YqiD

• Description: Similar to an E. coli protein called IspA which is a farnasyl pyrophosphate synthase
  
  

Gene name	yqiD
Synonyms	ispA
Essential	no
Product	unknown
Function	unknown
MW, pI	29 kDa, 5.021
Gene length, protein length	816 bp, 272 aa
Immediate neighbours	dxs, yqiC
Gene sequence (+200bp)	Protein sequence
Caution: The sequence for this gene in SubtiList contains errors
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU24280

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

Additional information

Farnasyl pyrophosphate is 15 carbon compound (C15) that is an intermediate in the isoprenoid pathway. In B. subtilis there are two major isoprenoids, the synthesis of both require farnasyl pyrophosphate. The first is heptapreyl pyrophosphate (C35) which acts as a membrane anchor in menaquinone, an electron acceptor in the electron transport chain. The second is undecaprenyl pyrophosphate (C55) which is required to transport both the peptidoglycan precursor, Lipid II, and teichoic acid across the membrane.

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: dimethylallyl pyrophosphate + 2 isopentanyl pyrophosphate -> farnasyl pyrophosphate

• Protein family:

• Paralogous protein(s): HepT

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: None

• Cofactor(s): Magnesium

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure:
  • 1RQI: IspA from E. coli. Co-crystal with substrate isopentyl pyrophosphate and substrate analogue dimethyallyl S-thiolodiphosphate PubMed

• Swiss prot entry:

• KEGG entry: [2]

• E.C. number: 2.5.1.1

Expression and regulation

• Operon:

• Sigma factor:

• Regulation:

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

Your additional remarks

All information about this gene is based on its sequence similarity to the IspA protein of E. coli. There is no published data on the activity of the B. subtilis protein.