gltA
168
large subunit of glutamate synthase, controls [protein|C36C8C9EEDCAD392D9BEC9728A1E0CBFF2F4E790|gudB] activity
locus
BSU_18450
Molecular weight
168.61 kDa
pI
5.47
function
glutamate biosynthesis and control of glutamate degradation
product
glutamate synthase (large subunit)
essential
no
ec
1.4.1.13
synonyms
gltA
Outlinks
Genomic Context
Categories containing this gene/protein
List of homologs in different organisms, belongs to COG0070 (Galperin et al., 2021)
This gene is a member of the following regulons
Gene
Coordinates
2,010,070 2,014,632
Phenotypes of a mutant
auxotrophic for glutamate [pubmed|38483038], can be bypassed by inactivation of [gene|A3A2EF3C95B833A11843553107D781EDEFF0BC41|citG] and [gene|146947C974D62BCB282BA3F5B924B35695D75886|ansR] (as a result of [gene|FED8E46AA1C4EFD27796D5DFBBB1663EBF336BFD|ansA]-[gene|5FAE80F22AEBAE63FC3C872EC651166A65C34DC2|ansB] derepression)[pubmed|38483038]
The protein
Catalyzed reaction/ biological activity
2 L-glutamate + NADP+ --> 2-oxoglutarate + H+ + L-glutamine + NADPH (according to UniProt)
binding to [protein|C36C8C9EEDCAD392D9BEC9728A1E0CBFF2F4E790|gudB] to inhibit glutamate degradation in the absence of glutamate [pubmed|34931064]
Protein family
glutamate synthase family (with [protein|D1AF9DA2594D2E2A94DC207A870C8495954A7A17|yerD] and [protein|AA07CC52B2DD48ACC9D3375E9D531CB1ACBE485A|gltB], according to UniProt)
[wiki|Domains]
[wiki|Glutamine amidotransferase type-2 domain] (aa 22-415) (according to UniProt)
Nucleotide binding domain (1060-1112)
[wiki|Cofactors]
one 3Fe-4S cluster [pubmed|29292548]
FMN [pubmed|34931064]
Structure
[PDB|7MFT] (the [protein|C36C8C9EEDCAD392D9BEC9728A1E0CBFF2F4E790|gudB]6-([protein|44DF1B7E476AD58B3CCC39300FFE0132D0D32AD0|gltA]-[protein|AA07CC52B2DD48ACC9D3375E9D531CB1ACBE485A|gltB])6 complex) [pubmed|34931064]
[PDB|2VDC] (the [protein|44DF1B7E476AD58B3CCC39300FFE0132D0D32AD0|gltA]-[protein|AA07CC52B2DD48ACC9D3375E9D531CB1ACBE485A|gltB] complex of ''Azospirillum brasiliense'') [Pubmed|18199747], note that the B. subtilis protein is unable to form dimers, thus [protein|44DF1B7E476AD58B3CCC39300FFE0132D0D32AD0|gltA]-[protein|AA07CC52B2DD48ACC9D3375E9D531CB1ACBE485A|gltB] exists as a heterodimer [pubmed|34931064]
[AF|P39812]
Modification
phosphorylated on Arg-904 AND/OR Arg-914 [Pubmed|22517742]
Paralogous protein(s)
[protein|D1AF9DA2594D2E2A94DC207A870C8495954A7A17|yerD]
[wiki|Localization]
membrane associated [pubmed|18763711], cytoplasm (according to UniProt)
Additional information
subject to Clp-dependent proteolysis upon glucose starvation [PubMed|17981983]
[wiki|translation] is likely to require [protein|3054CD45713BBD69C2A528DE24AF6AF37175FD9D|efp] due to the presence of several consecutive proline residues [Pubmed|23239624,23239623]
Expression and Regulation
Operons
genes
[gene|44DF1B7E476AD58B3CCC39300FFE0132D0D32AD0|gltA]-[gene|AA07CC52B2DD48ACC9D3375E9D531CB1ACBE485A|gltB]
description
[Pubmed|12823818]
regulation
expressed in the presence of ammonium [Pubmed|11029411]
regulatory mechanism
[protein|857EF1AC54DEA0690C01B7F8CEFFD16312C58F20|tnrA]: repression, [Pubmed|11029411], in [regulon|protein:857EF1AC54DEA0690C01B7F8CEFFD16312C58F20|tnrA regulon]
[protein|87BCAE725B02860156D50E1783F6DB68510C811E|gltC]: activation, [Pubmed|2548995], in [regulon|protein:87BCAE725B02860156D50E1783F6DB68510C811E|gltC regulon]
[protein|F899F1EE27E6D503BCC06BC52E3C7FD80B8EF725|fur]: indirect effect, in [regulon|protein:F899F1EE27E6D503BCC06BC52E3C7FD80B8EF725|fur regulon]
sigma factors
[protein|360F48D576DE950DF79C1A2677B7A35A8D8CC30C|sigA]: sigma factor, [Pubmed|2548995], in [regulon|protein:360F48D576DE950DF79C1A2677B7A35A8D8CC30C|sigA regulon]
Other regulations
[protein|CE542AE1A32CCD1ABB259E6159F7A37A8078E189|fsrA]: translation inhibition, [Pubmed|22389480]
Biological materials
Mutant
GP3906 (Δ[gene|44DF1B7E476AD58B3CCC39300FFE0132D0D32AD0|gltA]::aphA3), available in [wiki|Jörg Stülke]'s lab
BP123 (Δ[gene|44DF1B7E476AD58B3CCC39300FFE0132D0D32AD0|gltA]-[gene|AA07CC52B2DD48ACC9D3375E9D531CB1ACBE485A|gltB]::''ermC'') , available in [wiki|Fabian Commichau]'s lab
GP807 (Δ[gene|44DF1B7E476AD58B3CCC39300FFE0132D0D32AD0|gltA]-[gene|AA07CC52B2DD48ACC9D3375E9D531CB1ACBE485A|gltB]::''tet'') , available in [wiki|Jörg Stülke]'s lab
GP222 (''gltA'' under the control of p-xyl), available in [wiki|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]
BKE18450 ([gene|44DF1B7E476AD58B3CCC39300FFE0132D0D32AD0|gltA]::erm trpC2) available at [http://bgsc.org/getdetail.php?bgscid=BKE18450 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATAATTCCTCTCCCCCGAT, downstream forward: _UP4_GTACAGTAAGGAAGGGGAGA
BKK18450 ([gene|44DF1B7E476AD58B3CCC39300FFE0132D0D32AD0|gltA]::kan trpC2) available at [http://bgsc.org/getdetail.php?bgscid=BKK18450 BGSC], [Pubmed|28189581], upstream reverse: _UP1_CATAATTCCTCTCCCCCGAT, downstream forward: _UP4_GTACAGTAAGGAAGGGGAGA
two-hybrid system
''B. pertussis'' adenylate cyclase-based bacterial two hybrid system ([wiki|BACTH]), available in [wiki|Jörg Stülke]'s lab
lacZ fusion
pGP526 (in [wiki|pAC7]), available in [wiki|Jörg Stülke]'s lab [pubmed|14523131]
pGP919 (in [wiki|pAC5]), available in [wiki|Jörg Stülke]'s lab [pubmed|17183217]
labs
[wiki|Linc Sonenshein], Tufts University, Boston, MA, USA [http://www.tufts.edu/sackler/microbiology/faculty/sonenshein/index.html Homepage]
[wiki|Jörg Stülke], University of Göttingen, Germany [http://wwwuser.gwdg.de/~genmibio/stuelke.html Homepage]
[wiki|Fabian Commichau] Brandenburg Technical University Cottbus-Senftenberg, Germany [http://genmibio.uni-goettingen.de/index.php?id=130 Homepage]
References
Reviews
Original Publications
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Time of last update: 2024-04-26 23:57:48
Author of last update: Jstuelk