|
|
| (39 intermediate revisions by 9 users not shown) |
| Line 1: |
Line 1: |
| * '''Description:''' small subunit of glutamate synthase<br/><br/>
| | {{#bank: GltB}} |
|
| |
|
| {| align="right" border="1" cellpadding="2"
| |
| |-
| |
| |style="background:#ABCDEF;" align="center"|'''Gene name'''
| |
| |''gltB''
| |
| |-
| |
| |style="background:#ABCDEF;" align="center"| '''Synonyms''' || '' ''
| |
| |-
| |
| |style="background:#ABCDEF;" align="center"| '''Essential''' || no
| |
| |-
| |
| |style="background:#ABCDEF;" align="center"| '''Product''' || glutamate synthase (small subunit)
| |
| |-
| |
| |style="background:#ABCDEF;" align="center"|'''Function''' || glutamate biosynthesis
| |
| |-
| |
| |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 54.6 kDa, 7.69
| |
| |-
| |
| |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 1479 bp, 493 amino acids
| |
| |-
| |
| |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[gltA]]'', ''[[yogA]]''
| |
| |-
| |
| |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB13727]+-newId sequences] <br/> (Barbe ''et al.'', 2009)'''
| |
| |-
| |
| |-
| |
| |-
| |
| |colspan="2" | '''Genetic context''' <br/> [[Image:gltB_context.gif]]
| |
| <div align="right"> <small>This image was kindly provided by [http://genolist.pasteur.fr/SubtiList/ SubtiList]</small></div>
| |
| |-
| |
| |}
| |
|
| |
| __TOC__
| |
|
| |
| <br/><br/>
| |
|
| |
|
| |
| =The gene=
| |
|
| |
| === Basic information ===
| |
|
| |
| * '''Locus tag:''' BSU18440
| |
|
| |
| ===Phenotypes of a mutant ===
| |
|
| |
| auxotrophic for glutamate
| |
|
| |
| === Database entries ===
| |
|
| |
| * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/gltAB.html]
| |
|
| |
| * '''SubtiList entry:'''[http://genolist.pasteur.fr/SubtiList/genome.cgi?gene_detail+BG12594]
| |
|
| |
| === Additional information===
| |
|
| |
| =The protein=
| |
|
| |
| === Basic information/ Evolution ===
| |
|
| |
| * '''Catalyzed reaction/ biological activity:''' 2 L-glutamate + NADP<sup>+</sup> = L-glutamine + 2-oxoglutarate + NADPH (according to Swiss-Prot) 2 L-glutamate + NADP(+) <=> L-glutamine + 2-oxoglutarate + NADPH
| |
|
| |
| * '''Protein family:''' glutamate synthase family.
| |
|
| |
| * '''Paralogous protein(s):''' none
| |
|
| |
| === Extended information on the protein ===
| |
|
| |
| * '''Kinetic information:'''
| |
|
| |
| * '''Domains:'''
| |
| ** nucleotide binding domain (NADP) (299–313)
| |
|
| |
| * '''Modification:'''
| |
|
| |
| * '''Cofactor(s):'''
| |
|
| |
| * '''Effectors of protein activity:'''
| |
|
| |
| * '''Interactions:'''
| |
|
| |
| * '''Localization:''' cytoplasm (according to Swiss-Prot)
| |
|
| |
| === Database entries ===
| |
|
| |
| * '''Structure:'''
| |
|
| |
| * '''Swiss prot entry:''' [http://www.uniprot.org/uniprot/O34399 O34399]
| |
|
| |
| * '''KEGG entry:''' [http://www.genome.jp/dbget-bin/www_bget?bsu+BSU18440]
| |
|
| |
| * '''E.C. number:''' [http://www.expasy.org/enzyme/1.4.1.13 1.4.1.13] 3 1.4.1.13]
| |
|
| |
| === Additional information===
| |
|
| |
|
| |
| =Expression and regulation=
| |
|
| |
| * '''Operon:''' ''[[gltA]]-[[gltB]]''
| |
|
| |
| * '''[[Sigma factor]]:''' [[SigA]]
| |
|
| |
| * '''Regulation:''' see ''[[gltA]]''
| |
|
| |
| * '''Additional information:'''
| |
|
| |
| =Biological materials =
| |
|
| |
| * '''Mutant:''' GP807 (del ''gltAB''::''tet''), GP736 (spc), available in [[Stülke]] lab
| |
|
| |
| * '''Expression vector:''' pGP1119 (in [[pGP380]], for SPINE, expression in ''B. subtilis''), available in [[Stülke]] lab
| |
|
| |
| * '''lacZ fusion:''' see ''[[gltA]]''
| |
|
| |
| * '''GFP fusion:'''
| |
|
| |
| * '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab
| |
|
| |
| * '''Antibody:'''
| |
|
| |
| =Labs working on this gene/protein=
| |
|
| |
| [[Linc Sonenshein|Linc Sonenshein]], Tufts University, Boston, MA, USA [http://www.tufts.edu/sackler/microbiology/faculty/sonenshein/index.html Homepage]
| |
|
| |
| [[Stülke|Jörg Stülke]], University of Göttingen, Germany
| |
| [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
| |
|
| |
| =Your additional remarks=
| |
|
| |
| =References=
| |
|
| |
| <pubmed>11029411,7559360 15150225 2548995 17183217 17608797 17134717 14523131, 12823818 ,</pubmed>
| |
| # Yoshida K, et al. (2003) Identification of additional TnrA-regulated genes of Bacillus subtilis associated with a TnrA box. ''Mol Microbiol'' '''49(1):''' 157-65. [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+12823818 PubMed]
| |
| # Belitsky, B. R., and Sonenshein, A. L. (1995) Mutations in GltC that increase ''Bacillus subtilis gltA'' expression. J Bacteriol 177: 5696-5700.[http://www.ncbi.nlm.nih.gov/sites/entrez/7559360 PubMed]
| |
| # Belitsky, B. R., and Sonenshein, A. L. (2004) Modulation of activity of ''Bacillus subtilis'' regulatory proteins GltC and TnrA by glutamate dehydrogenase. J Bacteriol 186: 3399-3407.[http://www.ncbi.nlm.nih.gov/sites/entrez/15150225 PubMed]
| |
| # Bohannon, D. E., and Sonenshein, A. L. (1989) Positive regulation of glutamate biosynthesis in ''Bacillus subtilis''. J Bacteriol 171: 4718-4727.[http://www.ncbi.nlm.nih.gov/sites/entrez/2548995 PubMed]
| |
| # Commichau, F. M., Wacker, I., Schleider, J., Blencke, H.-M., Reif, I., Tripal, P., and Stülke, J. (2007) Characterization of ''Bacillus subtilis'' mutants with carbon source-independent glutamate biosynthesis. J Mol Microbiol Biotechnol 12: 106-113. [http://www.ncbi.nlm.nih.gov/sites/entrez/17183217 PubMed]
| |
| # Commichau, F. M., Herzberg, C., Tripal, P., Valerius, O., and Stülke, J. (2007) A regulatory protein-protein interaction governs glutamate biosynthesis in ''Bacillus subtilis'': The glutamate dehydrogenase RocG moonlights in controlling the transcription factor GltC. Mol Microbiol 65: 642-654. [http://www.ncbi.nlm.nih.gov/sites/entrez/17608797 PubMed]
| |
| # Picossi, S., Belitsky, B. R., and Sonenshein, A. L. (2007) Molecular mechanism of the regulation of ''Bacillus subtilis gltAB'' expression by GltC. J Mol Biol 365: 1298-1313. [http://www.ncbi.nlm.nih.gov/sites/entrez/17134717 PubMed]
| |
| # Wacker, I., Ludwig, H., Reif, I., Blencke, H. M., Detsch, C., and Stülke, J. (2003) The regulatory link between carbon and nitrogen metabolism in ''Bacillus subtilis'': regulation of the ''gltAB'' operon by the catabolite control protein CcpA. Microbiology 149: 3001-3009.[http://www.ncbi.nlm.nih.gov/sites/entrez/14523131 PubMed]
| |
| # Belitsky, B. R., Wray, L. V., Jr., Fisher, S. H., Bohannon, D. E. & Sonenshein, A. L. (2000). Role of TnrA in nitrogen source-dependent repression of ''Bacillus subtilis'' glutamate synthase gene expression. J Bacteriol 182, 5939-5947. [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+11029411 PubMed]
| |
| # Commichau, F. M., Gunka, K., Landmann, J. J. & Stülke, J. (2008) Glutamate metabolism in ''Bacillus subtilis'': Gene expression and enzyme activities evolved to avoid futile cycles and to allow rapid responses to perturbations in the system. J. Bacteriol. 190: 3557-3564. [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+18326565 PubMed]
| |
