gudB

gudB
168

glutamate dehydrogenase, trigger enzyme, the gene is cryptic in B. subtilis 168 due to a duplication of 9 bp

Locus
BSU_22960
Molecular weight
47.05 kDa
Isoelectric point
5.58
Protein length
427 aaSequenceBlast
Gene length
1284 bpSequenceBlast
Function
glutamate utilization, control of GltC activity
Product
glutamate dehydrogenase, trigger enzyme
Essential
no
E.C.
1.4.1.2
Synonyms
gudB, ypcA
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG0334 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
2,402,067 → 2,403,350
Phenotypes of a mutant
the gene is cryptic in B. subtilis 168. If gudB is activated (gudB1 mutation), the bacteria are able to utilize glutamate as the only carbon source PubMed
a rocG gudB mutant is sensitive to ß-lactam antibiotics such as cefuroxime and to fosfomycin due to the downregulation of the SigW regulon PubMed
transcription profile of a rocG gudB mutant strain: GEO PubMed
decryptification of gudB facilitates the adaptation a strain lacking c-di-AMP to growth on medium containing glutamate PubMed
The protein
Catalyzed reaction/ biological activity
H2O + L-glutamate + NAD+ --> 2-oxoglutarate + H+ + NADH + NH4+ (according to UniProt)
Protein family
Glu/Leu/Phe/Val dehydrogenases family (with Bcd and RocG, according to UniProt)
Cofactors
NAD+/NADH + H+
Structure
3K8Z (PDB) (enzymatically active GudB1) PubMed
7MFT (PDB) (the GudB6-(GltA-GltB)6 complex) PubMed
P50735 (AlphaFold)
Modification
phosphorylated on Arg-56, Arg-83, and Arg-421 and/or Arg-423 PubMed
Effectors of protein activity
GudB activity is inhibited by binding of GltA-GltB at low glutamate concentrations to prevent a futile cycle of glutamate synthesis and degradation PubMed
Paralogous protein(s)
RocG
Expression and Regulation
Operons
Genes
gudB
Description
PubMed
Regulation
constitutively expressed PubMed
expression is reduced in motile cells as compared to non-motile cells PubMed
Sigma factors
SigA: sigma factor, PubMed, in sigA regulon
Open in new tab

gudB

2025-02-28 12:36:11

Jstuelk

112

5EEC94A9C51B3592FE21BEA463CEB41CA19692D1

7F4947850BF574FD99A2544E8D38ADE261B2EAEB

Biological materials
Mutant with active GudB
GP2834 (gudB+), available in Jörg Stülke's lab
Mutant
GP691 (ΔgudB::cat), available in Jörg Stülke's lab
GP1160 (ΔgudB::aphA3), available in Jörg Stülke's lab PubMed
GP1161 (ΔgudB::aphA3 ΔrocG::Tn10 spc), available in Jörg Stülke's lab PubMed
MGNA-A397 (ypcA::erm), available at the NBRP B. subtilis, Japan
BKE22960 (ΔgudB::erm  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CATTTGAGTTAACCTCCTAG,  downstream forward: _UP4_TAAGTTGATGATTTGCATAA
BKK22960 (ΔgudB::kan  trpC2) available at BGSC,  PubMed, upstream reverse: _UP1_CATTTGAGTTAACCTCCTAG,  downstream forward: _UP4_TAAGTTGATGATTTGCATAA
Expression vectors
for purification of GudB from E. coli carrying an N-terminal Strep-tag: pGP863 (in pGP172) available in Jörg Stülke's lab
for purification of GudB1 from E. coli carrying an N-terminal Strep-tag: pGP864 (in pGP172) available in Jörg Stülke's lab
for ectopic expression of gudB with its native promoter: pGP900 (in pAC5), available in Jörg Stülke's lab
wild type gudB, expression in B. subtilis, in pBQ200: pGP1712, available in Jörg Stülke's lab
pBP179 (N-terminal Strep-tag gudB+, purification from B. subtilis, for SPINE, in pGP380), available in Fabian Commichau's lab
Two-hybrid system
B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Fabian Commichau's lab
FLAG-tag construct
GP1194 (gudB, spc, based on pGP1331), GP1195 (gudB1, spc, based on pGP1331),  available in Jörg Stülke's lab
LacZ fusion
pGP651 (in pAC5), available in Jörg Stülke's lab PubMed
Antibody
antibody against RocG recognizes GudB, available in Jörg Stülke's lab
Labs working on this gene/protein
Linc Sonenshein, Tufts University, Boston, MA, USA Homepage
Fabian Commichau, Senftenberg, Germany homepage
References
Reviews
Loading
Original Publications
Loading

C36C8C9EEDCAD392D9BEC9728A1E0CBFF2F4E790

Page visits: 8992

Time of last update: 2025-04-04 09:34:01

Author of last update: Jstuelk