IMP1_SOLLC
ID IMP1_SOLLC Reviewed; 273 AA.
AC P54926; K4BPY3; Q84MJ7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Inositol monophosphatase 1;
DE Short=IMP 1;
DE Short=IMPase 1;
DE Short=LeIMP1;
DE EC=3.1.3.25;
DE AltName: Full=Inositol-1(or 4)-monophosphatase 1;
GN Name=IMP1; Synonyms=IMP-1;
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 INDUCTION BY LIGHT AND LITHIUM, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
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 [GENOMIC DNA].
RC STRAIN=cv. Ailsa Craig;
RX PubMed=14729261; DOI=10.1016/j.gene.2003.09.048;
RA Styer J.C., Keddie J., Spence J., Gillaspy G.E.;
RT "Genomic organization and regulation of the LeIMP-1 and LeIMP-2 genes
RT encoding myo-inositol monophosphatase in tomato.";
RL Gene 326:35-41(2004).
RN [3]
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 seedlings, flowers, young and matures
CC green fruits. Detected in roots and stems.
CC {ECO:0000269|PubMed:8718627}.
CC -!- DEVELOPMENTAL STAGE: Expression decreases as fruits matures.
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; U39444; AAB19030.1; -; mRNA.
DR EMBL; AY227666; AAP15454.1; -; Genomic_DNA.
DR EMBL; AEKE02000440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001233901.1; NM_001246972.1.
DR AlphaFoldDB; P54926; -.
DR SMR; P54926; -.
DR STRING; 4081.Solyc04g014800.2.1; -.
DR PaxDb; P54926; -.
DR GeneID; 544280; -.
DR KEGG; sly:544280; -.
DR eggNOG; KOG2951; Eukaryota.
DR InParanoid; P54926; -.
DR OrthoDB; 915621at2759; -.
DR UniPathway; UPA00823; UER00788.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P54926; baseline and differential.
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..273
FT /note="Inositol monophosphatase 1"
FT /id="PRO_0000142523"
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 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"
FT CONFLICT 12
FT /note="G -> A (in Ref. 3; AEKE02000440)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="H -> Q (in Ref. 2; AAP15454)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="Y -> YG (in Ref. 2; AAP15454)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="A -> T (in Ref. 3; AEKE02000440)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="A -> V (in Ref. 2; AAP15454)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 29559 MW; 92D1D532E359E0FD CRC64;
MARNGSLEEF LGVAVDAAKR AGEIIRKGFH ETKHVVHKGQ VDLVTETDKA CEDLIFNHLK
QHFPSHKFIG EETSAATGDF DLTDEPTWIV DPVDGTTNFV HGFPSVCVSI GLTIGKIPTV
GVVYDPIIDE LFTGINGKGA YLNGKPIKVS SQSELVKSLL GTEVGTTRDN LTVETTTRRI
NNLLFKVRSL RMCGSCALDL CWVACGRLEL FYLIGYGGPW DVAGGAVIVK EAGGVLFDPS
GSEFDITSQR VAATNPHLKE AFVEALQLSE YVS
