Asd

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

• BsubCyc: BSU16750

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Domains:

• Modification: phosphorylation on Ser-98 AND Tyr-146 PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU16750

• Structure: 2GYY (from Streptococcus pneumoniae, 52% identity, 65% similarity) PubMed

• UniProt: Q04797

• KEGG entry: [3]

• E.C. number: 1.2.1.11

Expression and regulation

• Operon:
  • spoVFA-spoVFB-asd-dapG-dapA PubMed
  • asd-dapG-dapA PubMed

• Expression browser: asd PubMed

• Sigma factor:
  • spoVFA: SigK PubMed
  • asd: SigA PubMed

• 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:

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)