Difference between revisions of "SdhB"
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* '''Mutant:''' | * '''Mutant:''' | ||
− | ** GP792 ('' | + | ** GP792 (''[[sdhC]]-[[sdhA]]-[[sdhB]]''::''phleo''), available in [[Jörg Stülke]]'s lab |
* '''Expression vector:''' | * '''Expression vector:''' |
Revision as of 14:11, 13 August 2013
- 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 |
Contents
Categories containing this gene/protein
carbon core metabolism, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28430
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: 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:
- 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
- Additional information:
Biological materials
- Mutant:
- GP792 (sdhC-sdhA-sdhB::phleo), available in Jörg Stülke's lab
- Expression vector:
- lacZ fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Lars Hederstedt
Succinate:quinone oxidoreductase in the bacteria Paracoccus denitrificans and Bacillus subtilis.
Biochim Biophys Acta: 2002, 1553(1-2);74-83
[PubMed:11803018]
[WorldCat.org]
[DOI]
(P p)
Original publications