YqiD
- Description: Similar to an E. coli protein called IspA which is a farnasyl pyrophosphate synthase
| Gene name | yqiD |
| Synonyms | |
| 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 
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Contents
The gene
Basic information
- Locus tag: BSU24280
Phenotypes of a mutant
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
Additional information
Expression and regulation
- Operon:
- Sigma factor:
- Regulation:
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
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.
References
David J Hosfield, Yanming Zhang, Douglas R Dougan, Alexei Broun, Leslie W Tari, Ronald V Swanson, John Finn
Structural basis for bisphosphonate-mediated inhibition of isoprenoid biosynthesis.
J Biol Chem: 2004, 279(10);8526-9
[PubMed:14672944]
[WorldCat.org]
[DOI]
(P p)
- Hosfield DJ, Zhang Y, Dougan DR, Broun A, Tari LW, Swanson RV & Finn J (2004) Structural basis for bisphosphonate-mediated inhibition of isoprenoid biosynthesis Journal of Biological Chemistry 279(10): 8526-9 PubMed
