Difference between revisions of "GltA"
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= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
{{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}}, | {{SubtiWiki category|[[biosynthesis/ acquisition of amino acids]]}}, | ||
| − | {{SubtiWiki category|[[membrane proteins]]}} | + | {{SubtiWiki category|[[membrane proteins]]}}, |
| + | {{SubtiWiki category|[[phosphoproteins]]}} | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = | ||
Revision as of 15:19, 20 April 2012
- Description: large subunit of glutamate synthase
| Gene name | gltA |
| Synonyms | |
| Essential | no |
| Product | glutamate synthase (large subunit) |
| Function | glutamate biosynthesis |
| Interactions involving this protein in SubtInteract: GltA | |
| Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate | |
| MW, pI | 168 kDa, 5.47 |
| Gene length, protein length | 4560 bp, 1520 amino acids |
| Immediate neighbours | gltB, gltC |
| Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context 
This image was kindly provided by SubtiList
| |
Expression at a glance PubMed
| |
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids, membrane proteins, phosphoproteins
This gene is a member of the following regulons
GltC regulon, FsrA regulon, TnrA regulon
The gene
Basic information
- Locus tag: BSU18450
Phenotypes of a mutant
auxotrophic for glutamate
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 (according to Swiss-Prot) 2 L-glutamate + NADP(+) <=> L-glutamine + 2-oxoglutarate + NADPH
- Protein family: glutamate synthase family (according to Swiss-Prot) 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:
- Localization: membrane associated PubMed, cytoplasm
Database entries
- UniProt: P39812
- KEGG entry: [3]
- E.C. number: 1.4.1.13 3 1.4.1.13]
Additional information
subject to Clp-dependent proteolysis upon glucose starvation PubMed
Expression and regulation
- Regulation:
- expression activated by glucose (11 fold) (CcpA, GltC) PubMed
- repressed by arginine (GltC, RocG) PubMed
- expressed in the presence of ammonium PubMed
- repressed in the absence of good nitrogen sources (glutamine or ammonium) (TnrA) PubMed
- part of the iron sparing response, strong down-regulation in a fur mutant (Fur, FsrA) PubMed
- Regulatory mechanism:
- Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed
Biological materials
- Mutant: GP807 (del gltAB::tet), GP222 (gltA under the control of p-xyl), available in Stülke lab
- Expression vector:
- 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, Tufts University, Boston, MA, USA Homepage
Jörg Stülke, University of Göttingen, Germany Homepage
Your additional remarks
References
Reviews
Akira Suzuki, David B Knaff
Glutamate synthase: structural, mechanistic and regulatory properties, and role in the amino acid metabolism.
Photosynth Res: 2005, 83(2);191-217
[PubMed:16143852]
[WorldCat.org]
[DOI]
(P p)
Frank M Raushel, James B Thoden, Hazel M Holden
Enzymes with molecular tunnels.
Acc Chem Res: 2003, 36(7);539-48
[PubMed:12859215]
[WorldCat.org]
[DOI]
(P p)
Original publications
