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Transketolase-like TK C-terminal domain
transketolase C-terminal domain-containing protein
The C-terminal domain of transketolase has been proposed as a regulatory molecule binding site [2]. [1]. 8176731. Refined structure of transketolase from Saccharomyces cerevisiae. at 2.0 A resolution.. Nikkola M, Lindqvist Y, Schneider G;. J Mol Biol 1994;238:387-404.. [2]. 1628611. Three-dimensional structure of transketolase, a thiamine. diphosphate dependent enzyme, at 2.5 A resolution.. Lindqvist Y, Schneider G, Ermler U, Sundstrom M;. EMBO J 1992;11:2373-2379. (from Pfam)
Transketolase, pyrimidine binding domain
This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases. [1]. 8176731. Refined structure of transketolase from Saccharomyces cerevisiae. at 2.0 A resolution.. Nikkola M, Lindqvist Y, Schneider G;. J Mol Biol 1994;238:387-404.. [2]. 1628611. Three-dimensional structure of transketolase, a thiamine. diphosphate dependent enzyme, at 2.5 A resolution.. Lindqvist Y, Schneider G, Ermler U, Sundstrom M;. EMBO J 1992;11:2373-2379. (from Pfam)
thiamine pyrophosphate-dependent enzyme
This family uses thiamine pyrophosphate as a cofactor. This family includes pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase and 2-oxoisovalerate dehydrogenase. (from Pfam)
Transketolase, thiamine diphosphate binding domain
This family includes transketolase enzymes EC:2.2.1.1. and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit Swiss:P37941 EC:1.2.4.4. Both these enzymes utilise thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis. [1]. 8176731. Refined structure of transketolase from Saccharomyces cerevisiae. at 2.0 A resolution.. Nikkola M, Lindqvist Y, Schneider G;. J Mol Biol 1994;238:387-404.. [2]. 1628611. Three-dimensional structure of transketolase, a thiamine. diphosphate dependent enzyme, at 2.5 A resolution.. Lindqvist Y, Schneider G, Ermler U, Sundstrom M;. EMBO J 1992;11:2373-2379. (from Pfam)
transketolase family protein
transketolase family protein such as transketolase, which catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate
transketolase
This HMM is designed to capture orthologs of bacterial transketolases. The group includes two from the yeast Saccharomyces cerevisiae but excludes dihydroxyactetone synthases (formaldehyde transketolases) from various yeasts and the even more distant mammalian transketolases. Among the family of thiamine diphosphate-dependent enzymes that includes transketolases, dihydroxyacetone synthases, pyruvate dehydrogenase E1-beta subunits, and deoxyxylulose-5-phosphate synthases, mammalian and bacterial transketolases seem not to be orthologous.
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