YhfR

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  • Description: phosphatase involved in isopentenol (isoprenoid) biosynthesis

Gene name yhfR
Synonyms
Essential no
Product unknown
Function isoprenoid biosynthesis
Gene expression levels in SubtiExpress: yhfR
MW, pI 21 kDa, 5.164
Gene length, protein length 579 bp, 193 aa
Immediate neighbours yhfQ, yhfS
Sequences Protein DNA DNA_with_flanks
Genetic context
YhfR context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
YhfR expression.png

Contents
























Categories containing this gene/protein

biosynthesis of lipids

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU10340

Phenotypes of a mutant

no detectable phenotype PubMed

Database entries

  • DBTBS entry: no entry
  • SubtiList entry: [1]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: phosphatase involved in isopentenol (isoprenoid) biosynthesis
  • Protein family: GpmB subfamily (according to Swiss-Prot) similar to 2,3-diphosphoglycerate-dependent phosphoglycerate mutases PubMed
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure: 1H2F (enzyme of B. stearothermophilus) PubMed
  • KEGG entry: [2]
  • E.C. number:

Additional information

The gene is annotated in KEGG as an ortholog of phosphoglycerate mutase (PGM) EC 5.4.2.1. In MetaCyc the protein is marked as “similar to phosphoglycerate mutase”. No EC annotation is available in Swiss-Prot. Pearson et al. (PubMed) demonstrated that yhfR is non-essential for growth, sporulation, and spore germination. They also purified the gene, expressed it in B. subtilis but were not able to detect PGM activity in B. subtilis. PubMed

Expression and regulation

  • Operon:
  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information: weakly expressed PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 241 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1151 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 5135 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 4177 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 3220 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Tzu-Lin Hsiao, Olga Revelles, Lifeng Chen, Uwe Sauer, Dennis Vitkup
Automatic policing of biochemical annotations using genomic correlations.
Nat. Chem. Biol.: 2010, 6(1);34-40
[PubMed:19935659] [WorldCat.org] [DOI] (I p)

Sydnor T Withers, Shayin S Gottlieb, Bonny Lieu, Jack D Newman, Jay D Keasling
Identification of isopentenol biosynthetic genes from Bacillus subtilis by a screening method based on isoprenoid precursor toxicity.
Appl. Environ. Microbiol.: 2007, 73(19);6277-83
[PubMed:17693564] [WorldCat.org] [DOI] (P p)

Daniel J Rigden, Luciane V Mello, Peter Setlow, Mark J Jedrzejas
Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity.
J. Mol. Biol.: 2002, 315(5);1129-43
[PubMed:11827481] [WorldCat.org] [DOI] (P p)

D J Rigden, I Bagyan, E Lamani, P Setlow, M J Jedrzejas
A cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus is actually a broad specificity phosphatase.
Protein Sci.: 2001, 10(9);1835-46
[PubMed:11514674] [WorldCat.org] [DOI] (P p)

C L Pearson, C A Loshon, L B Pedersen, B Setlow, P Setlow
Analysis of the function of a putative 2,3-diphosphoglyceric acid-dependent phosphoglycerate mutase from Bacillus subtilis.
J. Bacteriol.: 2000, 182(14);4121-3
[PubMed:10869096] [WorldCat.org] (P p)

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