Difference between revisions of "PurF"

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=The gene=
 
=The gene=

Revision as of 08:52, 23 June 2009

  • Description: glutamine phosphoribosyldiphosphate amidotransferase

Gene name purF
Synonyms purB
Essential no
Product glutamine phosphoribosyldiphosphate amidotransferase
Function purine biosynthesis
Metabolic function and regulation of this protein in SubtiPathways:
Purine synthesis, Nucleotides (regulation)
MW, pI 51 kDa, 5.873
Gene length, protein length 1428 bp, 476 aa
Immediate neighbours purL, purM
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
PurF context.gif
This image was kindly provided by SubtiList







The gene

Basic information

  • Locus tag: BSU06490

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: 5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate + H2O (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

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

Database entries

  • Structure: 1GPH, 1AO0 (complex with ADP and GMP)
  • 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

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)

J L Smith, E J Zaluzec, J P Wery, L Niu, R L Switzer, H Zalkin, Y Satow
Structure of the allosteric regulatory enzyme of purine biosynthesis.
Science: 1994, 264(5164);1427-33
[PubMed:8197456] [WorldCat.org] [DOI] (P p)

Y A Oñate, S J Vollmer, R L Switzer, M K Johnson
Spectroscopic characterization of the iron-sulfur cluster in Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase.
J. Biol. Chem.: 1989, 264(31);18386-91
[PubMed:2553706] [WorldCat.org] (P p)

J A Grandoni, R L Switzer, C A Makaroff, H Zalkin
Evidence that the iron-sulfur cluster of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase determines stability of the enzyme to degradation in vivo.
J. Biol. Chem.: 1989, 264(11);6058-64
[PubMed:2495277] [WorldCat.org] (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)

S J Vollmer, R L Switzer, P G Debrunner
Oxidation-reduction properties of the iron-sulfur cluster in Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase.
J. Biol. Chem.: 1983, 258(23);14284-93
[PubMed:6315725] [WorldCat.org] (P p)

C A Makaroff, H Zalkin, R L Switzer, S J Vollmer
Cloning of the Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase gene in Escherichia coli. Nucleotide sequence determination and properties of the plasmid-encoded enzyme.
J. Biol. Chem.: 1983, 258(17);10586-93
[PubMed:6411717] [WorldCat.org] (P p)

S J Vollmer, R L Switzer, M A Hermodson, S G Bower, H Zalkin
The glutamine-utilizing site of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase.
J. Biol. Chem.: 1983, 258(17);10582-5
[PubMed:6411716] [WorldCat.org] (P p)

D A Bernlohr, R L Switzer
Regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase inactivation in vivo.
J. Bacteriol.: 1983, 153(2);937-49
[PubMed:6401710] [WorldCat.org] (P p)

R L Switzer, M E Ruppen, D A Bernlohr
Inactivation of glutamine: 5-phosphoribosyl 1-pyrophosphate amidotransferase in Bacillus subtilis: oxidation of an essential Fe-S centre precedes selective degradation.
Biochem. Soc. Trans.: 1982, 10(5);322-4
[PubMed:6814966] [WorldCat.org] [DOI] (P p)

D A Bernlohr, R L Switzer
Reaction of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase with oxygen: chemistry and regulation by ligands.
Biochemistry: 1981, 20(20);5675-81
[PubMed:6794614] [WorldCat.org] [DOI] (P p)

J Y Wong, D A Bernlohr, C L Turnbough, R L Switzer
Purification and properties of glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis.
Biochemistry: 1981, 20(20);5669-74
[PubMed:6794613] [WorldCat.org] [DOI] (P p)

B A Averill, A Dwivedi, P Debrunner, S J Vollmer, J Y Wong, R L Switzer
Evidence for a tetranuclear iron-sulfur center in glutamine phosphoribosylpyrophosphate amidotransferase from Bacillus subtilis.
J. Biol. Chem.: 1980, 255(13);6007-10
[PubMed:6771260] [WorldCat.org] (P p)

E Meyer, R L Switzer
Regulation of Bacillus subtilis glutamine phosphoribosylpyrophosphate amidotransferase activity by end products.
J. Biol. Chem.: 1979, 254(12);5397-402
[PubMed:109433] [WorldCat.org] (P p)