trigger enzyme: glutamate dehydrogenase (cryptic in 168 and derivatives)
function
glutamate utilization, control of GltC activity
product
trigger enzyme: glutamate dehydrogenase
Genomic Context
categories
[category|SW 2|Metabolism] → [category|SW 2.3|Amino acid/ nitrogen metabolism] → [category|SW 2.3.2|Utilization of amino acids] → [category|SW 2.3.2.1|Utilization of glutamine/ glutamate][category|SW 3|Information processing] → [category|SW 3.4|Regulation of gene expression] → [category|SW 3.4.2|Transcription factors and their control] → [category|SW 3.4.2.7|Control of transcription factor (other than two-component system)][category|SW 3|Information processing] → [category|SW 3.4|Regulation of gene expression] → [category|SW 3.4.3|Trigger enzyme] → [category|SW 3.4.3.2|Trigger enzymes that control gene expression by protein-protein interaction with transcription factors][category|SW 6|Groups of genes] → [category|SW 6.4|Phosphoproteins] → [category|SW 6.4.1|Phosphorylation on an Arg residue][SW|Categories] containing this gene/protein
[SW|utilization of amino acids], [SW|glutamate metabolism], [SW|transcription factors and their control], [SW|trigger enzyme], [SW|phosphoproteins]Gene
Coordinates on the chromosome (coding sequence)
2,402,067 -> 2,403,350
Phenotypes of a mutant
The gene is cryptic. If ''gudB'' is activated (''gudB1'' mutation), the bacteria are able to utilize glutamate as the only carbon source. [http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Abstract&list_uids=18326565 PubMed]A ''[protein|search|rocG] [protein|search|gudB]'' mutant is sensitive to ß-lactam antibiotics such as cefuroxime and to fosfomycin due to the downregulation of the [SW|SigW regulon] [Pubmed|22178969]transcription profile of a ''[protein|search|rocG] [protein|search|gudB]'' mutant strain: [http://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE34383&submit.x=22&submit.y=9 GEO] [Pubmed|22178969] The protein
Catalyzed reaction/ biological activity
L-glutamate H2O NAD = 2-oxoglutarate NH3 NADH H (according to Swiss-Prot) Protein family
Glu/Leu/Phe/Val dehydrogenases family (according to Swiss-Prot)Paralogous protein(s)
[protein|search|RocG]Modification
phosphorylated on Arg-56, Arg-83, and Arg-421 and/or Arg-423 [Pubmed|22517742][SW|Cofactors]
Structure
[PDB|3K8Z] (enzymatically active GudB1) [Pubmed|20630473][SW|Interactions]
[protein|search|GltC]-[protein|search|GudB] [Pubmed|25711804]Expression and Regulation
Operon
''gudB'' [Pubmed|22178973][SW|Sigma factor]
[protein|search|SigA] [PubMed|9829940]Regulation
constitutively expressed [Pubmed|22178973]Additional information
GudB is subject to Clp-dependent proteolysis upon glucose starvation [PubMed|17981983]Biological materials
Mutant
GP691 (''ΔgudB::cat''), GP1160 (''ΔgudB::aphA3'') both available in [SW|Jörg Stülke]'s labExpression vector
for purification of GudB from ''E. coli'' carrying an N-terminal Strep-tag: pGP863 (in [SW|pGP172]) available in [SW|Jörg Stülke]'s labfor purification of GudB1 from ''E. coli'' carrying an N-terminal Strep-tag: pGP864 (in [SW|pGP172]) available in [SW|Jörg Stülke]'s labfor ectopic expression of ''gudB'' with its native promoter: pGP900 (in [protein|search|pAC5]), available in [SW|Jörg Stülke]'s labwild type ''gudB'', expression in ''B. subtilis'', in [SW|pBQ200]: pGP1712, available in [SW|Jörg Stülke]'s labpBP179 (N-terminal Strep-tag ''gudB'', purification from ''B. subtilis'', for [SW|SPINE], in [SW|pGP380]), available in [SW|Fabian Commichau]'s lab lacZ fusion
pGP651 (in [protein|search|pAC5]), available in [SW|Jörg Stülke]'s labtwo-hybrid system
B. pertussis adenylate cyclase-based bacterial two hybrid system ([SW|BACTH]), available in [SW| Fabian Commichau]'s labFLAG-tag construct
GP1194 (''gudB'', ''spc'', based on [SW|pGP1331]), GP1195 (''gudB1'', ''spc'', based on [SW|pGP1331]), available in [SW|Jörg Stülke]'s labAntibody
antibody against [protein|search|RocG] recognizes GudB, available in [SW|Jörg Stülke]'s labLabs 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|Fabian Commichau] University of Göttingen, Germany [http://genmibio.uni-goettingen.de/index.php?id=130 Homepage]References
Reviews
19698086,8299344,7705101,19895831,22625175 Original publications
18603778,9829940,17183217,18723616,18326565,20630473,17981983,21219666,22178973,22517742,23338837,22178969,23785476,24263382,24473333,25610436,25711804