Difference between revisions of "AroA"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
{{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}}, | {{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}}, | ||
| − | {{SubtiWiki category|[[phosphoproteins]]}} | + | {{SubtiWiki category|[[phosphoproteins]]}}, |
| + | [[most abundant proteins]] | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
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=== Additional information=== | === Additional information=== | ||
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=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
| − | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
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| − | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' subject to feedback inhibition [http://www.ncbi.nlm.nih.gov/sites/entrez/19258532 PubMed] | * '''Effectors of protein activity:''' subject to feedback inhibition [http://www.ncbi.nlm.nih.gov/sites/entrez/19258532 PubMed] | ||
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* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=aroA_3045445_3046521_-1 aroA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=aroA_3045445_3046521_-1 aroA] {{PubMed|22383849}} | ||
| − | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
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* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| − | * '''Additional information:''' subject to feedback inhibition [http://www.ncbi.nlm.nih.gov/sites/entrez/19258532 PubMed] | + | * '''Additional information:''' |
| + | ** subject to feedback inhibition [http://www.ncbi.nlm.nih.gov/sites/entrez/19258532 PubMed] | ||
| + | ** belongs to the 100 [[most abundant proteins]] {{PubMed|15378759}} | ||
=Biological materials = | =Biological materials = | ||
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=References= | =References= | ||
| − | <pubmed>22938038,9387221,19258532 ,17726680 17218307, 22517742</pubmed> | + | <pubmed>22938038,9387221,19258532 ,17726680 17218307, 22517742 15378759</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 12:53, 5 March 2014
- Description: 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase / chorismate mutase-isozyme 3
| Gene name | aroA |
| Synonyms | aroG |
| Essential | no |
| Product | 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase /
chorismate mutase-isozyme 3 |
| Function | biosynthesis of aromatic amino acids |
| Gene expression levels in SubtiExpress: aroA | |
| Metabolic function and regulation of this protein in SubtiPathways: aroA | |
| MW, pI | 39 kDa, 5.341 |
| Gene length, protein length | 1074 bp, 358 aa |
| Immediate neighbours | ccpA, ytxJ |
| Sequences | Protein DNA DNA_with_flanks |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids, phosphoproteins, most abundant proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU29750
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Phosphoenolpyruvate + D-erythrose 4-phosphate + H2O = 3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate + phosphate (according to Swiss-Prot)
- Protein family: class-I DAHP synthetase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity: subject to feedback inhibition PubMed
Database entries
- Structure: 1VR6 (from Thermotoga maritima, 51% identity, 68% similarity)
- UniProt: P39912
- KEGG entry: [3]
- E.C. number: 2.5.1.54 5 and 5.4.99.5
Additional information
Expression and regulation
- Regulation:
- Regulatory mechanism:
- Additional information:
- subject to feedback inhibition PubMed
- belongs to the 100 most abundant proteins PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Bui Khanh Chi, Alexandra A Roberts, Tran Thi Thanh Huyen, Katrin Bäsell, Dörte Becher, Dirk Albrecht, Chris J Hamilton, Haike Antelmann
S-bacillithiolation protects conserved and essential proteins against hypochlorite stress in firmicutes bacteria.
Antioxid Redox Signal: 2013, 18(11);1273-95
[PubMed:22938038]
[WorldCat.org]
[DOI]
(I p)
Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742]
[WorldCat.org]
[DOI]
(I p)
Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532]
[WorldCat.org]
[DOI]
(I p)
Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680]
[WorldCat.org]
[DOI]
(P p)
Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307]
[WorldCat.org]
[DOI]
(P p)
Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759]
[WorldCat.org]
[DOI]
(P p)
Alia Lapidus, Nathalie Galleron, Alexei Sorokin, S Dusko Ehrlich
Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region.
Microbiology (Reading): 1997, 143 ( Pt 11);3431-3441
[PubMed:9387221]
[WorldCat.org]
[DOI]
(P p)
