Schultz et al. (1998) Proc. Natl. Acad. Sci. USA 95, 5857-5864
Letunic et al. (2012) Nucleic Acids Res , doi:10.1093/nar/gkr931

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TPK_B1_binding Thiamin pyrophosphokinase, vitamin B1 binding domain

SMART accession number:	SM00983
Description:	Thiamin pyrophosphokinase (TPK) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis (PUBMED:11435118).
Interpro abstract (IPR007373):	Thiamin pyrophosphokinase (TPK, EC 2.7.6.2) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis [(PUBMED:11435118)].
GO process:	thiamine diphosphate biosynthetic process (GO:0009229)
GO function:	thiamine diphosphokinase activity (GO:0004788)
Family alignment:	View or CHROMA formatCLUSTALW formatMSF formatFASTA formatPIR format

There are 725 TPK_B1_binding domains in 725 proteins in SMART's nrdb database.

Click on the following links for more information.

• Evolution (species in which this domain is found)

• Click on to expand nodes. To display all proteins with a TPK_B1_binding domain in a specific node, click on it.

  This tree shows only several representative species. The complete taxonomic breakdown of all proteins with TPK_B1_binding domain is also avaliable.

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  Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes

• Cellular role (predicted cellular role)

• Cellular role: metabolism
  

• Structure (3D structures containing this domain)

• 3D Structures of TPK_B1_binding domains in PDB

  PDB code	Main view	Title
  1ig0		Crystal structure of yeast thiamin pyrophosphokinase
  1ig3		Mouse thiamin pyrophosphokinase complexed with thiamin
  2f17		Mouse thiamin pyrophosphokinase in a ternary complex with pyrithiamin pyrophosphate and amp at 2.5 angstrom
  2g9z		Thiamin pyrophosphokinase from candida albicans
  2hh9		Thiamin pyrophosphokinase from candida albicans
  3cq9		Crystal structure of the lp_1622 protein from lactobacillus plantarum. northeast structural genomics consortium target lpr114
  3ihk		Crystal structure of thiamin pyrophosphokinase from s.mutans, northeast structural genomics consortium target smr83

• Links (links to other resources describing this domain)

• PFAM	TPK_B1_binding
  INTERPRO	IPR007373

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