Summary: Transketolase, pyrimidine binding domain
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Transketolase, pyrimidine binding domain Provide feedback
This family includes transketolase enzymes, pyruvate dehydrogenases, and branched chain alpha-keto acid decarboxylases.
Lindqvist Y, Schneider G, Ermler U, Sundstrom M; , EMBO J 1992;11:2373-2379.: Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 A resolution. PUBMED:1628611 EPMC:1628611
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005475
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 Kd 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 (also known as formaldehyde transketolase), which exhibits a very unusual specificity by including formaldehyde amongst its substrates.
1-deoxyxylulose-5-phosphate synthase (DXP synthase) [PUBMED:9371765] is an enzyme so far found in bacteria (gene dxs) and plants (gene CLA1) which catalyzes the thiamine pyrophosphoate-dependent acyloin condensation reaction between carbon atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D- xylulose-5-phosphate (dxp), a precursor in the biosynthetic pathway to isoprenoids, thiamine (vitamin B1), and pyridoxol (vitamin B6). DXP synthase is evolutionary related to TK. The N-terminal section, contains a histidine residue which appears to function in proton transfer during catalysis [PUBMED:1628611]. In the central section there are conserved acidic residues that are part of the active cleft and may participate in substrate-binding [PUBMED:1628611]. This family includes transketolase enzymes EC and also partially matches to 2-oxoisovalerate dehydrogenase beta subunit SWISSPROT EC. Both these enzymes utilise thiamine pyrophosphate as a cofactor, suggesting there may be common aspects in their mechanism of catalysis.
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This clan includes pyruvate dehydrogenases, branched chain alpha-keto acid decarboxylases, phosphoketolases and the pyrimidine binding region of transketolases.
The clan contains the following 9 members:DXP_synthase_N E1_dh POR_N TPP_enzyme_C TPP_enzyme_N Transket_pyr Transketolase_N XFP XFP_N
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Curation and family details
|Previous IDs:||transketolaseD2; transket_pyr;|
|Author:||Bateman A, Finn RD, Griffiths-Jones SR|
|Number in seed:||93|
|Number in full:||20295|
|Average length of the domain:||175.70 aa|
|Average identity of full alignment:||23 %|
|Average coverage of the sequence by the domain:||29.45 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||19|
|Download:||download the raw HMM for this family|
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There are 4 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Transket_pyr domain has been found. There are 173 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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