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: purF
MW, pI	51 kDa, 5.873
Gene length, protein length	1428 bp, 476 aa
Immediate neighbours	purL, purM
Sequences	Protein DNA DNA_with_flanks
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)