Difference between revisions of "YclM"
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=Expression and regulation= | =Expression and regulation= | ||
| − | * '''Operon:''' | + | * '''Operon:''' ''yclM'' (according to [http://dbtbs.hgc.jp/COG/prom/yclM.html DBTBS]) |
* '''[[Sigma factor]]:''' | * '''[[Sigma factor]]:''' | ||
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* '''Regulatory mechanism:''' | * '''Regulatory mechanism:''' | ||
| − | * '''Additional information:''' | + | * '''Additional information:''' |
=Biological materials = | =Biological materials = | ||
Revision as of 19:21, 19 August 2009
- Description: aspartokinase III
| Gene name | yclM |
| Synonyms | |
| Essential | no |
| Product | aspartokinase III |
| Function | unknown |
| Metabolic function and regulation of this protein in SubtiPathways: Lys, Thr | |
| MW, pI | 49 kDa, 4.783 |
| Gene length, protein length | 1362 bp, 454 aa |
| Immediate neighbours | phrC, yclN |
| 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: BSU03790
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):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- UniProt: P94417
- KEGG entry: [3]
- E.C. number: 2.7.2.4
Additional information
Expression and regulation
- Operon: yclM (according to DBTBS)
- Regulation:
- Regulatory mechanism:
- 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
N Kobashi, M Nishiyama, H Yamane
Characterization of aspartate kinase III of Bacillus subtilis.
Biosci Biotechnol Biochem: 2001, 65(6);1391-4
[PubMed:11471740]
[WorldCat.org]
[DOI]
(P p)
L M Graves, R L Switzer
Aspartokinase III, a new isozyme in Bacillus subtilis 168.
J Bacteriol: 1990, 172(1);218-23
[PubMed:2152900]
[WorldCat.org]
[DOI]
(P p)
