Difference between revisions of "OdhA"
(→Categories containing this gene/protein) |
|||
Line 46: | Line 46: | ||
= [[Categories]] containing this gene/protein = | = [[Categories]] containing this gene/protein = | ||
− | {{SubtiWiki category|[[carbon core metabolism]]}} | + | {{SubtiWiki category|[[carbon core metabolism]]}}, |
+ | {{SubtiWiki category|[[phosphoproteins]]}} | ||
= This gene is a member of the following [[regulons]] = | = This gene is a member of the following [[regulons]] = |
Revision as of 15:27, 20 April 2012
- Description: 2-oxoglutarate dehydrogenase (E1 subunit)
Gene name | odhA |
Synonyms | citK |
Essential | no |
Product | 2-oxoglutarate dehydrogenase (E1 subunit) |
Function | TCA cycle |
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 |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
carbon core metabolism, phosphoproteins
This gene is a member of the following regulons
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:
- Cofactor(s):
- Effectors of protein activity:
Database entries
- UniProt: P23129
- KEGG entry: [3]
- E.C. number: 1.2.4.2
Additional information
- extensive information on the structure and enzymatic properties of 2-oxoglutarate dehydrogenase can be found at Proteopedia
Expression and regulation
- Additional information:
Biological materials
- Mutant: GP671 (spc), GP665 (aphA3), GP684 (cat), available in Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke 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
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)