Trehalose-phosphatase Provide feedback
This family consist of trehalose-phosphatases EC:188.8.131.52 these enzyme catalyse the de-phosphorylation of trehalose-6-phosphate to trehalose and orthophosphate. The aligned region is present in trehalose-phosphatases and comprises the entire length of the protein it is also found in the C-terminus of trehalose-6-phosphate synthase EC:184.108.40.206 adjacent to the trehalose-6-phosphate synthase domain - PF00982. It would appear that the two equivalent genes in the E. coli otsBA operon  otsA the trehalose-6-phosphate synthase and otsB trehalose-phosphatase (this family) have undergone gene fusion in most eukaryotes e.g. P31688 and P93653. Trehalose is a common disaccharide of bacteria, fungi and invertebrates that appears to play a major role in desiccation tolerance .
Vogel G, Aeschbacher RA, Muller J, Boller T, Wiemken A; , Plant J 1998;13:673-683.: Trehalose-6-phosphate phosphatases from Arabidopsis thaliana: identification by functional complementation of the yeast tps2 mutant. PUBMED:9681009 EPMC:9681009
Kaasen I, McDougall J, Strom AR; , Gene 1994;145:9-15.: Analysis of the otsBA operon for osmoregulatory trehalose synthesis in Escherichia coli and homology of the OtsA and OtsB proteins to the yeast trehalose-6-phosphate synthase/phosphatase complex. PUBMED:8045430 EPMC:8045430
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This tab holds annotation information from the InterPro database.
InterPro entry IPR003337Trehalose-phosphatases EC catalyse the de-phosphorylation of trehalose-6-phosphate to trehalose and orthophosphate. Trehalose is a common disaccharide of bacteria, fungi and invertebrates that appears to play a major role in desiccation tolerance. A pathway for trehalose biosynthesis may also exist in plants [PUBMED:9681009]. The trehalose-phosphatase signature is found in the C terminus of trehalose-6-phosphate synthase EC adjacent to the trehalose-6-phosphate synthase domain (see INTERPRO). It would appear that the two equivalent genes in the Escherichia coli otsBA operon: otsA, the trehalose-6-phosphate synthase and otsB, trehalose-phosphatase (this family) have undergone gene fusion in most eukaryotes [PUBMED:8045430].
|Molecular function||catalytic activity (GO:0003824)|
|Biological process||trehalose biosynthetic process (GO:0005992)|
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This clan represents the haloacid dehalogenase (HAD) superfamily that includes a diverse range of enzymes that use an asp carboxylate as a nucleophile .
The clan contains the following 21 members:5_nucleotid Acid_phosphat_B Acid_PPase DUF705 HAD HAD_2 Hydrolase Hydrolase_3 Hydrolase_6 Hydrolase_like Hydrolase_like2 LNS2 NIF NT5C PGP_phosphatase PMM PNK3P Put_Phosphatase S6PP Trehalose_PPase UMPH-1
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_762 (release 5.2)|
|Author:||Bashton M, Bateman A|
|Number in seed:||24|
|Number in full:||2499|
|Average length of the domain:||215.20 aa|
|Average identity of full alignment:||27 %|
|Average coverage of the sequence by the domain:||42.78 %|
|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:||11|
|Download:||download the raw HMM for this family|
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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 Trehalose_PPase domain has been found. There are 1 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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