Difference between revisions of "PurC"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU06450&redirect=T BSU06450]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/purEKBCSQLFMNHD.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/purEKBCSQLFMNHD.html]
Line 89: Line 90:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU06450&redirect=T BSU06450]
  
 
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KUT 1KUT] (from ''Thermotoga maritima'', 40% identity, 57% similarity) {{PubMed|16582479}}
 
* '''Structure:''' [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1KUT 1KUT] (from ''Thermotoga maritima'', 40% identity, 57% similarity) {{PubMed|16582479}}

Revision as of 13:08, 2 April 2014

  • Description: phosphoribosylaminoimidazole succinocarboxamide synthase

Gene name purC
Synonyms
Essential no
Product phosphoribosylaminoimidazole
succinocarboxamide synthase
Function purine biosynthesis
Gene expression levels in SubtiExpress: purC
Metabolic function and regulation of this protein in SubtiPathways:
purC
MW, pI 27 kDa, 4.875
Gene length, protein length 723 bp, 241 aa
Immediate neighbours purB, purS
Sequences Protein DNA DNA_with_flanks
Genetic context
PurC context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PurC expression.png















Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, most abundant proteins

This gene is a member of the following regulons

G-box, PurR regulon

The gene

Basic information

  • Locus tag: BSU06450

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate (according to Swiss-Prot)
  • Protein family: SAICAR synthetase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • Structure: 1KUT (from Thermotoga maritima, 40% identity, 57% similarity) PubMed
  • KEGG entry: [3]

Additional information

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

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

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)

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)

G Hambraeus, C von Wachenfeldt, L Hederstedt
Genome-wide survey of mRNA half-lives in Bacillus subtilis identifies extremely stable mRNAs.
Mol Genet Genomics: 2003, 269(5);706-14
[PubMed:12884008] [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)

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)