Difference between revisions of "SdhA"
Cadu Cunha (talk | contribs) (→Additional information) |
Cadu Cunha (talk | contribs) (→Extended information on the protein) |
||
Line 68: | Line 68: | ||
* '''Modification:''' phosphorylated [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed] | * '''Modification:''' phosphorylated [http://www.ncbi.nlm.nih.gov/pubmed/16493705 PubMed], [http://www.ncbi.nlm.nih.gov/pubmed/17726680 PubMed] | ||
− | * '''Cofactor(s):''' | + | * '''Cofactor(s):''' Fe |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
+ | ** Inhibited by 2-(n-Heptyl)-4-hydroxy-quinoline N-oxide [http://www.ncbi.nlm.nih.gov/pubmed/3910107 PubMed] | ||
+ | ** Activated by Cytochrome b558 [http://www.ncbi.nlm.nih.gov/pubmed/6799760 PubMed] | ||
* '''Interactions:''' [[SdhA]]-[[SdhB]]-[[SdhC]] | * '''Interactions:''' [[SdhA]]-[[SdhB]]-[[SdhC]] |
Revision as of 16:24, 10 June 2009
- Description: succinate dehydrogenase (flavoprotein subunit)
Gene name | sdhA |
Synonyms | citF |
Essential | no |
Product | succinate dehydrogenase (flavoprotein subunit) |
Function | TCA cycle |
MW, pI | 65 kDa, 5.714 |
Gene length, protein length | 1758 bp, 586 aa |
Immediate neighbours | sdhC, sdhB |
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: BSU28440
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: FRD/SDH subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Cofactor(s): Fe
- Effectors of protein activity:
- Localization: membrane protein PubMed
Database entries
- Structure: 1NEK (E. coli)
- Swiss prot entry: P08065
- 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
- 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:
- 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)
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)
- Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
- Hahne et al. (2008) From complementarity to comprehensiveness - targeting the membrane proteome of growing Bacillus subtilis by divergent approaches. Proteomics 8: 4123-4136 PubMed# Eymann et al. (2007) Dynamics of protein phosphorylation on Ser/Thr/Tyr in Bacillus subtilis. Proteomics 7: 3509-3526. PubMed
- Levine et al. (2006) Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes. Proteomics 6, 2157-2173. PubMed
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed