Difference between revisions of "PurL"

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(Extended information on the protein)
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:''' [[PurS]]-[[PurQ]]-[[PurL]] [http://www.ncbi.nlm.nih.gov/sites/entrez/15301530 PubMed]
+
* '''[[SubtInteract|Interactions]]:'''
 +
** [[PurS]]-[[PurQ]]-[[PurL]] [http://www.ncbi.nlm.nih.gov/sites/entrez/15301530 PubMed]
  
* '''Localization:''' cytoplasm (according to Swiss-Prot),  membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]
+
* '''[[Localization]]:''' cytoplasm (according to Swiss-Prot),  membrane associated [http://www.ncbi.nlm.nih.gov/pubmed/18763711 PubMed]
  
 
=== Database entries ===
 
=== Database entries ===

Revision as of 20:45, 8 December 2011

  • Description: phosphoribosylformylglycinamidine synthase

Gene name purL
Synonyms
Essential no
Product phosphoribosylformylglycinamidine synthase
Function purine biosynthesis
Interactions involving this protein in SubtInteract: PurL
Metabolic function and regulation of this protein in SubtiPathways:
Purine synthesis, Nucleotides (regulation)
MW, pI 80 kDa, 4.554
Gene length, protein length 2226 bp, 742 aa
Immediate neighbours purQ, purF
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PurL context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, membrane proteins

This gene is a member of the following regulons

G-box, PurR regulon

The gene

Basic information

  • Locus tag: BSU06480

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate (according to Swiss-Prot)
  • Protein family: FGAMS 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: 3D54 (from Thermotoga maritima, 39% identity, 58% similarity) PubMed
  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation:
    • repressed in the presence of purine nucleotides (PurR) PubMed
    • repressed in the presence of adenine or adenosine(PurR) PubMed
    • repressed in the presence of guanine(G-box) PubMed
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

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

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Aaron A Hoskins, Ruchi Anand, Steven E Ealick, JoAnne Stubbe
The formylglycinamide ribonucleotide amidotransferase complex from Bacillus subtilis: metabolite-mediated complex formation.
Biochemistry: 2004, 43(32);10314-27
[PubMed:15301530] [WorldCat.org] [DOI] (P p)

Lars Engholm Johansen, Per Nygaard, Catharina Lassen, Yvonne Agersø, Hans H Saxild
Definition of a second Bacillus subtilis pur regulon comprising the pur and xpt-pbuX operons plus pbuG, nupG (yxjA), and pbuE (ydhL).
J Bacteriol: 2003, 185(17);5200-9
[PubMed:12923093] [WorldCat.org] [DOI] (P p)

M Weng, P L Nagy, H Zalkin
Identification of the Bacillus subtilis pur operon repressor.
Proc Natl Acad Sci U S A: 1995, 92(16);7455-9
[PubMed:7638212] [WorldCat.org] [DOI] (P p)

D J Ebbole, H Zalkin
Cloning and characterization of a 12-gene cluster from Bacillus subtilis encoding nine enzymes for de novo purine nucleotide synthesis.
J Biol Chem: 1987, 262(17);8274-87
[PubMed:3036807] [WorldCat.org] (P p)