Difference between revisions of "OdhB"

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(Categories containing this gene/protein)
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=== Additional information===
=== Additional information===
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* '''Kinetic information:'''
* '''Kinetic information:'''
* '''Domains:'''  
* '''[[Domains]]:'''  
* '''Modification:'''
* '''Modification:'''
** phosphorylated on several Arg residues {{PubMed|24263382}}
* '''Cofactor(s):'''
* '''[[Cofactors]]:'''
** lipoic acid
** lipoic acid
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<pubmed> 10672230</pubmed>
<pubmed> 10672230</pubmed>
==Original publications==
==Original publications==
<pubmed>2500417,,1508153,12850135 18763711 12682299,11976317  20933603 24178028 </pubmed>
<pubmed>2500417,,1508153,12850135 18763711 12682299,11976317  20933603 24178028 24263382</pubmed>
[[Category:Protein-coding genes]]
[[Category:Protein-coding genes]]

Revision as of 10:55, 17 December 2013

  • 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:
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
OdhB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
OdhB expression.png

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

Phenotypes of a mutant

Database entries

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

Additional information

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)

Extended information on the protein

  • Kinetic information:
  • Modification:
    • phosphorylated on several Arg residues PubMed
  • Effectors of protein activity:

Database entries

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

  • Expression vector:
  • 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

Labs working on this gene/protein

Your additional remarks



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

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] (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] (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)