YhfR

• Description: phosphatase involved in isopentenol (isoprenoid) biosynthesis
  
  

Gene name	yhfR
Synonyms
Essential	no
Product	unknown
Function	isoprenoid biosynthesis
MW, pI	21 kDa, 5.164
Gene length, protein length	579 bp, 193 aa
Immediate neighbours	yhfQ, yhfS
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU10340

Phenotypes of a mutant

no detectable phenotype PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

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:

• Interactions:

• Localization:

Database entries

• Structure: 1H2F (enzyme of B. stearothermophilus) PubMed

• UniProt: O07617

• 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 ininB. 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

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

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)

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] [DOI] (P p)