Difference between revisions of "GlmS"
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− | <pubmed> 17981983 , 18079181 , 16784238 , 17114942 ,16484375 ,15029187 ,11160890,17283212 ,16298301,19228039 </pubmed> | + | <pubmed> 17981983 ,18079181 ,16784238 ,16990543 ,17114942 ,16484375 , 15029187 , 11160890, 17283212 , 16298301, 19228039 </pubmed> |
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] |
Revision as of 19:10, 5 June 2009
- Description: glutamine-fructose-6-phosphate transaminase
Gene name | glmS |
Synonyms | gcaA, ybxD |
Essential | yes PubMed |
Product | glutamine-fructose-6-phosphate transaminase |
Function | cell wall synthesis |
MW, pI | 65 kDa, 4.796 |
Gene length, protein length | 1800 bp, 600 aa |
Immediate neighbours | glmM, ybbU |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU01780
Phenotypes of a mutant
essential PubMed
Database entries
- DBTBS entry: no entry
- SubtiList entry: [1]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate (according to Swiss-Prot)
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- Swiss prot entry: P39754
- KEGG entry: [2]
- E.C. number: 2.6.1.16
Additional information
- subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Regulatory mechanism: glmS ribozyme: glucosamine 6-phosphate binds the leader mRNA, and a riboswitch with ribozyme activity cleaves off the glmS section from the mRNA, resulting in stopp of transcript elongation
- Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Wade Winkler, University of Texas, USA, Homepage
Your additional remarks
References
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed