Transketolase, C-terminal domain (IPR033248)

Short name: Transketolase_C

Overlapping homologous superfamilies

Domain relationships



The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site [PMID: 8176731, PMID: 1628611].

Transketolase EC: (TK) catalyzes the reversible transfer of a two-carbon ketol unit from xylulose 5-phosphate to an aldose receptor, such as ribose 5-phosphate, to form sedoheptulose 7-phosphate and glyceraldehyde 3- phosphate. This enzyme, together with transaldolase, provides a link between the glycolytic and pentose-phosphate pathways. TK requires thiamine pyrophosphate as a cofactor. In most sources where TK has been purified, it is a homodimer of approximately 70 kDa subunits. TK sequences from a variety of eukaryotic and prokaryotic sources [PMID: 1567394, PMID: 1737042] show that the enzyme has been evolutionarily conserved. In the peroxisomes of methylotrophic yeast Pichia angusta (Yeast) (Hansenula polymorpha), there is a highly related enzyme, dihydroxy-acetone synthase (DHAS) EC: (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.

Contributing signatures

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