Difference between revisions of "PyrK"

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Revision as of 13:18, 16 May 2013

  • Description: dihydroorotic acid dehydrogenase (electron transfer subunit)

Gene name pyrK
Synonyms pyrDII, ylxD
Essential no
Product dihydroorotic acid dehydrogenase (electron transfer subunit)
Function pyrimidine biosynthesis
Gene expression levels in SubtiExpress: pyrK
Metabolic function and regulation of this protein in SubtiPathways:
Pyrimidines, Nucleotides (regulation)
MW, pI 27 kDa, 5.582
Gene length, protein length 768 bp, 256 aa
Immediate neighbours pyrAB, pyrD
Sequences Protein DNA DNA_with_flanks
Genetic context
PyrK context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
PyrK expression.png




























Categories containing this gene/protein

biosynthesis/ acquisition of nucleotides

This gene is a member of the following regulons

PyrR regulon

The gene

Basic information

  • Locus tag: BSU15530

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: FAD-binding FR-type domain (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s): contains an iron-sulfur cluster
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

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:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

A E Kahler, F S Nielsen, R L Switzer
Biochemical characterization of the heteromeric Bacillus subtilis dihydroorotate dehydrogenase and its isolated subunits.
Arch Biochem Biophys: 1999, 371(2);191-201
[PubMed:10545205] [WorldCat.org] [DOI] (P p)

A E Kahler, R L Switzer
Identification of a novel gene of pyrimidine nucleotide biosynthesis, pyrDII, that is required for dihydroorotate dehydrogenase activity in Bacillus subtilis.
J Bacteriol: 1996, 178(16);5013-6
[PubMed:8759868] [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)