The domain within your query sequence starts at position 226 and ends at position 349; the E-value for the Transketolase_C domain shown below is 2.4e-40.

GKAKIERQGTHITVVAHSRPVGHCLEAAAVLSKEGIECEVINLRTIRPMDIEAIEASVMK
TNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKVLEDNSVPQ
VKDI

Transketolase_C

Transketolase_C
PFAM accession number:PF02780
Interpro abstract (IPR033248):

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

Transketolase EC 2.2.1.1 (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 [(PUBMED:1567394), (PUBMED: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 2.2.1.3 (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Transketolase_C