Difference between revisions of "MoaD"
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU14310&redirect=T BSU14310] | ||
* '''DBTBS entry:''' no entry | * '''DBTBS entry:''' no entry | ||
| Line 88: | Line 89: | ||
=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU14310&redirect=T BSU14310] | ||
* '''Structure:''' | * '''Structure:''' | ||
Revision as of 13:35, 2 April 2014
- Description: molybdopterin synthase (small subunit)
| Gene name | moaD |
| Synonyms | |
| Essential | no |
| Product | molybdopterin synthase (small subunit) |
| Function | nitrate respiration |
| Gene expression levels in SubtiExpress: moaD | |
| Interactions involving this protein in SubtInteract: MoaD | |
| MW, pI | 7 kDa, 3.829 |
| Gene length, protein length | 231 bp, 77 aa |
| Immediate neighbours | moaE, yknU |
| 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: BSU14310
Phenotypes of a mutant
Database entries
- BsubCyc: BSU14310
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- BsubCyc: BSU14310
- UniProt: O31706
- 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)
Tadhg P Begley, Steven E Ealick, Fred W McLafferty
Thiamin biosynthesis: still yielding fascinating biological chemistry.
Biochem Soc Trans: 2012, 40(3);555-60
[PubMed:22616866]
[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)
Michael J Rudolph, Margot M Wuebbens, Oliver Turque, K V Rajagopalan, Hermann Schindelin
Structural studies of molybdopterin synthase provide insights into its catalytic mechanism.
J Biol Chem: 2003, 278(16);14514-22
[PubMed:12571227]
[WorldCat.org]
[DOI]
(P p)
