YclM

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  • 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
YclM context.gif
This image was kindly provided by SubtiList







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: inhibited by the simultaneous presence of threonine and lysine PubMed
  • Interactions:
  • Localization:

Database entries

  • Structure:
  • KEGG entry: [3]

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

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)