Dxs

• Description: 1-deoxyxylulose-5-phosphate synthase
  
  

Gene name	dxs
Synonyms	yqiE
Essential	yes PubMed
Product	1-deoxyxylulose-5-phosphate synthase
Function	biosynthesis of thiamine
Metabolic function and regulation of this protein in SubtiPathways: Thiamin
MW, pI	69 kDa, 6.002
Gene length, protein length	1899 bp, 633 aa
Immediate neighbours	yqxC, yqiD
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

Categories containing this gene/protein

biosynthesis of cofactors, essential genes

This gene is a member of the following regulons

stringent response

The gene

Basic information

• Locus tag: BSU24270

Phenotypes of a mutant

essential PubMed

Database entries

• DBTBS entry: no entry

• SubtiList entry: [1]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Pyruvate + D-glyceraldehyde 3-phosphate = 1-deoxy-D-xylulose 5-phosphate + CO₂ (according to Swiss-Prot)

• Protein family: DXPS subfamily (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 2O1S (from E. coli, 44% identity, 62% similarity) PubMed

• UniProt: P54523

• KEGG entry: [2]

• E.C. number: 2.2.1.7

Expression and regulation

• Operon:

• Expression browser: dxs PubMed

• Sigma factor:

• Regulation:
  • RelA dependent downregulation (Class I) during stringent response PubMed

• Regulatory mechanism:

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Reviews

Christopher T Jurgenson, Tadhg P Begley, Steven E Ealick
The structural and biochemical foundations of thiamin biosynthesis.
Annu Rev Biochem: 2009, 78;569-603
[PubMed:19348578] [WorldCat.org] [DOI] (I p)

Original publications

Junfeng Xue, Birgitte K Ahring
Enhancing isoprene production by genetic modification of the 1-deoxy-d-xylulose-5-phosphate pathway in Bacillus subtilis.
Appl Environ Microbiol: 2011, 77(7);2399-405
[PubMed:21296950] [WorldCat.org] [DOI] (I p)

Song Xiang, Gerlinde Usunow, Gudrun Lange, Marco Busch, Liang Tong
Crystal structure of 1-deoxy-D-xylulose 5-phosphate synthase, a crucial enzyme for isoprenoids biosynthesis.
J Biol Chem: 2007, 282(4);2676-82
[PubMed:17135236] [WorldCat.org] [DOI] (P p)

Akihiro Sakai, Natsumi Kinoshita, Makoto Kita, Tohoru Katsuragi, Yoshiki Tani
Investigation of 1-deoxy-D-xylulose 5-phosphate synthase and transketolase of Bacillus subtilis in relation to vitamin B6 biosynthesis.
J Nutr Sci Vitaminol (Tokyo): 2003, 49(1);73-5
[PubMed:12882400] [WorldCat.org] [DOI] (P p)