IMPA1_XENLA
ID IMPA1_XENLA Reviewed; 285 AA.
AC P29219;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Inositol monophosphatase 1;
DE Short=IMP 1;
DE Short=IMPase 1;
DE EC=3.1.3.25 {ECO:0000250|UniProtKB:P29218};
DE AltName: Full=D-galactose 1-phosphate phosphatase {ECO:0000250|UniProtKB:P29218};
DE EC=3.1.3.94 {ECO:0000250|UniProtKB:P29218};
DE AltName: Full=Inositol-1(or 4)-monophosphatase 1;
GN Name=impa1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RX PubMed=1325777; DOI=10.1042/bj2860147;
RA Wreggett K.A.;
RT "Inositol monophosphatase is a highly conserved enzyme having localized
RT structural similarity to both glycerol 3-phosphate dehydrogenase and
RT haemoglobin.";
RL Biochem. J. 286:147-152(1992).
CC -!- FUNCTION: Responsible for the provision of inositol required for
CC synthesis of phosphatidylinositol and polyphosphoinositides and has
CC been implicated as the pharmacological target for lithium action in
CC brain. Has broad substrate specificity and can use myo-inositol
CC monophosphates, myo-inositol 1,3-diphosphate, myo-inositol 1,4-
CC diphosphate, scyllo-inositol-phosphate, D-galactose 1-phosphate,
CC glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-
CC glycerophosphate, and 2'-AMP as substrates.
CC {ECO:0000250|UniProtKB:P29218}.
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 Evidence={ECO:0000250|UniProtKB:P29218};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-galactose 1-phosphate + H2O = D-galactose + phosphate;
CC Xref=Rhea:RHEA:29315, ChEBI:CHEBI:4139, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58336; EC=3.1.3.94;
CC Evidence={ECO:0000250|UniProtKB:P29218};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P29218};
CC -!- ACTIVITY REGULATION: Inhibited by Li(+), Ca(2+) and Mn(2+), but also by
CC Mg(2+) at concentrations above 3 mM. {ECO:0000250|UniProtKB:P29218}.
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P29218}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P29218}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; X65513; CAA46486.1; -; mRNA.
DR PIR; S24343; S24343.
DR RefSeq; NP_001095235.1; NM_001101765.1.
DR AlphaFoldDB; P29219; -.
DR SMR; P29219; -.
DR MaxQB; P29219; -.
DR GeneID; 397905; -.
DR CTD; 3612; -.
DR UniPathway; UPA00823; UER00788.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0052834; F:inositol monophosphate phosphatase activity; ISS:UniProtKB.
DR GO; GO:0031403; F:lithium ion binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; ISS:UniProtKB.
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 InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PRINTS; PR00378; LIIMPHPHTASE.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Lithium; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..285
FT /note="Inositol monophosphatase 1"
FT /id="PRO_0000142518"
FT BINDING 73
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 95..98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 198..200
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 217
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 224
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P29218"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P29218"
SQ SEQUENCE 285 AA; 30729 MW; 34E9CD9A99231292 CRC64;
MEDRWQECMD FLAVSIARKA GSVVCAALKE DVSIMVKTSL APADLVTATD QKVEEMIISS
IKEKYPSHSF IGEESVAAGA GSTLTDNPTW IIDPIDGTTN FVHRFPFVAV SIGFAVHKQV
EFGVVYSCVE DKMYTGRKGK GSFCNGQKLQ VSGQKDITKS MIITELGSNR NPEFIKTVSL
SNMERLLCIP IHGIRAVGTA AVNMCLVATG GADAYYEMGL HCWDMAAASV IVTEAGGTIL
DATGGLFDLM SCRIISASSR EIAERIAKEL QIIPLERDDG KSTNS
