Difference between revisions of "LysC"
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<pubmed> 19946135 </pubmed> | <pubmed> 19946135 </pubmed> | ||
==Orginal Publications== | ==Orginal Publications== | ||
− | <pubmed>2168395,1624109,14523230,2559145,14597663,2557260,,12850135 12107147, 14523230, 12850135, 12107147, 17981983 19636616 </pubmed> | + | <pubmed>2168395,1624109,14523230,2559145,14597663,2557260,,12850135 12107147, 14523230, 12850135, 12107147, 17981983 19636616 21169337 </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 10:29, 21 December 2010
- Description: aspartokinase II (alpha and beta subunits)
Gene name | lysC |
Synonyms | ask, aecA |
Essential | no |
Product | aspartokinase II (alpha and beta subunits) |
Function | biosynthesis of lysine |
Metabolic function and regulation of this protein in SubtiPathways: Lys, Thr | |
MW, pI | 43 kDa, 4.643 |
Gene length, protein length | 1224 bp, 408 aa |
Immediate neighbours | yslB, ask |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
Categories containing this gene/protein
biosynthesis/ acquisition of amino acids
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU28470
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + L-aspartate = ADP + 4-phospho-L-aspartate (according to Swiss-Prot)
- Protein family: aspartokinase family (according to Swiss-Prot)
- Paralogous protein(s): DapG
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 2RE1 (from Neisseria meningitidis mc58, 40% identity, 58% similarity)
- UniProt: P08495
- KEGG entry: [3]
- E.C. number: 2.7.2.4
Additional information
Expression and regulation
- Operon: lysC PubMed
- Regulation:
- Regulatory mechanism:
- Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed, also degraded upon ammonium or amino acid starvation PubMed
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Reviews
Orginal Publications