SdhC
- Description: succinate dehydrogenase(cytochrome b558 subunit)
Gene name | sdhC |
Synonyms | |
Essential | no |
Product | succinate dehydrogenase (cytochrome b558 subunit) |
Function | TCA cycle |
MW, pI | 22 kDa, 9.831 |
Gene length, protein length | 606 bp, 202 aa |
Immediate neighbours | yslB, sdhA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
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Contents
The gene
Basic information
- Locus tag: BSU28450
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
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
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: cytochrome b558 family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Localization: cell membrane (according to Swiss-Prot), membrane protein PubMed
Database entries
- Structure: 1NEK (E. coli)
- Swiss prot entry: P08064
- KEGG entry: [3]
- E.C. number: 1.3.99.1
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant: GP743 (sdhCA, cat), available in Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
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)
Ahmed Gaballa, Haike Antelmann, Claudio Aguilar, Sukhjit K Khakh, Kyung-Bok Song, Gregory T Smaldone, John D Helmann
The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins.
Proc Natl Acad Sci U S A: 2008, 105(33);11927-32
[PubMed:18697947]
[WorldCat.org]
[DOI]
(I p)
- Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed
- Gaballa A, Antelmann H, Aguilar C, Khakh SK, Song KB, Smaldone GT, Helmann JD (2008) The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins. PNAS 105: 11927-11932. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed