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164  structures 7594  species 0  interactions 27556  sequences 179  architectures

Family: Inositol_P (PF00459)

Summary: Inositol monophosphatase family

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Inositol monophosphatase family Provide feedback

No Pfam abstract.

Literature references

  1. York JD, Ponder JW, Chen ZW, Mathews FS, Majerus PW; , Biochemistry 1994;33:13164-13171.: Crystal structure of inositol polyphosphate 1-phosphatase at 2.3-A resolution. PUBMED:7947723 EPMC:7947723

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR000760

It has been shown that several proteins share two sequence motifs [ PUBMED:1660408 ]. Two of these proteins, vertebrate and plant inositol monophosphatase ( EC ), and vertebrate inositol polyphosphate 1-phosphatase ( EC ), are enzymes of the inositol phosphate second messenger signalling pathway, and share similar enzyme activity. Both enzymes exhibit an absolute requirement for metal ions (Mg2 is preferred), and their amino acid sequences contain a number of conserved motifs, which are also shared by several other proteins related to MPTASE (including products of fungal QaX and qutG, bacterial suhB and cysQ, and yeast hal2) [ PUBMED:7761465 ]. The function of the other proteins is not yet clear, but it is suggested that they may act by enhancing the synthesis or degradation of phosphorylated messenger molecules [ PUBMED:1660408 ]. Structural analysis of these proteins has revealed a common core of 155 residues, which includes residues essential for metal binding and catalysis. An interesting property of the enzymes of this family is their sensitivity to Li+. The targets and mechanism of action of Li+ are unknown, but overactive inositol phosphate signalling may account for symptoms of manic depression [ PUBMED:2553271 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Phospoesterase (CL0171), which has the following description:

Members of this clan show metal-dependent / lithium sensitive phosphomonoesterase activity. The clan includes inositol polyphosphate 1 phosphatase and fructose 1,6-bisphosphatase [1].

The clan contains the following 3 members:

FBPase FBPase_glpX Inositol_P


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

Representative proteomes UniProt
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PP/heatmap 1            

1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

Representative proteomes UniProt

Download options

We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

Representative proteomes UniProt
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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: inositol_P;
Type: Family
Sequence Ontology: SO:0100021
Author: Finn RD , Griffiths-Jones SR
Number in seed: 43
Number in full: 27556
Average length of the domain: 260.4 aa
Average identity of full alignment: 23 %
Average coverage of the sequence by the domain: 90.93 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.0 27.0
Trusted cut-off 27.0 27.0
Noise cut-off 26.9 26.9
Model length: 272
Family (HMM) version: 28
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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The tree shows the occurrence of this domain across different species. More...


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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 Inositol_P domain has been found. There are 164 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 sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044QYC5 View 3D Structure Click here
A0A044SEK9 View 3D Structure Click here
A0A044V8T9 View 3D Structure Click here
A0A077Z1R2 View 3D Structure Click here
A0A077Z4V4 View 3D Structure Click here
A0A077Z6Q9 View 3D Structure Click here
A0A077ZKZ1 View 3D Structure Click here
A0A0D2DM75 View 3D Structure Click here
A0A0D2FF45 View 3D Structure Click here
A0A0D2GAH2 View 3D Structure Click here
A0A0H3GJW0 View 3D Structure Click here
A0A0H3GL18 View 3D Structure Click here
A0A0H3GLJ4 View 3D Structure Click here
A0A0H3H1J3 View 3D Structure Click here
A0A0K0DV66 View 3D Structure Click here
A0A0K0EAJ9 View 3D Structure Click here
A0A0K0EEI3 View 3D Structure Click here
A0A0N4UEH7 View 3D Structure Click here
A0A0N4UEX0 View 3D Structure Click here
A0A0N4UPW4 View 3D Structure Click here
A0A0P0XL79 View 3D Structure Click here
A0A0P0Y8A3 View 3D Structure Click here
A0A0R0G583 View 3D Structure Click here
A0A0R0G610 View 3D Structure Click here
A0A150ATW9 View 3D Structure Click here
A0A175VWY0 View 3D Structure Click here
A0A175VXN4 View 3D Structure Click here
A0A175W3V0 View 3D Structure Click here
A0A1C1CRY7 View 3D Structure Click here
A0A1C1CXM9 View 3D Structure Click here
A0A1C1CXU3 View 3D Structure Click here
A0A1D6FBS3 View 3D Structure Click here
A0A1D6IF45 View 3D Structure Click here
A0A1D6KWE2 View 3D Structure Click here
A0A1D6QBR8 View 3D Structure Click here
A0A2R8QN59 View 3D Structure Click here
A0A3P7EVS7 View 3D Structure Click here
A0A3Q0KT85 View 3D Structure Click here
A0A5K4EAJ8 View 3D Structure Click here
A0A5K4EYH7 View 3D Structure Click here