Difference between revisions of "GltA"
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# 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] | ||
− | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov | + | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=+12823818 PubMed] |
Revision as of 16:19, 5 January 2009
- Description: large subunit of glutamate synthase, small subunit is gltB, glutamate biosynthesis is induced by sugar and repressed by arginine
Gene name | gltA |
Synonyms | |
Essential | no |
Product | glutamate synthase (large subunit) |
Function | glutamate biosynthesis |
MW, pI | 168 kDa, 5.47 |
Gene length, protein length | 4560 bp, 1520 amino acids |
Immediate neighbours | gltC, gltB |
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: glutamate synthase family
- Paralogous protein(s): YerD
Extended information on the protein
- Kinetic information:
- Domains:
- Glutamine amidotransferase type-2 domain (22-415)
- Nucleotide binding domain (1060-1112)
- Modification:
- Cofactor(s): 3Fe-4S, FAD, FMN
- Effectors of protein activity:
- Interactions:
- Localization: membrane protein
Database entries
- Structure:
- Swiss prot entry: [3]
- KEGG entry: [4]
- E.C. number: [5]
Additional information
subject to Clp-dependent proteolysis upon glucose starvation
Expression and regulation
- Operon: gltAB
- Sigma factor: SigA
- Regulation: induced by sugar, repressed by arginine, ammonium required
- 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
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed