PDBsum entry 2tps

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protein ligands metals Protein-protein interface(s) links
Thiamin biosynthesis PDB id
Protein chains
226 a.a. *
TPS ×2
POP ×2
_MG ×2
Waters ×444
* Residue conservation analysis
PDB id:
Name: Thiamin biosynthesis
Title: Thiamin phosphate synthase
Structure: Protein (thiamin phosphate synthase). Chain: a, b. Ec:
Source: Bacillus subtilis. Organism_taxid: 1423. Strain: de3
Biol. unit: Monomer (from PDB file)
1.25Å     R-factor:   0.181     R-free:   0.222
Authors: H.-J.Chiu,J.J.Reddick,T.P.Begley,S.E.Ealick
Key ref: Y.Zhang et al. (1997). Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis. J Bacteriol, 179, 3030-3035. PubMed id: 9139923
09-Mar-99     Release date:   18-Mar-99    
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Protein chains
Pfam   ArchSchema ?
P39594  (THIE_BACSU) -  Thiamine-phosphate synthase
222 a.a.
226 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Thiamine-phosphate diphosphorylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: 2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5- (2-phosphono-oxyethyl)thiazole = diphosphate + thiamine phosphate
2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate
+ 4-methyl-5- (2-phosphono-oxyethyl)thiazole
Bound ligand (Het Group name = POP)
corresponds exactly
thiamine phosphate
Bound ligand (Het Group name = TPS)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     thiamine diphosphate biosynthetic process   2 terms 
  Biochemical function     catalytic activity     5 terms  


J Bacteriol 179:3030-3035 (1997)
PubMed id: 9139923  
Characterization of the Bacillus subtilis thiC operon involved in thiamine biosynthesis.
Y.Zhang, S.V.Taylor, H.J.Chiu, T.P.Begley.
The characterization of a three-gene operon (the thiC operon) at 331 min, which is involved in thiamine biosynthesis in Bacillus subtilis, is described. The first gene in the operon is homologous to transcription activators in the lysR family. The second and third genes (thiK and thiC) have been subcloned and overexpressed in Escherichia coli. ThiK (30 kDa) catalyzes the phosphorylation of 4-methyl-5-(beta-hydroxyethyl)thiazole. ThiC (27 kDa) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5-hydroxymethylpyrimidine pyrophosphate by 4-methyl-5-(beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. Transcription of the thiC operon is not regulated by thiamine or 2-methyl-4-amino-5-hydroxymethylpyrimidine and is only slightly repressed by 4-methyl-5-(beta-hydroxyethyl)thiazole.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18332905 D.Kong, Y.Zhu, H.Wu, X.Cheng, H.Liang, and H.Q.Ling (2008).
AtTHIC, a gene involved in thiamine biosynthesis in Arabidopsis thaliana.
  Cell Res, 18, 566-576.  
16497163 C.Wrenger, M.L.Eschbach, I.B.Müller, N.P.Laun, T.P.Begley, and R.D.Walter (2006).
Vitamin B1 de novo synthesis in the human malaria parasite Plasmodium falciparum depends on external provision of 4-amino-5-hydroxymethyl-2-methylpyrimidine.
  Biol Chem, 387, 41-51.  
16291685 G.Schyns, S.Potot, Y.Geng, T.M.Barbosa, A.Henriques, and J.B.Perkins (2005).
Isolation and characterization of new thiamine-deregulated mutants of Bacillus subtilis.
  J Bacteriol, 187, 8127-8136.  
16113286 I.T.Kudva, R.W.Griffin, J.M.Garren, S.B.Calderwood, and M.John (2005).
Identification of a protein subset of the anthrax spore immunome in humans immunized with the anthrax vaccine adsorbed preparation.
  Infect Immun, 73, 5685-5696.  
11717296 J.M.Lee, S.Zhang, S.Saha, S.Santa Anna, C.Jiang, and J.Perkins (2001).
RNA expression analysis using an antisense Bacillus subtilis genome array.
  J Bacteriol, 183, 7371-7380.  
10891066 N.Campobasso, I.I.Mathews, T.P.Begley, and S.E.Ealick (2000).
Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from Bacillus subtilis at 1.5 A resolution.
  Biochemistry, 39, 7868-7877.
PDB codes: 1c3q 1ekk 1ekq 1esj 1esq
  9515933 J.Blanco, J.J.Coque, and J.F.Martin (1998).
The folate branch of the methionine biosynthesis pathway in Streptomyces lividans: disruption of the 5,10-methylenetetrahydrofolate reductase gene leads to methionine auxotrophy.
  J Bacteriol, 180, 1586-1591.  
  9244280 L.A.Petersen, and D.M.Downs (1997).
Identification and characterization of an operon in Salmonella typhimurium involved in thiamine biosynthesis.
  J Bacteriol, 179, 4894-4900.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.