gltA

gltA
168

large subunit of glutamate synthase, controls GudB activity

Locus
BSU_18450
Molecular weight
168.61 kDa
Isoelectric point
5.47
Protein length
Gene length
Function
glutamate biosynthesis and control of glutamate degradation
Product
glutamate synthase (large subunit)
Essential
no
E.C.
1.4.1.13
Synonyms
gltA

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, can be bypassed by inactivation of citG and ansR (as a result of ansA-ansB derepression)PubMed
The protein
Catalyzed reaction/ biological activity
2 L-glutamate + NADP+ --> 2-oxoglutarate + H+ + L-glutamine + NADPH (according to UniProt)
binding to GudB to inhibit glutamate degradation in the absence of glutamate PubMed
Protein family
glutamate synthase family (with YerD and GltB, according to UniProt)
Glutamine amidotransferase type-2 domain (aa 22-415) (according to UniProt)
Nucleotide binding domain (1060-1112)
one 3Fe-4S cluster PubMed
Structure
7MFT (PDB) (the GudB6-(GltA-GltB)6 complex) PubMed
2VDC (PDB) (the GltA-GltB complex of Azospirillum brasiliense) PubMed, note that the B. subtilis protein is unable to form dimers, thus GltA-GltB exists as a heterodimer PubMed
Modification
phosphorylated on Arg-904 AND/OR Arg-914 PubMed
Paralogous protein(s)
membrane associated PubMed, cytoplasm (according to UniProt)
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
Operons
Genes
Description
Regulation
expressed in the presence of ammonium PubMed
Regulatory mechanism
TnrA: repression, PubMed, in tnrA regulon
GltC: activation, PubMed, in gltC regulon
Fur: indirect effect, in fur regulon
Sigma factors
SigA: sigma factor, PubMed, in sigA regulon
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gltAgltB

2025-03-17 17:35:45

Bzhu

136

90b560615ccdd0da363a7f12dfb0b2af980e6000

F7C02591D79E87C32CC816954DB16451EB2276C9

Other regulations
FsrA: translation inhibition, PubMed
Biological materials
Mutant
GP3906 (ΔgltA::aphA3), available in Jörg Stülke's lab
BP123 (ΔgltA-gltB::ermC) , available in Fabian Commichau's lab
GP807 (ΔgltA-gltB::tet) , available in Jörg Stülke's lab
GP222 (gltA under the control of p-xyl), available in Jörg Stülke's lab
1A808 ( gltA::cat), PubMed, available at BGSC
1A809 ( gltA::kan), PubMed, available at BGSC
BKE18450 (gltA::erm  trpC2) available at BGSCPubMed, upstream reverse: _UP1_CATAATTCCTCTCCCCCGAT,  downstream forward: _UP4_GTACAGTAAGGAAGGGGAGA
BKK18450 (gltA::kan  trpC2) available at BGSCPubMed, upstream reverse: _UP1_CATAATTCCTCTCCCCCGAT,  downstream forward: _UP4_GTACAGTAAGGAAGGGGAGA
Two-hybrid system
B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
LacZ fusion
pGP526 (in pAC7), available in Jörg Stülke's lab PubMed
pGP919 (in pAC5), available in Jörg Stülke's lab PubMed
Labs working on this gene/protein
Linc Sonenshein, Tufts University, Boston, MA, USA Homepage
Jörg Stülke, University of Göttingen, Germany Homepage
Fabian Commichau Brandenburg Technical University Cottbus-Senftenberg, Germany Homepage
References
Reviews
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Original Publications
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Page visits: 10850

Time of last update: 2025-04-04 07:11:19

Author of last update: Jstuelk