Difference between revisions of "SdhB"

From SubtiWiki
Jump to: navigation, search
(Biological materials)
(Additional information)
Line 85: Line 85:
  
 
=== Additional information===
 
=== Additional information===
 +
This enzyme is a trimer membrane-bound [http://www.ncbi.nlm.nih.gov/pubmed/3910107 PubMed] [http://www.ncbi.nlm.nih.gov/pubmed/6799760 PubMed]
 +
* One subunit is bound to citochrome b558, and this subunit is the one bound to the cytosolic side of the membrane [http://www.ncbi.nlm.nih.gov/pubmed/3910107 PubMed] [http://www.ncbi.nlm.nih.gov/pubmed/6799760 PubMed]
 +
* Another subunit is the flavoprotein one, required for FAD usage [http://www.ncbi.nlm.nih.gov/pubmed/3910107 PubMed] [http://www.ncbi.nlm.nih.gov/pubmed/6799760 PubMed]
 +
* The other subunit has an iron-sulphur domain necessary for the catalytic activity [http://www.ncbi.nlm.nih.gov/pubmed/3910107 PubMed] [http://www.ncbi.nlm.nih.gov/pubmed/6799760 PubMed]
  
 
=Expression and regulation=
 
=Expression and regulation=

Revision as of 16:19, 10 June 2009

  • Description: succinate dehydrogenase

Gene name sdhB
Synonyms
Essential no
Product succinate dehydrogenase (iron-sulfur protein)
Function TCA cycle
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
SdhB context.gif
This image was kindly provided by SubtiList



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):
  • Effectors of protein activity:
  • Localization: attached to the membrane 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

Expression and regulation

  • 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:

Labs working on this gene/protein

Your additional remarks

References

  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