Summary: Thiamine pyrophosphate enzyme, central domain
Thiamine pyrophosphate enzyme, central domain Provide feedback
The central domain of TPP enzymes contains a 2-fold Rossman fold.
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
|Similarity to PfamA using HHSearch:||CO_dh|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR012000
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 central domain of TPP enzymes contains a 2-fold Rossman fold.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||magnesium ion binding (GO:0000287)|
|thiamine pyrophosphate binding (GO:0030976)|
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The members of this family adopt a Rossmann fold, similar to CLAN:CL0063. However, the members of this family are distinguished in that the FAD/NAD cofactor is bound in the opposite direction. In this arrangement, the adenosine moiety is found bound at the second half of the fold. In addition, the conserved GxGxxG motif found in classical NADP binding Rossmann folds is absent. Finally, another distinguishing characteristic is the formation of an internal hydrogen bond in the FAD molecule .
The clan contains the following 7 members:CO_dh DS ETF_alpha PNTB SIR2 SIR2_2 TPP_enzyme_M
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
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- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
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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|
|Number in seed:||309|
|Number in full:||15120|
|Average length of the domain:||134.60 aa|
|Average identity of full alignment:||28 %|
|Average coverage of the sequence by the domain:||23.53 %|
|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:||17|
|Download:||download the raw HMM for this family|
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There are 3 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_M domain has been found. There are 251 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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