GltB
Revision as of 10:04, 13 April 2012 by 134.76.70.252 (talk)
- Description: small subunit of glutamate synthase
Gene name | gltB |
Synonyms | |
Essential | no |
Product | glutamate synthase (small subunit) |
Function | glutamate biosynthesis |
Interactions involving this protein in SubtInteract: GltB | |
Metabolic function and regulation of this protein in SubtiPathways: Ammonium/ glutamate | |
MW, pI | 54.6 kDa, 7.69 |
Gene length, protein length | 1479 bp, 493 amino acids |
Immediate neighbours | yogA, gltA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids
This gene is a member of the following regulons
GltC regulon, FsrA regulon, TnrA regulon
The gene
Basic information
- Locus tag: BSU18440
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.
- 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:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- UniProt: O34399
- KEGG entry: [3]
- E.C. number: 1.4.1.13
Additional information
Expression and regulation
- Regulation: see gltA
- Additional information:
Biological materials
- Mutant: GP807 (del gltAB::tet), GP517 (ermC), both available in Stülke lab
- Expression vector:
- 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, 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