Difference between revisions of "Asd"

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|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of threonine, lysine, dipicolic acid, peptidoglycan  
 
|style="background:#ABCDEF;" align="center"|'''Function''' || biosynthesis of threonine, lysine, dipicolic acid, peptidoglycan  
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://cellpublisher.gobics.de/subtiexpress/ ''Subti''Express]''': [http://cellpublisher.gobics.de/subtiexpress/bsu/BSU16750 asd]
 
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/Asd Asd]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/Asd Asd]

Revision as of 09:53, 7 August 2012

  • 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:
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
Asd context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Asd expression.png




























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

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:
  • Domains:
  • Modification: phosphorylation on Ser-98 AND Tyr-146 PubMed
  • Cofactor(s):
  • 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:

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)