SubtiBank SubtiBank

Categories containing this gene/protein

biosynthesis of lipids

This gene is a member of the following regulons


  • Coordinates on the chromosome (coding sequence): 1,108,736 -> 1,109,317
  • Phenotypes of a mutant

  • no detectable phenotype PubMed
  • The protein

    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)

    Kinetic information




    Effectors of protein activity


  • 1H2F (enzyme of B. stearothermophilus) PubMed
  • Localization


    Additional information

  • The gene is annotated in KEGG as an ortholog of phosphoglycerate mutase (PGM) EC 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


  • yhfU-yhfT-yhfS-yhfR PubMed
  • yhfT-yhfS-yhfR PubMed
  • yhfR PubMed
  • Sigma factor


    Regulatory mechanism

    Additional information

  • weakly expressed PubMed
  • Biological materials


    Expression vector

    lacZ fusion

    GFP fusion

    two-hybrid system

    FLAG-tag construct


    Labs working on this gene/protein


    Hsiao TL, Revelles O, Chen L, Sauer U, Vitkup D

    Automatic policing of biochemical annotations using genomic correlations

    Nat Chem Biol. 2010 Jan;6(1):34-40. doi: 10.1038/nchembio.266. Epub 2009 Nov 22. PubMed PMID: 19935659; PubMed Central PMCID: PMC2935526.
    Withers ST, Gottlieb SS, Lieu B, Newman JD, Keasling JD

    Identification of isopentenol biosynthetic genes from Bacillus subtilis by a screening method based on isoprenoid precursor toxicity

    Appl Environ Microbiol. 2007 Oct;73(19):6277-83. Epub 2007 Aug 10. PubMed PMID: 17693564; PubMed Central PMCID: PMC2075014.
    Rigden DJ, Mello LV, Setlow P, Jedrzejas MJ

    Structure and mechanism of action of a cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus with broad specificity phosphatase activity

    J Mol Biol. 2002 Feb 1;315(5):1129-43. PubMed PMID: 11827481.
    Rigden DJ, Bagyan I, Lamani E, Setlow P, Jedrzejas MJ

    A cofactor-dependent phosphoglycerate mutase homolog from Bacillus stearothermophilus is actually a broad specificity phosphatase

    Protein Sci. 2001 Sep;10(9):1835-46. PubMed PMID: 11514674; PubMed Central PMCID: PMC2253200.
    Pearson CL, Loshon CA, Pedersen LB, Setlow B, Setlow P

    Analysis of the function of a putative 2,3-diphosphoglyceric acid-dependent phosphoglycerate mutase from Bacillus subtilis

    J Bacteriol. 2000 Jul;182(14):4121-3. PubMed PMID: 10869096; PubMed Central PMCID: PMC94603.
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