Difference between revisions of "AroE"
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<big>Mol Microbiol. 2011 81(6): 1459-1473. </big> | <big>Mol Microbiol. 2011 81(6): 1459-1473. </big> | ||
[http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947] | [http://www.ncbi.nlm.nih.gov/pubmed/21815947 PubMed:21815947] | ||
− | <pubmed>,3106153, </pubmed> | + | <pubmed>3924737,3106153,6436812 1551827 8419914</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 20:20, 19 November 2011
- Description: 3-phosphoshikimate 1-carboxyvinyltransferase
Gene name | aroE |
Synonyms | |
Essential | no |
Product | 3-phosphoshikimate 1-carboxyvinyltransferase |
Function | biosynthesis of aromatic amino acids |
Metabolic function and regulation of this protein in SubtiPathways: Phe, Tyr, Trp | |
MW, pI | 45 kDa, 6.341 |
Gene length, protein length | 1284 bp, 428 aa |
Immediate neighbours | ypiA, tyrA |
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: BSU22600
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate (according to Swiss-Prot)
- Protein family: ABC transporter 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
- Structure: 3RMT (from B. halodurans, 68% identity, 87% similarity)
- UniProt: P20691
- KEGG entry: [3]
- E.C. number: 2.5.1.19
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
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, 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)
D J Henner, L Band, G Flaggs, E Chen
The organization and nucleotide sequence of the Bacillus subtilis hisH, tyrA and aroE genes.
Gene: 1986, 49(1);147-52
[PubMed:3106153]
[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)