OdhA

• Description: 2-oxoglutarate dehydrogenase (E1 subunit)
  
  

Gene name	odhA
Synonyms	citK
Essential	no
Product	2-oxoglutarate dehydrogenase (E1 subunit)
Function	TCA cycle
Interactions involving this protein in SubtInteract: OdhA
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	105 kDa, 5.871
Gene length, protein length	2823 bp, 941 aa
Immediate neighbours	odhB, yojO
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

carbon core metabolism

This gene is a member of the following regulons

CcpA regulon

The gene

Basic information

• Locus tag: BSU19370

Database entries

• 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:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • OdhA-OdhB-PdhD PubMed

• Localization:

Database entries

• 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

• Sigma factor: SigA PubMed

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

• Regulatory mechanism:
  • CcpA: transcription repression PubMed

• Additional information:

Biological materials

• Mutant: GP671 (spc), GP665 (aphA3), GP684 (cat), available in Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

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

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)