PurF

• Description: glutamine phosphoribosyldiphosphate amidotransferase
  
  

Gene name	purF
Synonyms	purB
Essential	no
Product	glutamine phosphoribosyldiphosphate amidotransferase
Function	purine biosynthesis
Gene expression levels in SubtiExpress: purF
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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides

This gene is a member of the following regulons

G-box, PurR regulon

The gene

Basic information

• Locus tag: BSU06490

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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)

• UniProt: P00497

• KEGG entry: [3]

• E.C. number: 2.4.2.14

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon: purE-purK-purB-purC-purS-purQ-purL-purF-purM-purN-purH-purD PubMed

• Expression browser: purF PubMed

• Sigma factor: SigA PubMed

• 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

• Regulatory mechanism:
  • [PurR]]: transcription repression PubMed
  • PurR: transcription repression (molecular inducer: PRPP) PubMed
  • G-box: transcription termination/ antitermination (riboswitch) PubMed1 PubMed2

• Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

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] [DOI] (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)