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• Description: 2-oxoglutarate dehydrogenase (E1 subunit)
  
  

Gene name	odhA
Synonyms	citK
Essential	no
Product	2-oxoglutarate dehydrogenase (E1 subunit)
Function	TCA cycle
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	yojO, odhB
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

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

• Localization:

Database entries

• Structure:

• Swiss prot entry: P23129

• KEGG entry: [3]

• E.C. number: 1.2.4.2

Expression and regulation

• Operon: odhA-odhB

• Sigma factor: SigA

• Regulation: constitutive

• Regulatory mechanism:

• Additional information:

Biological materials

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

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

1. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed