SdhA

• Description: succinate dehydrogenase (flavoprotein subunit)
  
  

Gene name	sdhA
Synonyms	citF
Essential	no
Product	succinate dehydrogenase (flavoprotein subunit)
Function	TCA cycle
Interactions involving this protein in SubtInteract: SdhA
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism
MW, pI	65 kDa, 5.714
Gene length, protein length	1758 bp, 586 aa
Immediate neighbours	sdhB, sdhC
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

carbon core metabolism, membrane proteins, phosphoproteins

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

• Localization: attached to the membrane PubMed

Database entries

• Structure: 1NEK (E. coli)

• UniProt: P08065

• KEGG entry: [3]

• E.C. number: 1.3.99.1

Additional information

• This enzyme is a membrane-bound trimer PubMed PubMed
  • One subunit is bound to cytochrome 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

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

• 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)

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, 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)

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)

K Magnusson, L Hederstedt, L Rutberg
Cloning and expression in Escherichia coli of sdhA, the structural gene for cytochrome b558 of the Bacillus subtilis succinate dehydrogenase complex.
J Bacteriol: 1985, 162(3);1180-5
[PubMed:2987185] [WorldCat.org] [DOI] (P p)

L Hederstedt
Succinate dehydrogenase mutants of Bacillus subtilis lacking covalently bound flavin in the flavoprotein subunit.
Eur J Biochem: 1983, 132(3);589-93
[PubMed:6406223] [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)