ID   IMPP_MESCR              Reviewed;         270 AA.
AC   O49071;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Inositol monophosphatase;
DE            Short=IMP;
DE            Short=IMPase;
DE            EC=3.1.3.25;
DE   AltName: Full=Inositol-1(or 4)-monophosphatase;
GN   Name=IMP1;
OS   Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Aizoaceae; Mesembryanthemum;
OC   Mesembryanthemum subgen. Cryophytum.
OX   NCBI_TaxID=3544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Nelson D.E., Bohnert H.J.;
RL   Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Responsible for the provision of inositol required for
CC       synthesis of phosphatidylinositol and polyphosphoinositides.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC         Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by Li(+). {ECO:0000250}.
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 2/2.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF037220; AAB92418.1; -; mRNA.
DR   PIR; T12205; T12205.
DR   AlphaFoldDB; O49071; -.
DR   SMR; O49071; -.
DR   UniPathway; UPA00823; UER00788.
DR   GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd01639; IMPase; 1.
DR   InterPro; IPR033942; IMPase.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR020552; Inositol_monoPase_Li-sen.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   PRINTS; PR00378; LIIMPHPHTASE.
DR   PROSITE; PS00629; IMP_1; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Lithium; Magnesium; Metal-binding.
FT   CHAIN           1..270
FT                   /note="Inositol monophosphatase"
FT                   /id="PRO_0000142526"
FT   BINDING         71
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         71
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         93..96
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         194..196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   270 AA;  29161 MW;  0C045EB33D903A6C CRC64;
     MAANVPLSDF LATAVDAAKR AGEVIRKGFY VKKNVEHKGQ VDLVTETDKS CEDIIFNCLK
     QQYPNHKFIG EETTAAYGAT ELTDEPTWIV DPLDGTTNFV HGFPFVCVSI GLTIGKVPTV
     GVVYNPIMNE LFTGVRRQGA FLNGVPIHVS SKDELVNCLL VTEVGTKRDK STVDATTNRI
     NGLLFKVRSI RMAGSCALDL CGIACGRADL MYENGYGGAW DVTAGIVIVE EAGGVIFDPS
     GKDFDITVTR IAASNPLIKD SFVEAFKQAE