Difference between revisions of "MoeB"
Line 35: | Line 35: | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
<br/><br/><br/><br/> | <br/><br/><br/><br/> | ||
− | |||
− | |||
− | |||
− | |||
<br/><br/> | <br/><br/> | ||
Line 62: | Line 58: | ||
=== Additional information=== | === Additional information=== | ||
− | |||
− | |||
− | |||
=The protein= | =The protein= | ||
Line 80: | Line 73: | ||
* '''Kinetic information:''' | * '''Kinetic information:''' | ||
− | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
− | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
Line 110: | Line 103: | ||
* '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=moeB_1496155_1497174_1 moeB] {{PubMed|22383849}} | * '''Expression browser:''' [http://genome.jouy.inra.fr/cgi-bin/seb/viewdetail.py?id=moeB_1496155_1497174_1 moeB] {{PubMed|22383849}} | ||
− | * '''Sigma factor:''' | + | * '''[[Sigma factor]]:''' |
* '''Regulation:''' | * '''Regulation:''' | ||
Line 137: | Line 130: | ||
=References= | =References= | ||
+ | == Reviews == | ||
+ | <pubmed> 23539623 </pubmed> | ||
+ | == Original publications == | ||
<pubmed> 15896804 22383849</pubmed> | <pubmed> 15896804 22383849</pubmed> | ||
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 12:26, 19 March 2014
- Description: molybdopterin biosynthesis protein
Gene name | moeB |
Synonyms | |
Essential | no |
Product | unknown |
Function | nitrate respiration |
Gene expression levels in SubtiExpress: moeB | |
MW, pI | 37 kDa, 6.089 |
Gene length, protein length | 1017 bp, 339 aa |
Immediate neighbours | mobA, moeA |
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
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU14270
Phenotypes of a mutant
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s): ThiF
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- UniProt: O31702
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- 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
Reviews
Ralf R Mendel
The molybdenum cofactor.
J Biol Chem: 2013, 288(19);13165-72
[PubMed:23539623]
[WorldCat.org]
[DOI]
(I p)
Original publications
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)
David M Duda, Helen Walden, John Sfondouris, Brenda A Schulman
Structural analysis of Escherichia coli ThiF.
J Mol Biol: 2005, 349(4);774-86
[PubMed:15896804]
[WorldCat.org]
[DOI]
(P p)