Difference between revisions of "GltB"
(→Database entries) |
(→Database entries) |
||
| Line 81: | Line 81: | ||
* '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34399] | * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34399] | ||
| − | * '''KEGG entry:''' | + | * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu:BSU18440] |
* '''E.C. number:''' [http://www.expasy.ch/cgi-bin/get-enzyme-entry?1.4.1.13] | * '''E.C. number:''' [http://www.expasy.ch/cgi-bin/get-enzyme-entry?1.4.1.13] | ||
Revision as of 11:54, 8 January 2009
- Description: small subunit of glutamate synthase, large subunit is gltA, glutamate biosynthesis is induced by sugar and repressed by arginine
| Gene name | gltB |
| Synonyms | |
| Essential | no |
| Product | glutamate synthase (small subunit) |
| Function | glutamate biosynthesis |
| MW, pI | 54.6 kDa, 7.69 |
| Gene length, protein length | 1479 bp, 493 amino acids |
| Immediate neighbours | gltA, yogA |
| Gene sequence (+200bp) | Protein sequence |
| Genetic context File:GenE context.gif | |
Contents
The gene
Basic information
- Coordinates:
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry:[2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: 2 L-glutamate + NADP(+) <=> L-glutamine + 2-oxoglutarate + NADPH
- Protein family:
- Paralogous protein(s): none
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- Swiss prot entry: [3]
- KEGG entry: [4]
- E.C. number: [5]
Additional information
Expression and regulation
- Operon: gltA gltB
- Sigma factor:
- Regulation: induced by sugar, repressed by arginine (both mediated by GltC), repressed in the absence of ammonium (mediated by TnrA)
- Additional information:
Biological materials
Labs working on this gene/protein
Linc Sonenshein, Tufts University, Boston, MA, USA Homepage
Jörg Stülke, University of Göttingen, Germany Homepage
Your additional remarks
References
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed
