PurA

• Description: adenylosuccinate synthetase
  
  

Gene name	purA
Synonyms
Essential	no
Product	adenylosuccinate synthetase
Function	purine biosynthesis
Gene expression levels in SubtiExpress: purA
Metabolic function and regulation of this protein in SubtiPathways: purA
MW, pI	47 kDa, 5.459
Gene length, protein length	1290 bp, 430 aa
Immediate neighbours	trnY-Lys, yycE
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, phosphoproteins, most abundant proteins

This gene is a member of the following regulons

PurR regulon

The gene

Basic information

• Locus tag: BSU40420

Database entries

• BsubCyc: BSU40420

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP (according to Swiss-Prot)

• Protein family: adenylosuccinate synthetase family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:
  • phosphorylated on Arg-97 PubMed

• Cofactors:

• Effectors of protein activity:

• Interactions:

• Localization:
  • cytoplasm (according to Swiss-Prot)

Database entries

• BsubCyc: BSU40420

• Structure: 1KJX (from Escherichia coli k12, 46% identity, 64% similarity) PubMed

• UniProt: P29726

• KEGG entry: [3]

• E.C. number: 6.3.4.4

Expression and regulation

• Operon: purA PubMed

• Expression browser: purA PubMed

• Sigma factor: SigA PubMed

• Regulation: expression activated by glucose (4.9 fold) (CcpA) PubMed
  • repressed in the presence of purine nucleotides (PurR) PubMed

• Regulatory mechanism:
  • PurR: transcription repression PubMed

• Additional information:
  • belongs to the 100 most abundant proteins PubMed
  • number of protein molecules per cell (minimal medium with glucose and ammonium): 1965 PubMed
  • number of protein molecules per cell (complex medium with amino acids, without glucose): 9672 PubMed

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

Haojian Li, Guoqiang Zhang, Aihua Deng, Ning Chen, Tingyi Wen
De novo engineering and metabolic flux analysis of inosine biosynthesis in Bacillus subtilis.
Biotechnol Lett: 2011, 33(8);1575-80
[PubMed:21424839] [WorldCat.org] [DOI] (I p)

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)

Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135] [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)

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)