Difference between revisions of "PyrB"

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=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15490&redirect=T BSU15490]
  
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/pyrRPBCAAABKDFE.html]
 
* '''DBTBS entry:''' [http://dbtbs.hgc.jp/COG/prom/pyrRPBCAAABKDFE.html]
Line 96: Line 97:
  
 
=== Database entries ===
 
=== Database entries ===
 +
* '''BsubCyc:''' [http://bsubcyc.org/BSUB/NEW-IMAGE?type=NIL&object=BSU15490&redirect=T BSU15490]
  
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=3R7D 3R7D] {{PubMed|21663747}}
 
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=3R7D 3R7D] {{PubMed|21663747}}

Revision as of 13:40, 2 April 2014

  • Description: aspartate carbamoyltransferase

Gene name pyrB
Synonyms
Essential no
Product aspartate carbamoyltransferase
Function pyrimidine biosynthesis
Gene expression levels in SubtiExpress: pyrB
Metabolic function and regulation of this protein in SubtiPathways:
pyrB
MW, pI 34 kDa, 5.341
Gene length, protein length 912 bp, 304 aa
Immediate neighbours pyrP, pyrC
Sequences Protein DNA DNA_with_flanks
Genetic context
PyrB context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PyrB expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides, phosphoproteins

This gene is a member of the following regulons

PyrR regulon

The gene

Basic information

  • Locus tag: BSU15490

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate (according to Swiss-Prot)
  • Protein family: ATCase/OTCase family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylation on Ser-303 PubMed
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation:
    • induced in the absence of uridine nucleotides (PyrR) PubMed
  • Regulatory mechanism:
    • PyrR: RNA switch, transcription termination/ antitermination (in the presence of uridine nucleotides: termination, in their absence: antitermination) PubMed
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Katharine M Harris, Gregory M Cockrell, David E Puleo, Evan R Kantrowitz
Crystallographic snapshots of the complete catalytic cycle of the unregulated aspartate transcarbamoylase from Bacillus subtilis.
J Mol Biol: 2011, 411(1);190-200
[PubMed:21663747] [WorldCat.org] [DOI] (I p)

Birgit Hobl, Matthias Mack
The regulator protein PyrR of Bacillus subtilis specifically interacts in vivo with three untranslated regions within pyr mRNA of pyrimidine biosynthesis.
Microbiology (Reading): 2007, 153(Pt 3);693-700
[PubMed:17322189] [WorldCat.org] [DOI] (P p)

Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307] [WorldCat.org] [DOI] (P p)

Hesheng Zhang, Robert L Switzer
Transcriptional pausing in the Bacillus subtilis pyr operon in vitro: a role in transcriptional attenuation?
J Bacteriol: 2003, 185(16);4764-71
[PubMed:12896995] [WorldCat.org] [DOI] (P p)

Y Lu, R J Turner, R L Switzer
Roles of the three transcriptional attenuators of the Bacillus subtilis pyrimidine biosynthetic operon in the regulation of its expression.
J Bacteriol: 1995, 177(5);1315-25
[PubMed:7868607] [WorldCat.org] [DOI] (P p)

P Hu, R L Switzer
Evidence for substrate stabilization in regulation of the degradation of Bacillus subtilis aspartate transcarbamylase in vivo.
Arch Biochem Biophys: 1995, 316(1);260-6
[PubMed:7840626] [WorldCat.org] [DOI] (P p)

R J Turner, Y Lu, R L Switzer
Regulation of the Bacillus subtilis pyrimidine biosynthetic (pyr) gene cluster by an autogenous transcriptional attenuation mechanism.
J Bacteriol: 1994, 176(12);3708-22
[PubMed:8206849] [WorldCat.org] [DOI] (P p)

C L Quinn, B T Stephenson, R L Switzer
Functional organization and nucleotide sequence of the Bacillus subtilis pyrimidine biosynthetic operon.
J Biol Chem: 1991, 266(14);9113-27
[PubMed:1709162] [WorldCat.org] (P p)

C G Lerner, R L Switzer
Cloning and structure of the Bacillus subtilis aspartate transcarbamylase gene (pyrB).
J Biol Chem: 1986, 261(24);11156-65
[PubMed:3015959] [WorldCat.org] (P p)

J S Brabson, M R Maurizi, R L Switzer
Aspartate transcarbamylase from Bacillus subtilis.
Methods Enzymol: 1985, 113;627-35
[PubMed:3937019] [WorldCat.org] [DOI] (P p)

R W Bond, R L Switzer
Degradation of aspartate transcarbamylase in Bacillus subtilis is deficient in rel mutants but is not mediated by guanosine polyphosphates.
J Bacteriol: 1984, 158(2);746-8
[PubMed:6427186] [WorldCat.org] [DOI] (P p)