SdhB

• Description: succinate dehydrogenase
  
  

Gene name	sdhB
Synonyms
Essential	no
Product	succinate dehydrogenase (iron-sulfur protein)
Function	TCA cycle
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	28 kDa, 7.989
Gene length, protein length	759 bp, 253 aa
Immediate neighbours	sdhA, ysmA
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: BSU28430

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: succinate dehydrogenase/fumarate reductase iron-sulfur protein family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• 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: attached to the membrane PubMed

Database entries

• Structure: 1NEK (E. coli)

• Swiss prot entry: P08066

• KEGG entry: [3]

• E.C. number:EC 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:

• Expression vector:

• lacZ fusion:

• GFP fusion:

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

• Antibody:

References

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. Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed
2. Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed