OdhB

• Description: 2-oxoglutarate dehydrogenase complex (dihydrolipoamide transsuccinylase, E2 subunit)
  
  

Gene name	odhB
Synonyms	citM
Essential	yes PubMed
Product	2-oxoglutarate dehydrogenase complex (dihydrolipoamide transsuccinylase, E2 subunit)
Function	TCA cycle
Gene expression levels in SubtiExpress: odhB
Interactions involving this protein in SubtInteract: OdhB
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	45 kDa, 4.859
Gene length, protein length	1251 bp, 417 aa
Immediate neighbours	yocS, odhA
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, essential genes, membrane proteins

This gene is a member of the following regulons

CcpA regulon

The gene

Basic information

• Locus tag: BSU19360

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Succinyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-succinyldihydrolipoyl)lysine (according to Swiss-Prot)

• Protein family: sodium:bile acid symporter family (according to Swiss-Prot)

• Paralogous protein(s): AcoC, BkdB, PdhC

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):
  • lipoic acid

• Effectors of protein activity:

• Interactions:
  • OdhA-OdhB-PdhD PubMed
  • OdhB-Icd PubMed

• Localization:
  • membrane associated PubMed

Database entries

• Structure: 1C4T (from Escherichia coli bl21, 57% identity, 78% similarity) PubMed

• UniProt: P16263

• KEGG entry: [3]

• E.C. number: 2.3.1.61

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: 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:
  • GP1276 (odhA-odhB::cat), available in Jörg Stülke's lab

• Expression vector:
  • pGP1145 (N-terminal Strep-tag, for SPINE, purification from B. subtilis, in pGP380) (available in Stülke lab)

• lacZ fusion:

• GFP fusion:

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

• Antibody:

• FLAG-tag construct: GP1424 (spc, based on pGP1331), available in the Stülke lab

References

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)

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [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)

K Kobayashi, S D Ehrlich, A Albertini, G Amati, K K Andersen, M Arnaud, K Asai, S Ashikaga, S Aymerich, P Bessieres, F Boland, S C Brignell, S Bron, K Bunai, J Chapuis, L C Christiansen, A Danchin, M Débarbouille, E Dervyn, E Deuerling, K Devine, S K Devine, O Dreesen, J Errington, S Fillinger, S J Foster, Y Fujita, A Galizzi, R Gardan, C Eschevins, T Fukushima, K Haga, C R Harwood, M Hecker, D Hosoya, M F Hullo, H Kakeshita, D Karamata, Y Kasahara, F Kawamura, K Koga, P Koski, R Kuwana, D Imamura, M Ishimaru, S Ishikawa, I Ishio, D Le Coq, A Masson, C Mauël, R Meima, R P Mellado, A Moir, S Moriya, E Nagakawa, H Nanamiya, S Nakai, P Nygaard, M Ogura, T Ohanan, M O'Reilly, M O'Rourke, Z Pragai, H M Pooley, G Rapoport, J P Rawlins, L A Rivas, C Rivolta, A Sadaie, Y Sadaie, M Sarvas, T Sato, H H Saxild, E Scanlan, W Schumann, J F M L Seegers, J Sekiguchi, A Sekowska, S J Séror, M Simon, P Stragier, R Studer, H Takamatsu, T Tanaka, M Takeuchi, H B Thomaides, V Vagner, J M van Dijl, K Watabe, A Wipat, H Yamamoto, M Yamamoto, Y Yamamoto, K Yamane, K Yata, K Yoshida, H Yoshikawa, U Zuber, N Ogasawara
Essential Bacillus subtilis genes.
Proc Natl Acad Sci U S A: 2003, 100(8);4678-83
[PubMed:12682299] [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)