Difference between revisions of "Asd"

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** number of protein molecules per cell (minimal medium with glucose and ammonium): 5224 {{PubMed|24696501}}
 
** number of protein molecules per cell (minimal medium with glucose and ammonium): 5224 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 8453 {{PubMed|24696501}}
 
** number of protein molecules per cell (complex medium with amino acids, without glucose): 8453 {{PubMed|24696501}}
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 932 {{PubMed|21395229}}
 +
 +
** number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3982 {{PubMed|21395229}}
  
 
=Biological materials =
 
=Biological materials =
 
 
* '''Mutant:'''
 
* '''Mutant:'''
  

Revision as of 13:32, 17 April 2014

  • Description: aspartate-semialdehyde dehydrogenase

Gene name asd
Synonyms
Essential yes PubMed
Product aspartate-semialdehyde dehydrogenase
Function biosynthesis of threonine, lysine, dipicolic acid, peptidoglycan
Gene expression levels in SubtiExpress: asd
Interactions involving this protein in SubtInteract: Asd
Metabolic function and regulation of this protein in SubtiPathways:
asd
MW, pI 37 kDa, 4.971
Gene length, protein length 1038 bp, 346 aa
Immediate neighbours spoVFB, dapG
Sequences Protein DNA DNA_with_flanks
Genetic context
Asd context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Asd expression.png















Categories containing this gene/protein

cell wall synthesis, biosynthesis/ acquisition of amino acids, Biosynthesis of cell wall components, sporulation proteins, essential genes, phosphoproteins

This gene is a member of the following regulons

SigK regulon

The gene

Basic information

  • Locus tag: BSU16750

Phenotypes of a mutant

essential PubMed

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-aspartate 4-semialdehyde + phosphate + NADP+ = L-4-aspartyl phosphate + NADPH (according to Swiss-Prot)
  • Protein family: aspartate-semialdehyde dehydrogenase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification: phosphorylation on Ser-98 AND Tyr-146 PubMed
  • Effectors of protein activity:

Database entries

  • Structure: 2GYY (from Streptococcus pneumoniae, 52% identity, 65% similarity) PubMed
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 5224 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 8453 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 932 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3982 PubMed

Biological materials

  • Mutant:
  • 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)

Leif Steil, Mónica Serrano, Adriano O Henriques, Uwe Völker
Genome-wide analysis of temporally regulated and compartment-specific gene expression in sporulating cells of Bacillus subtilis.
Microbiology (Reading): 2005, 151(Pt 2);399-420
[PubMed:15699190] [WorldCat.org] [DOI] (P p)

R A Daniel, J Errington
Cloning, DNA sequence, functional analysis and transcriptional regulation of the genes encoding dipicolinic acid synthetase required for sporulation in Bacillus subtilis.
J Mol Biol: 1993, 232(2);468-83
[PubMed:8345520] [WorldCat.org] [DOI] (P p)

N Y Chen, S Q Jiang, D A Klein, H Paulus
Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase.
J Biol Chem: 1993, 268(13);9448-65
[PubMed:8098035] [WorldCat.org] (P p)