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
Sequences	Protein DNA Advanced_DNA
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)