Homologous Superfamily

Thiamin pyrophosphokinase, thiamin-binding domain superfamily (IPR036371)

Short name: TPK_B1-bd_sf

Description

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 [PMID: 11435118].

TPK is a homodimer, and each subunit consists of two domains. One domain resembles a Rossman fold, while the other domain forms a beta-sheet flattened sandwich structure containing a jelly-roll topology. The active site is located in a cleft at the dimer interface and is formed from residues from domains of both subunits. The thiamin binding site is primarily defined by the sandwich domain of one subunit and by a loop from the alpha-beta domain of the other subunit [PMID: 11435118]. This superfamily describes the jelly-roll sandwich domain.

GO terms

Biological Process

GO:0009229 thiamine diphosphate biosynthetic process

Molecular Function

GO:0030975 thiamine binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
SUPERFAMILY
GENE3D