OdhA

From SubtiWiki
Revision as of 13:11, 13 August 2013 by Aklewing (talk | contribs) (Biological materials)
Jump to: navigation, search
  • 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:
Central C-metabolism
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
OdhA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
OdhA expression.png















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

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

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
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 2JGD (from Escherichia coli, 38% identity, 55% similarity) PubMed
  • KEGG entry: [3]

Additional information

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

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Mutant: GP671 (spc), GP684 (cat), GP1274 (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:

Labs working on this gene/protein

Your additional remarks

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

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)