Difference between revisions of "SdhB"

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(Biological materials)
(Biological materials)
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* '''Mutant:'''
 
* '''Mutant:'''
** GP792 (''sdhCAB''::''phleo''), available in [[Jörg Stülke]]'s lab
+
** GP792 (''[[sdhC]]-[[sdhA]]-[[sdhB]]''::''phleo''), available in [[Jörg Stülke]]'s lab
  
 
* '''Expression vector:'''
 
* '''Expression vector:'''

Revision as of 14:11, 13 August 2013

  • Description: succinate dehydrogenase

Gene name sdhB
Synonyms
Essential no
Product succinate dehydrogenase (iron-sulfur protein)
Function TCA cycle
Gene expression levels in SubtiExpress: sdhB
Interactions involving this protein in SubtInteract: SdhB
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 ysmA, sdhA
Sequences Protein DNA DNA_with_flanks
Genetic context
SdhB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SdhB expression.png















Categories containing this gene/protein

carbon core metabolism, membrane proteins

This gene is a member of the following regulons

FsrA regulon

The gene

Basic information

  • Locus tag: BSU28430

Phenotypes of a mutant

Database entries

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

Additional information

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

Database entries

  • Structure: 1NEK (E. coli)
  • 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
  • extensive information on the structure and enzymatic properties of succinate dehydrogenase can be found at Proteopedia

Expression and regulation

  • Regulation: constitutive
  • Regulatory mechanism:
  • Additional information:

Biological materials

  • Expression vector:
  • lacZ fusion:
  • GFP fusion: GP1436 (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: GP1426 (spc, based on pGP1331), available in the Stülke lab

Labs working on this gene/protein

Your additional remarks

References

Reviews

Lars Hederstedt
Succinate:quinone oxidoreductase in the bacteria Paracoccus denitrificans and Bacillus subtilis.
Biochim Biophys Acta: 2002, 1553(1-2);74-83
[PubMed:11803018] [WorldCat.org] [DOI] (P p)

Original publications