GuaA

• Description: GMP synthase (glutamine-hydrolysing)
  
  

Gene name	guaA
Synonyms	guaB
Essential	no
Product	GMP synthetase (glutamine-hydrolysing)
Function	biosynthesis of GMP
Gene expression levels in SubtiExpress: guaA
Metabolic function and regulation of this protein in SubtiPathways: guaA
MW, pI	57 kDa, 4.747
Gene length, protein length	1539 bp, 513 aa
Immediate neighbours	yebA, pbuG
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, most abundant proteins

The gene

Basic information

• Locus tag: BSU06360

Database entries

• BsubCyc: BSU06360

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: ATP + xanthosine 5'-phosphate + L-glutamine + H₂O = AMP + diphosphate + GMP + L-glutamate (according to Swiss-Prot)

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactors:

• Effectors of protein activity:
  • the enzyme is inhibited by guanosine tetraphosphate (stringent response) PubMed

• Interactions:

• Localization:

Database entries

• BsubCyc: BSU06360

• Structure: 2YWB (from Thermus thermophilus hb8, 45% identity, 57% similarity)

• UniProt: P29727

• KEGG entry: [3]

• E.C. number: 6.3.5.2

Expression and regulation

• Operon: guaA PubMed

• Expression browser: guaA PubMed

• Sigma factor: SigA PubMed

• Regulation:

• Regulatory mechanism:

• Additional information:
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 2612 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 12454 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 4578 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 5511 PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 7521 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Christine Eymann, Annette Dreisbach, Dirk Albrecht, Jörg Bernhardt, Dörte Becher, Sandy Gentner, Le Thi Tam, Knut Büttner, Gerrit Buurman, Christian Scharf, Simone Venz, Uwe Völker, Michael Hecker
A comprehensive proteome map of growing Bacillus subtilis cells.
Proteomics: 2004, 4(10);2849-76
[PubMed:15378759] [WorldCat.org] [DOI] (P p)

P Mäntsälä, H Zalkin
Cloning and sequence of Bacillus subtilis purA and guaA, involved in the conversion of IMP to AMP and GMP.
J Bacteriol: 1992, 174(6);1883-90
[PubMed:1312531] [WorldCat.org] [DOI] (P p)

H H Saxild, P Nygaard
Regulation of levels of purine biosynthetic enzymes in Bacillus subtilis: effects of changing purine nucleotide pools.
J Gen Microbiol: 1991, 137(10);2387-94
[PubMed:1722815] [WorldCat.org] [DOI] (P p)

T Mitani, J E Heinze, E Freese
Induction of sporulation in Bacillus subtilis by decoyinine or hadacidin.
Biochem Biophys Res Commun: 1977, 77(3);1118-25
[PubMed:409404] [WorldCat.org] [DOI] (P p)