IMP3_SOLLC
ID IMP3_SOLLC Reviewed; 268 AA.
AC P54928;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Inositol monophosphatase 3;
DE Short=IMP 3;
DE Short=IMPase 3;
DE Short=LeIMP3;
DE EC=3.1.3.25;
DE AltName: Full=Inositol-1(or 4)-monophosphatase 3;
GN Name=IMP3;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, INDUCTION BY LIGHT AND LITHIUM, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. VFNT Cherry;
RX PubMed=8718627; DOI=10.2307/3870160;
RA Gillaspy G.E., Keddie J.S., Oda K., Gruissem W.;
RT "Plant inositol monophosphatase is a lithium-sensitive enzyme encoded by a
RT multigene family.";
RL Plant Cell 7:2175-2185(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706;
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
CC -!- FUNCTION: Responsible for the provision of inositol required for
CC synthesis of phosphatidylinositol and polyphosphoinositides.
CC {ECO:0000269|PubMed:8718627}.
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:0000269|PubMed:8718627};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:8718627};
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2.
CC -!- TISSUE SPECIFICITY: Expressed in the shoot apex, roots, stems, leaves,
CC flowers and young and mature green fruits.
CC {ECO:0000269|PubMed:8718627}.
CC -!- INDUCTION: Up-regulated by light and down-regulated by Li(+).
CC {ECO:0000269|PubMed:8718627}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; U39059; AAB19031.1; -; mRNA.
DR EMBL; AEKE02005274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; T07795; T07795.
DR RefSeq; NP_001233837.1; NM_001246908.2.
DR AlphaFoldDB; P54928; -.
DR SMR; P54928; -.
DR STRING; 4081.Solyc11g012410.1.1; -.
DR PaxDb; P54928; -.
DR PRIDE; P54928; -.
DR EnsemblPlants; Solyc11g012410.2.1; Solyc11g012410.2.1; Solyc11g012410.2.
DR GeneID; 544013; -.
DR Gramene; Solyc11g012410.2.1; Solyc11g012410.2.1; Solyc11g012410.2.
DR KEGG; sly:544013; -.
DR eggNOG; KOG2951; Eukaryota.
DR HOGENOM; CLU_044118_1_0_1; -.
DR InParanoid; P54928; -.
DR OMA; RVDGYWE; -.
DR OrthoDB; 915621at2759; -.
DR PhylomeDB; P54928; -.
DR UniPathway; UPA00823; UER00788.
DR Proteomes; UP000004994; Chromosome 11.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0006021; P:inositol biosynthetic process; IDA:UniProtKB.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 1: Evidence at protein level;
KW Hydrolase; Lithium; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..268
FT /note="Inositol monophosphatase 3"
FT /id="PRO_0000142525"
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 268 AA; 29054 MW; BCB635A029804901 CRC64;
MAQNGSVEQF LDVAVEAAKK AGEIIREGFY KTKHVEHKGM VDLVTETDKA CEDFIFNHLK
QRFPSHKFIG EETTAACGNF ELTDEPTWIV DPLDGTTNFV HGFPFVCVSI GLTIEKKPTV
GVVYNPIIDE LFTGIDGKGA FLNGKPIKVS SQSELVKALL ATEAGTNRDK LVVDATTGRI
NSLLFKVRSL RMCGSCALNL CGVACGRLDL FYELEFGGPW DVAGGAVIVK EAGGFVFDPS
GSEFDLTARR VAATNAHLKD AFIKALNE
