Difference between revisions of "SucC"
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|style="background:#ABCDEF;" align="center"|'''Function''' || TCA cycle | |style="background:#ABCDEF;" align="center"|'''Function''' || TCA cycle | ||
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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]''' | ||
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 41 kDa, 4.846 | |style="background:#ABCDEF;" align="center"| '''MW, pI''' || 41 kDa, 4.846 |
Revision as of 12:43, 11 June 2009
- Description: succinyl-CoA synthetase (beta subunit)
Gene name | sucC |
Synonyms | |
Essential | no |
Product | succinyl-CoA synthetase (beta subunit) |
Function | TCA cycle |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 41 kDa, 4.846 |
Gene length, protein length | 1155 bp, 385 aa |
Immediate neighbours | ylqH, sucD |
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: BSU16090
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + succinate + CoA = ADP + phosphate + succinyl-CoA (according to Swiss-Prot)
- Protein family: ATP-grasp domain (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: Reversible Michaelis-Menten FEBS Letters
- Domains:
- Modification: phosphorylation on Ser-220 PubMed
- Cofactor(s):
- Effectors of protein activity:
- Inhibited by 2-oxoglutarate, ATP and NADH FEBS Letters
- GTP is not accept by the enzyme FEBS Letters
- Inhibited by 2-oxoglutarate, ATP and NADH FEBS Letters
- Interactions:
- Localization:
Database entries
- Structure: 1JKJ (E. coli)
- Swiss prot entry: P80886
- KEGG entry: [3]
- E.C. number: 6.2.1.5
Additional information
The enzyme is a dimer FEBS Letters
Expression and regulation
- Sigma factor:
- Regulatory mechanism: CcpA: transcription repression
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307]
[WorldCat.org]
[DOI]
(P p)
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P p)
- Blencke et al. (2003) Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways. Metab Eng. 5: 133-149 PubMed
- Macek et al. (2007) The serine/ threonine/ tyrosine phosphoproteome of the model bacterium Bacillus subtilis. Mol. Cell. Proteomics 6: 697-707 PubMed
- Danson MJ et al. (1984) Citric acid cycle enzymes of the archaebacteria: citrate synthase and succinate thiokinase. FEBS Letters. FEBS Letters
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed