SucD

• Description: succinyl-CoA synthetase (alpha subunit)
  
  

Gene name	sucD
Synonyms
Essential	no
Product	succinyl-CoA synthetase (alpha subunit)
Function	TCA cycle
Gene expression levels in SubtiExpress: sucD
Interactions involving this protein in SubtInteract: SucD
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

ATP synthesis, carbon core metabolism, phosphoproteins

This gene is a member of the following regulons

CcpA regulon

The gene

Basic information

• Locus tag: BSU16100

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:
  • Inhibited by 2-oxoglutarate, ATP and NADH FEBS Letters
  • GTP is not accepted by the enzyme FEBS Letters

• Interactions:
  • SucC-SucD PubMed

• Localization:

Database entries

• Structure: 1JKJ (E. coli)

• UniProt: P80865

• KEGG entry: [3]

• E.C. number: 6.2.1.5

Additional information

• extensive information on the structure and enzymatic properties of succinyl-CoA synthetase can be found at Proteopedia

Expression and regulation

• Operon: sucC-sucD PubMed

• Expression browser: sucD PubMed

• 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
  • 1A1008 ( sucD::spec), PubMed, available at BGSC

• Expression vector:

• lacZ fusion:

• GFP fusion: GP1435 (spc, based on pGP1870), available in the Stülke lab

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

• Antibody:

• FLAG-tag construct: GP1425 (spc, based on pGP1331), available in the Stülke lab

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] [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)