Asd

• Description: aspartate-semialdehyde dehydrogenase
  
  

Gene name	asd
Synonyms
Essential	yes PubMed
Product	aspartate-semialdehyde dehydrogenase
Function	biosynthesis of threonine, lysine, dipicolic acid, peptidoglycan
Interactions involving this protein in SubtInteract: Asd
Metabolic function and regulation of this protein in SubtiPathways: Lys, Thr
MW, pI	37 kDa, 4.971
Gene length, protein length	1038 bp, 346 aa
Immediate neighbours	spoVFB, dapG
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, sporulation proteins, essential genes, phosphoproteins

This gene is a member of the following regulons

SigK regulon

The gene

Basic information

• Locus tag: BSU16750

Expression

Phenotypes of a mutant

essential PubMed

Database entries

• 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

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• 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

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

• Regulation:

• Regulatory mechanism:

• Additional information:

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)