880]
[WorldCat.org]
(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, C Yanofsky
Reconstitution of Bacillus subtilis trp attenuation in vitro with TRAP, the trp RNA-binding attenuation protein.
Proc Natl Acad Sci U S A: 1993, 90(1);133-7
[PubMed:7678334]
[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)
M I Kuroda, D Henner, C Yanofsky
cis-acting sites in the transcript of the Bacillus subtilis trp operon regulate expression of the operon.
J Bacteriol: 1988, 170(7);3080-8
[PubMed:3133360]
[WorldCat.org]
[DOI]
(P p)
H Shimotsu, M I Kuroda, C Yanofsky, D J Henner
Novel form of transcription attenuation regulates expression the Bacillus subtilis tryptophan operon.
J Bacteriol: 1986, 166(2);461-71
[PubMed:2422155]
[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)
E W Nester, R A Jensen
Control of aromatic acid biosynthesis in Bacillus subtilis: sequenial feedback inhibition.
J Bacteriol: 1966, 91(4);1594-8
[PubMed:4956345]
[WorldCat.org]
[DOI]
(P p)