SdhA

• Description: succinate dehydrogenase (flavoprotein subunit)
  
  

Gene name	sdhA
Synonyms	citF
Essential	no
Product	succinate dehydrogenase (flavoprotein subunit)
Function	TCA cycle
MW, pI	65 kDa, 5.714
Gene length, protein length	1758 bp, 586 aa
Immediate neighbours	sdhC, sdhB
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU28440

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Succinate + acceptor = fumarate + reduced acceptor (according to Swiss-Prot)

• Protein family: FRD/SDH subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated PubMed, PubMed

• Cofactor(s): Fe

• Effectors of protein activity:
  • Inhibited by 2-(n-Heptyl)-4-hydroxy-quinoline N-oxide PubMed
  • Activated by Cytochrome b558 PubMed

• Interactions: SdhA-SdhB-SdhC

• Localization: membrane protein PubMed

Database entries

• Structure: 1NEK (E. coli)

• Swiss prot entry: P08065

• KEGG entry: [3]

• E.C. number: 1.3.99.1

Additional information

This enzyme is a trimer membrane-bound PubMed PubMed

• One subunit is bound to citochrome b558, and this subunit is the one bound to the cytosolic side of the membrane PubMed PubMed
• Another subunit is the flavoprotein one, required for FAD usage PubMed PubMed
• The other subunit has an iron-sulphur domain necessary for the catalytic activity PubMed PubMed

Expression and regulation

• Operon: sdhC-sdhA-sdhB PubMed

• Sigma factor: SigA PubMed

• Regulation: constitutive

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant: GP743 (sdhCA, cat), available in Stülke lab

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

Christine Eymann, Dörte Becher, Jörg Bernhardt, Katrin Gronau, Anja Klutzny, Michael Hecker
Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis.
Proteomics: 2007, 7(19);3509-26
[PubMed:17726680] [WorldCat.org] [DOI] (P p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

S T Cole, C Condon, B D Lemire, J H Weiner
Molecular biology, biochemistry and bioenergetics of fumarate reductase, a complex membrane-bound iron-sulfur flavoenzyme of Escherichia coli.
Biochim Biophys Acta: 1985, 811(4);381-403
[PubMed:3910107] [WorldCat.org] [DOI] (P p)

L Hederstedt, L Rutberg
Succinate dehydrogenase--a comparative review.
Microbiol Rev: 1981, 45(4);542-55
[PubMed:6799760] [WorldCat.org] [DOI] (P p)

1. Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
2. Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed# Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
3. Levine et al. (2006) Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 6, 2157-2173. PubMed
4. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed