gltA [2017-02-27 15:02:04]

large subunit of glutamate synthase

locus: BSU18450

pI: 5.00

mw: 168.00 kDa

protein length: 1520 aa

gene length: 4560 bp

function: glutamate biosynthesis

product: glutamate synthase (large subunit)

essential: no

ec: 1.4.1.13

synonyms

Genomic Context

categories

• [category|SW 2|Metabolism] → [category|SW 2.3|Amino acid/ nitrogen metabolism] → [category|SW 2.3.1|Biosynthesis/ acquisition of amino acids] → [category|SW 2.3.1.1|Biosynthesis/ acquisition of glutamate/ glutamine/ ammonium assimilation]
• [category|SW 6|Groups of genes] → [category|SW 6.11|Efp-dependent proteins]
• [category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.1|Phosphorylation on an Arg residue]

This gene is a member of the following [SW|regulons]

• [SW|GltC regulon], [SW|FsrA regulon], [SW|TnrA regulon], [SW|Efp-dependent proteins]

Gene

Coordinates on the chromosome (coding sequence): 2,010,070 -> 2,014,632

Phenotypes of a mutant

• auxotrophic for glutamate

The protein

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)

• [protein|D1AF9DA2594D2E2A94DC207A870C8495954A7A17|YerD]

[SW|Domains]

• Glutamine amidotransferase type-2 domain (22-415)
• Nucleotide binding domain (1060-1112)

Modification

• phosphorylated on Arg-904 AND/OR Arg-914 [Pubmed|22517742]

[SW|Cofactors]

• [3 Fe- 4 S] cluster, FAD, FMN

Structure

• [PDB|2VDC] (the [protein|44DF1B7E476AD58B3CCC39300FFE0132D0D32AD0|GltA]-[protein|AA07CC52B2DD48ACC9D3375E9D531CB1ACBE485A|GltB] complex of ''Azospirillum brasiliense'') [Pubmed|18199747]

[SW|Localization]

• membrane associated [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids= 18763711 PubMed], cytoplasm

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation [PubMed|17981983]
• [SW|translation] is likely to require [protein|3054CD45713BBD69C2A528DE24AF6AF37175FD9D|Efp] due to the presence of several consecutive proline residues [Pubmed|23239624,23239623]

Expression and Regulation: [[this]]

Biological materials

Mutant

• GP807 (del ''[gene|44DF1B7E476AD58B3CCC39300FFE0132D0D32AD0|gltA]-[gene|AA07CC52B2DD48ACC9D3375E9D531CB1ACBE485A|gltB]''::''tet'') , available in [SW|Jörg Stülke]'s lab
• GP222 (''gltA'' under the control of p-xyl), available in [SW|Jörg Stülke]'s lab
• 1A808 ( ''gltA''::''cat''), [Pubmed|15109830], available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A808&Search=1A808 BGSC]
• 1A809 ( ''gltA''::''kan''), [Pubmed|15109830], available at [http://pasture.asc.ohio-state.edu/BGSC/getdetail.cfm?bgscid=1A809&Search=1A809 BGSC]

lacZ fusion

• pGP526 (in [protein|search|pAC7]), pGP919 (in [protein|search|pAC5]), available in [SW|Jörg Stülke]'s lab

two-hybrid system

• ''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW|Jörg Stülke]'s lab

Labs working on this gene/protein

• [SW|Linc Sonenshein], Tufts University, Boston, MA, USA [http://www.tufts.edu/sackler/microbiology/faculty/sonenshein/index.html Homepage]
• [SW|Jörg Stülke], University of Göttingen, Germany
• [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
• [SW|Fabian Commichau] University of Göttingen, Germany
• [http://genmibio.uni-goettingen.de/index.php?id=130 Homepage]

References

Reviews

• 16143852,12859215,22625175,12859215

Original publications

• 12823818,18199747,11029411,12850135,7559360,15150225,2548995,17183217,17608797,17134717,14523131,12823818,18326565,17981983,18763711,20933603,17012385,22389480,22517742,25755103