Difference between revisions of "GltA"
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU18450&redirect=T BSU18450] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/gltAB.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/gltAB.html] | ||
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=== Database entries === | === Database entries === | ||
+ | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU18450&redirect=T BSU18450] | ||
* '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=2VDC 2VDC] (the [[GltA]]-[[GltB]] complex of ''Azospirillum brasiliense'') {{PubMed|18199747}} | * '''Structure:''' [http://www.pdb.org/pdb/explore/explore.do?structureId=2VDC 2VDC] (the [[GltA]]-[[GltB]] complex of ''Azospirillum brasiliense'') {{PubMed|18199747}} |
Revision as of 13:52, 2 April 2014
- Description: large subunit of glutamate synthase
Gene name | gltA |
Synonyms | |
Essential | no |
Product | glutamate synthase (large subunit) |
Function | glutamate biosynthesis |
Gene expression levels in SubtiExpress: gltA | |
Interactions involving this protein in SubtInteract: GltA | |
Metabolic function and regulation of this protein in SubtiPathways: gltA | |
MW, pI | 168 kDa, 5.47 |
Gene length, protein length | 4560 bp, 1520 amino acids |
Immediate neighbours | gltB, gltC |
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, membrane proteins, phosphoproteins
This gene is a member of the following regulons
GltC regulon, FsrA regulon, TnrA regulon, Efp-dependent proteins
The gene
Basic information
- Locus tag: BSU18450
Phenotypes of a mutant
auxotrophic for glutamate
Database entries
- BsubCyc: BSU18450
- 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:
- phosphorylated on Arg-904 AND/OR Arg-914 PubMed
- Cofactor(s): 3Fe-4S, FAD, FMN
- Effectors of protein activity:
- Localization:
- membrane associated PubMed, cytoplasm
Database entries
- BsubCyc: BSU18450
- 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
- translation is likely to require Efp due to the presence of several consecutive proline residues 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
- translation is likely to require Efp due to the presence of several consecutive proline residues 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
Fabian Commichau University of Göttingen, Germany Homepage
Your additional remarks
References
Reviews
Original publications