Difference between revisions of "GltB"
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|style="background:#ABCDEF;" align="center"|'''Function''' || glutamate biosynthesis | |style="background:#ABCDEF;" align="center"|'''Function''' || glutamate biosynthesis | ||
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| − | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU18440 gltB] |
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/GltB GltB] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/GltB GltB] | ||
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|style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yogA]]'', ''[[gltA]]'' | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[yogA]]'', ''[[gltA]]'' | ||
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| − | | | + | |style="background:#FAF8CC;" align="center"|'''Sequences'''||[http://bsubcyc.org/BSUB/sequence-aa?type=GENE&object=BSU18440 Protein] [http://bsubcyc.org/BSUB/sequence?type=GENE&object=BSU18440 DNA] [http://bsubcyc.org/BSUB/seq-selector?chromosome=CHROM-1&object=BSU18440 Advanced_DNA] |
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Revision as of 12:58, 13 May 2013
- 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: Ammonium/ glutamate | |
| MW, pI | 54.6 kDa, 7.69 |
| Gene length, protein length | 1479 bp, 493 amino acids |
| Immediate neighbours | yogA, gltA |
| Sequences | Protein DNA Advanced_DNA |
Genetic context 
This image was kindly provided by SubtiList
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Expression at a glance PubMed
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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
- 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
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
