Difference between revisions of "SdhB"
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=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU28430&redirect=T BSU28430] | ||
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/sdhCAB.html] | * '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/sdhCAB.html] | ||
| Line 99: | Line 100: | ||
=== Database entries === | === Database entries === | ||
| + | * '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU28430&redirect=T BSU28430] | ||
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1NEK 1NEK] (''E. coli'') | * '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1NEK 1NEK] (''E. coli'') | ||
Revision as of 15:26, 2 April 2014
- 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: sdhB | |
| 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
- BsubCyc: BSU28430
- 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
- BsubCyc: BSU28430
- 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

