Difference between revisions of "SucD"
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|style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 900 bp, 300 aa | |style="background:#ABCDEF;" align="center"| '''Gene length, protein length''' || 900 bp, 300 aa | ||
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− | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[sucC]], [[ | + | |style="background:#ABCDEF;" align="center"|'''Immediate neighbours''' || ''[[sucC]], [[dprA]]'' |
|- | |- | ||
|colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB13483]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' | |colspan="2" style="background:#FAF8CC;" align="center"|'''Get the DNA and protein [http://srs.ebi.ac.uk/srsbin/cgi-bin/wgetz?-e+[EMBLCDS:CAB13483]+-newId sequences] <br/> (Barbe ''et al.'', 2009)''' |
Revision as of 19:59, 9 July 2009
- Description: succinyl-CoA synthetase (alpha subunit)
Gene name | sucD |
Synonyms | |
Essential | no |
Product | succinyl-CoA synthetase (alpha subunit) |
Function | TCA cycle |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 31 kDa, 5.587 |
Gene length, protein length | 900 bp, 300 aa |
Immediate neighbours | sucC, dprA |
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: BSU16100
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: succinate/malate CoA ligase alpha subunit family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: Reversible Michaelis-Menten FEBS Letters
- Domains:
- Modification: phosphorylation on (Ser-19 OR Thr-20) 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: P80865
- 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: GP720 (spc), available in Stülke lab
- 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)