OdhA

• Description: 2-oxoglutarate dehydrogenase (E1 subunit)
  
  

Gene name	odhA
Synonyms	citK
Essential	no
Product	2-oxoglutarate dehydrogenase (E1 subunit)
Function	TCA cycle
Gene expression levels in SubtiExpress: odhA
Interactions involving this protein in SubtInteract: OdhA
Metabolic function and regulation of this protein in SubtiPathways: odhA
MW, pI	105 kDa, 5.871
Gene length, protein length	2823 bp, 941 aa
Immediate neighbours	odhB, yojO
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

carbon core metabolism, phosphoproteins

This gene is a member of the following regulons

CcpA regulon

The gene

Basic information

• Locus tag: BSU19370

Database entries

• BsubCyc: BSU19370

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: 2-oxoglutarate + [dihydrolipoyllysine-residue succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine + CO₂ (according to Swiss-Prot)

• Protein family: 2-oxoacid dehydrogenase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-66 and Arg-621 PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:
  • OdhA-OdhB-PdhD PubMed

• Localization:

Database entries

• BsubCyc: BSU19370

• Structure: 2JGD (from Escherichia coli, 38% identity, 55% similarity) PubMed

• UniProt: P23129

• KEGG entry: [3]

• E.C. number: 1.2.4.2

Additional information

• extensive information on the structure and enzymatic properties of 2-oxoglutarate dehydrogenase can be found at Proteopedia

Expression and regulation

• Operon: odhA-odhB PubMed

• Expression browser: odhA PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • repressed by glucose (2.4-fold) (CcpA) PubMed

• Regulatory mechanism:
  • CcpA: transcription repression PubMed

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 2760 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 30660 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 2474 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2111 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3918 PubMed

Biological materials

• Mutant:
  • GP671 (spc), GP684 (cat), GP1274 (cat) available in Jörg Stülke's lab
  • GP1276 (odhA-odhB::cat), available in Jörg Stülke's lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

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

• Antibody:

References

Reviews

K F Sheu, J P Blass
The alpha-ketoglutarate dehydrogenase complex.
Ann N Y Acad Sci: 1999, 893;61-78
[PubMed:10672230] [WorldCat.org] [DOI] (P p)

Original publications

Andreas Schmidt, Débora Broch Trentini, Silvia Spiess, Jakob Fuhrmann, Gustav Ammerer, Karl Mechtler, Tim Clausen
Quantitative phosphoproteomics reveals the role of protein arginine phosphorylation in the bacterial stress response.
Mol Cell Proteomics: 2014, 13(2);537-50
[PubMed:24263382] [WorldCat.org] [DOI] (I p)

Bogumiła C Marciniak, Monika Pabijaniak, Anne de Jong, Robert Dűhring, Gerald Seidel, Wolfgang Hillen, Oscar P Kuipers
High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis.
BMC Genomics: 2012, 13;401
[PubMed:22900538] [WorldCat.org] [DOI] (I e)

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Frederik M Meyer, Jan Gerwig, Elke Hammer, Christina Herzberg, Fabian M Commichau, Uwe Völker, Jörg Stülke
Physical interactions between tricarboxylic acid cycle enzymes in Bacillus subtilis: evidence for a metabolon.
Metab Eng: 2011, 13(1);18-27
[PubMed:20933603] [WorldCat.org] [DOI] (I p)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [WorldCat.org] [DOI] (P p)

Ciarán Condon, Jordi Rourera, Dominique Brechemier-Baey, Harald Putzer
Ribonuclease M5 has few, if any, mRNA substrates in Bacillus subtilis.
J Bacteriol: 2002, 184(10);2845-9
[PubMed:11976317] [WorldCat.org] [DOI] (P p)

O Resnekov, L Melin, P Carlsson, M Mannerlöv, A von Gabain, L Hederstedt
Organization and regulation of the Bacillus subtilis odhAB operon, which encodes two of the subenzymes of the 2-oxoglutarate dehydrogenase complex.
Mol Gen Genet: 1992, 234(2);285-96
[PubMed:1508153] [WorldCat.org] [DOI] (P p)

P Carlsson, L Hederstedt
Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase, respectively.
J Bacteriol: 1989, 171(7);3667-72
[PubMed:2500417] [WorldCat.org] [DOI] (P p)