YclM

• Description: aspartokinase III
  
  

Gene name	yclM
Synonyms
Essential	no
Product	aspartokinase III
Function	unknown
Gene expression levels in SubtiExpress: yclM
Metabolic function and regulation of this protein in SubtiPathways: yclM
MW, pI	49 kDa, 4.783
Gene length, protein length	1362 bp, 454 aa
Immediate neighbours	yczN, yclN
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids

The gene

Basic information

• Locus tag: BSU03790

Database entries

• BsubCyc: BSU03790

• DBTBS entry: [1]

• SubtiList entry: [2]

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: inhibited by the simultaneous presence of threonine and lysine PubMed

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU03790

• Structure:

• UniProt: P94417

• KEGG entry: [3]

• E.C. number: 2.7.2.4

Expression and regulation

• Operon: yclM (according to DBTBS)

• Expression browser: yclM PubMed

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 78 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Chien-Chi Lo, Carol A Bonner, Gary Xie, Mark D'Souza, Roy A Jensen
Cohesion group approach for evolutionary analysis of aspartokinase, an enzyme that feeds a branched network of many biochemical pathways.
Microbiol Mol Biol Rev: 2009, 73(4);594-651
[PubMed:19946135] [WorldCat.org] [DOI] (I p)

Original publications

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)