Difference between revisions of "SdhA"
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU28440 sdhA] | |colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU28440 sdhA] | ||
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− | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http:// | + | |colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=SdhA SdhA] |
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]''' | |colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/carbon_flow.html Central C-metabolism]''' |
Revision as of 09:04, 12 November 2013
- Description: succinate dehydrogenase (flavoprotein subunit)
Gene name | sdhA |
Synonyms | citF |
Essential | no |
Product | succinate dehydrogenase (flavoprotein subunit) |
Function | TCA cycle |
Gene expression levels in SubtiExpress: sdhA | |
Interactions involving this protein in SubtInteract: SdhA | |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 65 kDa, 5.714 |
Gene length, protein length | 1758 bp, 586 aa |
Immediate neighbours | sdhB, sdhC |
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, phosphoproteins
This gene is a member of the following regulons
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:
- attached to the membrane PubMed
Database entries
- Structure: 1NEK (E. coli)
- UniProt: P08065
- KEGG entry: [3]
- E.C. number: 1.3.99.1
Additional information
- This enzyme is a membrane-bound trimer PubMed PubMed
- One subunit is bound to cytochrome 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:
- GP743 (sdhC-sdhA, cat), available in Jörg Stülke's lab
- GP792 (sdhC-sdhA-sdhB::phleo), available in Jörg Stülke's lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's 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