Summary: Myo-inositol-1-phosphate synthase
Myo-inositol-1-phosphate synthase Provide feedback
This is a family of myo-inositol-1-phosphate synthases. Inositol-1-phosphate catalyses the conversion of glucose-6- phosphate to inositol-1-phosphate, which is then dephosphorylated to inositol . Inositol phosphates play an important role in signal transduction.
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This tab holds annotation information from the InterPro database.
InterPro entry IPR002587
1L-myo-Inositol-1-phosphate synthase (EC) catalyzes the conversion of D-glucose 6-phosphate to 1L-myo-inositol-1-phosphate, the first committed step in the production of all inositol-containing compounds, including phospholipids, either directly or by salvage. The enzyme exists in a cytoplasmic form in a wide range of plants, animals, and fungi. It has also been detected in several bacteria and a chloroplast form is observed in alga and higher plants. Inositol phosphates play an important role in signal transduction.
In Saccharomyces cerevisiae (Baker's yeast), the transcriptional regulation of the INO1 gene has been studied in detail [PUBMED:7975896] and its expression is sensitive to the availability of phospholipid precursors as well as growth phase. The regulation of the structural gene encoding 1L-myo-inositol-1-phosphate synthase has also been analyzed at the transcriptional level in the aquatic angiosperm, Spirodela polyrrhiza (Giant duckweed) and the halophyte, Mesembryanthemum crystallinum (Common ice plant) [PUBMED:9370339].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||inositol-3-phosphate synthase activity (GO:0004512)|
|Biological process||phospholipid biosynthetic process (GO:0008654)|
|inositol biosynthetic process (GO:0006021)|
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Curation and family details
|Seed source:||Pfam-B_959 (release 4.1)|
|Author:||Bashton M, Bateman A|
|Number in seed:||37|
|Number in full:||1323|
|Average length of the domain:||337.10 aa|
|Average identity of full alignment:||33 %|
|Average coverage of the sequence by the domain:||89.86 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null --hand HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||7|
|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 NAD_binding_5 domain has been found. There are 36 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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