OdhB

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

Gene name	odhB
Synonyms	citM
Essential	no 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: odhB
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, membrane proteins

This gene is a member of the following regulons

CcpA regulon

The gene

Basic information

• Locus tag: BSU19360

Database entries

• BsubCyc: BSU19360

• 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:
  • phosphorylated on several Arg residues PubMed

• Cofactors:
  • lipoic acid

• Effectors of protein activity:

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

• Localization:
  • membrane associated PubMed

Database entries

• BsubCyc: BSU19360

• 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 PubMed

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

• lacZ fusion:

• GFP fusion:

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

• Antibody:

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

References

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)

Raphael H Michna, Fabian M Commichau, Dominik Tödter, Christopher P Zschiedrich, Jörg Stülke
SubtiWiki-a database for the model organism Bacillus subtilis that links pathway, interaction and expression information.
Nucleic Acids Res: 2014, 42(Database issue);D692-8
[PubMed:24178028] [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)

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)