Difference between revisions of "GltB"
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=Biological materials = | =Biological materials = | ||
− | * '''Mutant:''' GP807 (del '' | + | * '''Mutant:''' |
+ | ** GP807 (del ''[[gltA]]-[[gltB]]''::''tet'') , available in [[Jörg Stülke]]'s lab | ||
+ | ** GP517 (ermC), available in [[Jörg Stülke]]'s lab | ||
* '''Expression vector:''' | * '''Expression vector:''' | ||
− | ** pGP1119 (in [[pGP380]], for SPINE, expression in ''B. subtilis''), available in [[Stülke]] lab | + | ** pGP1119 (in [[pGP380]], for SPINE, expression in ''B. subtilis''), available in [[Jörg Stülke]]'s lab |
* '''lacZ fusion:''' see ''[[gltA]]'' | * '''lacZ fusion:''' see ''[[gltA]]'' | ||
Line 139: | Line 141: | ||
* '''GFP fusion:''' | * '''GFP fusion:''' | ||
− | * '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab | + | * '''two-hybrid system:''' ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Jörg Stülke]]'s lab |
* '''Antibody:''' | * '''Antibody:''' |
Revision as of 08:13, 24 September 2014
- Description: small subunit of glutamate synthase
Gene name | gltB |
Synonyms | |
Essential | no |
Product | glutamate synthase (small subunit) |
Function | glutamate biosynthesis |
Gene expression levels in SubtiExpress: gltB | |
Interactions involving this protein in SubtInteract: GltB | |
Metabolic function and regulation of this protein in SubtiPathways: gltB | |
MW, pI | 54.6 kDa, 7.69 |
Gene length, protein length | 1479 bp, 493 amino acids |
Immediate neighbours | yogA, gltA |
Sequences | Protein DNA DNA_with_flanks |
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, glutamate metabolism
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
- BsubCyc: BSU18440
- 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
- BsubCyc: BSU18440
- UniProt: O34399
- KEGG entry: [3]
- E.C. number: 1.4.1.13
Additional information
Expression and regulation
- Regulation: see gltA
- Additional information:
- number of protein molecules per cell (minimal medium with glucose and ammonium): 1128 PubMed
Biological materials
- Mutant:
- GP807 (del gltA-gltB::tet) , available in Jörg Stülke's lab
- GP517 (ermC), available in Jörg Stülke's lab
- Expression vector:
- pGP1119 (in pGP380, for SPINE, expression in B. subtilis), available in Jörg Stülke's lab
- lacZ fusion: see gltA
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
- Antibody:
Labs working on this gene/protein
Linc Sonenshein, Tufts University, Boston, MA, USA Homepage
Jörg Stülke, University of Göttingen, Germany Homepage
Fabian Commichau University of Göttingen, Germany Homepage
Your additional remarks
References
Reviews
Katrin Gunka, Fabian M Commichau
Control of glutamate homeostasis in Bacillus subtilis: a complex interplay between ammonium assimilation, glutamate biosynthesis and degradation.
Mol Microbiol: 2012, 85(2);213-24
[PubMed:22625175]
[WorldCat.org]
[DOI]
(I p)
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