Summary: Thiamine pyrophosphate enzyme, C-terminal TPP binding domain
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Thiamine pyrophosphate enzyme, C-terminal TPP binding domain Provide feedback
No Pfam abstract.
Arjunan P, Umland T, Dyda F, Swaminathan S, Furey W, Sax M, Farrenkopf B, Gao Y, Zhang D, Jordan F; , J Mol Biol 1996;256:590-600.: Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 A resolution. PUBMED:8604141 EPMC:8604141
Internal database links
|SCOOP:||TPP_enzyme_N XFP_N DXP_synthase_N|
|Similarity to PfamA using HHSearch:||Transketolase_N E1_dh DXP_synthase_N|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR011766
A number of enzymes require thiamine pyrophosphate (TPP) (vitamin B1) as a cofactor. It has been shown [PUBMED:8604141] that some of these enzymes are structurally related. This represents the C-terminal TPP binding domain of TPP enzymes.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||catalytic activity (GO:0003824)|
|thiamine pyrophosphate binding (GO:0030976)|
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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
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the UniProtKB sequence database using the family HMM
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- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Author:||Finn RD, Griffiths-Jones SR, Mistry J|
|Number in seed:||323|
|Number in full:||9445|
|Average length of the domain:||148.00 aa|
|Average identity of full alignment:||21 %|
|Average coverage of the sequence by the domain:||24.99 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||18|
|Download:||download the raw HMM for this family|
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There are 9 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 TPP_enzyme_C domain has been found. There are 360 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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