Difference between revisions of "SdaAA"
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* '''Modification:''' | * '''Modification:''' | ||
| − | * '''Cofactor(s):''' | + | * '''Cofactor(s):''' iron-sulfur cluster {{PubMed|22686449}} |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
* '''[[SubtInteract|Interactions]]:''' | * '''[[SubtInteract|Interactions]]:''' | ||
| + | ** [[SdaAA]]-[[SdaAB]] {{PubMed|22686449}} | ||
* '''[[Localization]]:''' | * '''[[Localization]]:''' | ||
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=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' | + | * '''Operon:''' ''[[sdaAB]]-[[sdaAA]]'' {{PubMed|22383849}} |
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sdaAA_1658930_1659832_1 sdaAA] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=sdaAA_1658930_1659832_1 sdaAA] {{PubMed|22383849}} | ||
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=References= | =References= | ||
| − | + | <pubmed>22383849 22686449</pubmed> | |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] | ||
Revision as of 11:04, 13 June 2012
- Description: L-serine deaminase
| Gene name | sdaAA |
| Synonyms | ylpA, sdaA |
| Essential | no |
| Product | L-serine deaminase (alpha chain) |
| Function | serine utilization |
| Metabolic function and regulation of this protein in SubtiPathways: Ala, Gly, Ser | |
| MW, pI | 30 kDa, 4.87 |
| Gene length, protein length | 900 bp, 300 aa |
| Immediate neighbours | sdaAB, recG |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU15860
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-serine = pyruvate + NH3 (according to Swiss-Prot)
- Protein family: iron-sulfur dependent L-serine dehydratase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s): iron-sulfur cluster PubMed
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: O34607
- KEGG entry: [2]
- E.C. number: 4.3.1.17
Additional information
Expression and regulation
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Shawei Chen, Xiao Lan Xu, Gregory A Grant
Allosteric activation and contrasting properties of L-serine dehydratase types 1 and 2.
Biochemistry: 2012, 51(26);5320-8
[PubMed:22686449]
[WorldCat.org]
[DOI]
(I p)
Pierre Nicolas, Ulrike Mäder, Etienne Dervyn, Tatiana Rochat, Aurélie Leduc, Nathalie Pigeonneau, Elena Bidnenko, Elodie Marchadier, Mark Hoebeke, Stéphane Aymerich, Dörte Becher, Paola Bisicchia, Eric Botella, Olivier Delumeau, Geoff Doherty, Emma L Denham, Mark J Fogg, Vincent Fromion, Anne Goelzer, Annette Hansen, Elisabeth Härtig, Colin R Harwood, Georg Homuth, Hanne Jarmer, Matthieu Jules, Edda Klipp, Ludovic Le Chat, François Lecointe, Peter Lewis, Wolfram Liebermeister, Anika March, Ruben A T Mars, Priyanka Nannapaneni, David Noone, Susanne Pohl, Bernd Rinn, Frank Rügheimer, Praveen K Sappa, Franck Samson, Marc Schaffer, Benno Schwikowski, Leif Steil, Jörg Stülke, Thomas Wiegert, Kevin M Devine, Anthony J Wilkinson, Jan Maarten van Dijl, Michael Hecker, Uwe Völker, Philippe Bessières, Philippe Noirot
Condition-dependent transcriptome reveals high-level regulatory architecture in Bacillus subtilis.
Science: 2012, 335(6072);1103-6
[PubMed:22383849]
[WorldCat.org]
[DOI]
(I p)
