Difference between revisions of "ProA"

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Revision as of 13:04, 16 May 2013

  • Description: glutamate-5-semialdehyde dehydrogenase, required for normal and osmoadaptive proline biosynthesis

Gene name proA
Synonyms
Essential no
Product glutamate-5-semialdehyde dehydrogenase
Function biosynthesis of proline
Gene expression levels in SubtiExpress: proA
Metabolic function and regulation of this protein in SubtiPathways:
Pro, Stress
MW, pI 45 kDa, 5.098
Gene length, protein length 1245 bp, 415 aa
Immediate neighbours proB, ohrA
Sequences Protein DNA DNA_with_flanks
Genetic context
ProA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
ProA expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of amino acids, coping with hyper-osmotic stress

This gene is a member of the following regulons

T-box

The gene

Basic information

  • Locus tag: BSU13130

Phenotypes of a mutant

  • auxotrophic for proline PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH (according to Swiss-Prot)
  • Protein family: gamma-glutamyl phosphate reductase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1O20 (from Thermotoga maritima, 46% identity, 67% similarity) PubMed
  • KEGG entry: [2]

Additional information

Expression and regulation

  • Regulation:
  • 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

Additional publications: PubMed

Vivianne J Goosens, Ruben A T Mars, Michiel Akeroyd, Andre Vente, Annette Dreisbach, Emma L Denham, Thijs R H M Kouwen, Tjeerd van Rij, Maurien Olsthoorn, Jan Maarten van Dijl
Is proteomics a reliable tool to probe the oxidative folding of bacterial membrane proteins?
Antioxid Redox Signal: 2013, 18(10);1159-64
[PubMed:22540663] [WorldCat.org] [DOI] (I p)

Jeanette Brill, Tamara Hoffmann, Harald Putzer, Erhard Bremer
T-box-mediated control of the anabolic proline biosynthetic genes of Bacillus subtilis.
Microbiology (Reading): 2011, 157(Pt 4);977-987
[PubMed:21233158] [WorldCat.org] [DOI] (I p)

Ana Gutiérrez-Preciado, Tina M Henkin, Frank J Grundy, Charles Yanofsky, Enrique Merino
Biochemical features and functional implications of the RNA-based T-box regulatory mechanism.
Microbiol Mol Biol Rev: 2009, 73(1);36-61
[PubMed:19258532] [WorldCat.org] [DOI] (I p)