ThiD

• Description: 4-amino-5-hydroxymethyl-2-methylpyrimidine and 4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate kinase
  
  

Gene name	thiD
Synonyms	yjbV
Essential	no
Product	4-amino-5-hydroxymethyl-2-methylpyrimidine pyrophosphate kinase
Function	biosynthesis of thiamine pyrophosphate (TPP)
Gene expression levels in SubtiExpress: thiD
Metabolic function and regulation of this protein in SubtiPathways: thiD
MW, pI	28 kDa, 5.709
Gene length, protein length	813 bp, 271 aa
Immediate neighbours	thiF, fabI
Gene sequence (+200bp)	Protein sequence
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

biosynthesis of cofactors

This gene is a member of the following regulons

Thi-box

The gene

Basic information

• Locus tag: BSU11710

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity:

• Protein family:

• Paralogous protein(s): PdxK

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization:

Database entries

• Structure: 2I5B PubMed

• UniProt: O31620

• KEGG entry: [3]

• E.C. number: 2.7.1.49, 2.7.4.7

Expression and regulation

• Operon: tenA-tenI-thiO-thiS-thiG-thiF-thiD PubMed

• Expression browser: thiD PubMed

• Sigma factor:

• Regulation:
  • repressed by thiamine (Thi-box) PubMed

• Regulatory mechanism:
  • Thi-box: RNA switch PubMed

• 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)

T P Begley, D M Downs, S E Ealick, F W McLafferty, A P Van Loon, S Taylor, N Campobasso, H J Chiu, C Kinsland, J J Reddick, J Xi
Thiamin biosynthesis in prokaryotes.
Arch Microbiol: 1999, 171(5);293-300
[PubMed:10382260] [WorldCat.org] [DOI] (P p)

Original publications

Joseph A Newman, Sanjan K Das, Svetlana E Sedelnikova, David W Rice
The crystal structure of an ADP complex of Bacillus subtilis pyridoxal kinase provides evidence for the parallel emergence of enzyme activity during evolution.
J Mol Biol: 2006, 363(2);520-30
[PubMed:16978644] [WorldCat.org] [DOI] (P p)

Joo-Heon Park, Kristin Burns, Cynthia Kinsland, Tadhg P Begley
Characterization of two kinases involved in thiamine pyrophosphate and pyridoxal phosphate biosynthesis in Bacillus subtilis: 4-amino-5-hydroxymethyl-2methylpyrimidine kinase and pyridoxal kinase.
J Bacteriol: 2004, 186(5);1571-3
[PubMed:14973012] [WorldCat.org] [DOI] (P p)