Difference between revisions of "SdhC"
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 606 bp, 202 aa | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 606 bp, 202 aa | ||
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− | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[ | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[sdhA]], [[yslB]]'' |
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|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB14805]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB14805]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' |
Revision as of 09:15, 7 December 2009
- Description: succinate dehydrogenase(cytochrome b558 subunit)
Gene name | sdhC |
Synonyms | |
Essential | no |
Product | succinate dehydrogenase (cytochrome b558 subunit) |
Function | TCA cycle |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 22 kDa, 9.831 |
Gene length, protein length | 606 bp, 202 aa |
Immediate neighbours | sdhA, yslB |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU28450
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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): Fe
- Effectors of protein activity:
- Localization: membrane protein PubMed
Database entries
- Structure: 1NEK (E. coli)
- UniProt: P08064
- KEGG entry: [3]
- E.C. number: 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
- 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)
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)
M Matsson, D Tolstoy, R Aasa, L Hederstedt
The distal heme center in Bacillus subtilis succinate:quinone reductase is crucial for electron transfer to menaquinone.
Biochemistry: 2000, 39(29);8617-24
[PubMed:10913269]
[WorldCat.org]
[DOI]
(P p)
C Hägerhäll, H Fridén, R Aasa, L Hederstedt
Transmembrane topology and axial ligands to hemes in the cytochrome b subunit of Bacillus subtilis succinate:menaquinone reductase.
Biochemistry: 1995, 34(35);11080-9
[PubMed:7669765]
[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)
H Fridén, M R Cheesman, L Hederstedt, K K Andersson, A J Thomson
Low temperature EPR and MCD studies on cytochrome b-558 of the Bacillus subtilis succinate: quinone oxidoreductase indicate bis-histidine coordination of the heme iron.
Biochim Biophys Acta: 1990, 1041(2);207-15
[PubMed:2176107]
[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)
H Fridén, L Hederstedt
Role of His residues in Bacillus subtilis cytochrome b558 for haem binding and assembly of succinate: quinone oxidoreductase (complex II).
Mol Microbiol: 1990, 4(6);1045-56
[PubMed:2120540]
[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)
H Fridén, L Rutberg, K Magnusson, L Hederstedt
Genetic and biochemical characterization of Bacillus subtilis mutants defective in expression and function of cytochrome b-558.
Eur J Biochem: 1987, 168(3);695-701
[PubMed:3117551]
[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)
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)