SdhB

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

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, SdhB-SdhC (as part of the SdhC-SdhB-SdhA complex)

• Localization: attached to the membrane PubMed

Database entries

• Structure: 1NEK (E. coli)

• UniProt: 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
• extensive information on the structure and enzymatic properties of succinate dehydrogenase can be found at Proteopedia

Expression and regulation

• Operon: sdhC-sdhA-sdhB PubMed

• Expression browser: sdhB PubMed

• Sigma factor: SigA PubMed

• Regulation: constitutive
  • part of the iron sparing response (FsrA) PubMed

• Regulatory mechanism:
  • FsrA: translation inhibition PubMed

• Additional information:

Biological materials

• Mutant:

• 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

References

Gregory T Smaldone, Olga Revelles, Ahmed Gaballa, Uwe Sauer, Haike Antelmann, John D Helmann
A global investigation of the Bacillus subtilis iron-sparing response identifies major changes in metabolism.
J Bacteriol: 2012, 194(10);2594-605
[PubMed:22389480] [WorldCat.org] [DOI] (I p)

Victoria Yankovskaya, Rob Horsefield, Susanna Törnroth, César Luna-Chavez, Hideto Miyoshi, Christophe Léger, Bernadette Byrne, Gary Cecchini, So Iwata
Architecture of succinate dehydrogenase and reactive oxygen species generation.
Science: 2003, 299(5607);700-4
[PubMed:12560550] [WorldCat.org] [DOI] (I p)

C Hägerhäll, V Sled, L Hederstedt, T Ohnishi
The trinuclear iron-sulfur cluster S3 in Bacillus subtilis succinate:menaquinone reductase; effects of a mutation in the putative cluster ligation motif on enzyme activity and EPR properties.
Biochim Biophys Acta: 1995, 1229(3);356-62
[PubMed:7748886] [WorldCat.org] [DOI] (P p)

C Hägerhäll, R Aasa, C von Wachenfeldt, L Hederstedt
Two hemes in Bacillus subtilis succinate:menaquinone oxidoreductase (complex II).
Biochemistry: 1992, 31(32);7411-21
[PubMed:1324713] [WorldCat.org] [DOI] (P p)

L Melin, H Fridén, E Dehlin, L Rutberg, A von Gabain
The importance of the 5'-region in regulating the stability of sdh mRNA in Bacillus subtilis.
Mol Microbiol: 1990, 4(11);1881-9
[PubMed:1707123] [WorldCat.org] [DOI] (P p)

L Melin, L Rutberg, A von Gabain
Transcriptional and posttranscriptional control of the Bacillus subtilis succinate dehydrogenase operon.
J Bacteriol: 1989, 171(4);2110-5
[PubMed:2495271] [WorldCat.org] [DOI] (P p)

A AEvarsson, L Hederstedt
Ligands to the 2Fe iron-sulfur center in succinate dehydrogenase.
FEBS Lett: 1988, 232(2);298-302
[PubMed:2837411] [WorldCat.org] [DOI] (P p)

L Melin, K Magnusson, L Rutberg
Identification of the promoter of the Bacillus subtilis sdh operon.
J Bacteriol: 1987, 169(7);3232-6
[PubMed:3036777] [WorldCat.org] [DOI] (P p)

M K Phillips, L Hederstedt, S Hasnain, L Rutberg, J R Guest
Nucleotide sequence encoding the flavoprotein and iron-sulfur protein subunits of the Bacillus subtilis PY79 succinate dehydrogenase complex.
J Bacteriol: 1987, 169(2);864-73
[PubMed:3027051] [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
Orientation of succinate dehydrogenase and cytochrome b558 in the Bacillus subtilis cytoplasmic membrane.
J Bacteriol: 1983, 153(1);57-65
[PubMed:6401289] [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)