SucD

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  • Description: succinyl-CoA synthetase (alpha subunit)

Gene name sucD
Synonyms
Essential no
Product succinyl-CoA synthetase (alpha subunit)
Function TCA cycle
Metabolic function and regulation of this protein in SubtiPathways:
Central C-metabolism
MW, pI 31 kDa, 5.587
Gene length, protein length 900 bp, 300 aa
Immediate neighbours sucC, dprA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SucD context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU16100

Phenotypes of a mutant

Database entries

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

Additional information

Categories containing this gene/protein

ATP synthesis, carbon core metabolism, phosphoproteins

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + succinate + CoA = ADP + phosphate + succinyl-CoA (according to Swiss-Prot)
  • Protein family: succinate/malate CoA ligase alpha subunit family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information: Reversible Michaelis-Menten FEBS Letters
  • Domains:
  • Modification: phosphorylation on (Ser-19 OR Thr-20) PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization:

Database entries

  • Structure: 1JKJ (E. coli)
  • KEGG entry: [3]

Additional information

The enzyme is a dimer FEBS Letters

Expression and regulation

  • Sigma factor:
  • Regulation: repressed by glucose (2.4-fold) (CcpA) PubMed
  • Regulatory mechanism: CcpA: transcription repression PubMed
  • Additional information:

Biological materials

  • Mutant: GP720 (spc), 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

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)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol. Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P 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)

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] (P p)