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Inositol monophosphatase 1 (IMP 1) (IMPase 1) (LeIMP1) (EC 3.1.3.25) (Inositol-1(or 4)-monophosphatase 1)

 IMP1_SOLLC              Reviewed;         273 AA.
P54926; K4BPY3; Q84MJ7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
31-JAN-2018, entry version 101.
RecName: Full=Inositol monophosphatase 1;
Short=IMP 1;
Short=IMPase 1;
Short=LeIMP1;
EC=3.1.3.25;
AltName: Full=Inositol-1(or 4)-monophosphatase 1;
Name=IMP1; Synonyms=IMP-1;
Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
Solaneae; Solanum; Lycopersicon.
NCBI_TaxID=4081;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
INDUCTION BY LIGHT AND LITHIUM, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
STRAIN=cv. VFNT Cherry;
PubMed=8718627; DOI=10.1105/tpc.7.12.2175;
Gillaspy G.E., Keddie J.S., Oda K., Gruissem W.;
"Plant inositol monophosphatase is a lithium-sensitive enzyme encoded
by a multigene family.";
Plant Cell 7:2175-2185(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=cv. Ailsa Craig;
PubMed=14729261; DOI=10.1016/j.gene.2003.09.048;
Styer J.C., Keddie J., Spence J., Gillaspy G.E.;
"Genomic organization and regulation of the LeIMP-1 and LeIMP-2 genes
encoding myo-inositol monophosphatase in tomato.";
Gene 326:35-41(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Heinz 1706;
PubMed=22660326; DOI=10.1038/nature11119;
Tomato Genome Consortium;
"The tomato genome sequence provides insights into fleshy fruit
evolution.";
Nature 485:635-641(2012).
-!- FUNCTION: Responsible for the provision of inositol required for
synthesis of phosphatidylinositol and polyphosphoinositides.
{ECO:0000269|PubMed:8718627}.
-!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
+ phosphate. {ECO:0000269|PubMed:8718627}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:8718627};
-!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-
inositol from D-glucose 6-phosphate: step 2/2.
-!- TISSUE SPECIFICITY: Expressed in seedlings, flowers, young and
matures green fruits. Detected in roots and stems.
{ECO:0000269|PubMed:8718627}.
-!- DEVELOPMENTAL STAGE: Expression decreases as fruits matures.
{ECO:0000269|PubMed:8718627}.
-!- INDUCTION: Up-regulated by light and down-regulated by Li(+).
{ECO:0000269|PubMed:8718627}.
-!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
{ECO:0000305}.
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EMBL; U39444; AAB19030.1; -; mRNA.
EMBL; AY227666; AAP15454.1; -; Genomic_DNA.
EMBL; AEKE02000440; -; NOT_ANNOTATED_CDS; Genomic_DNA.
RefSeq; NP_001233901.1; NM_001246972.1.
UniGene; Les.3599; -.
ProteinModelPortal; P54926; -.
SMR; P54926; -.
STRING; 4081.Solyc04g014800.2.1; -.
PaxDb; P54926; -.
GeneID; 544280; -.
KEGG; sly:544280; -.
eggNOG; KOG2951; Eukaryota.
eggNOG; COG0483; LUCA.
InParanoid; P54926; -.
KO; K10047; -.
UniPathway; UPA00823; UER00788.
Proteomes; UP000004994; Unplaced.
ExpressionAtlas; P54926; baseline and differential.
GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IBA:GO_Central.
GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0052834; F:inositol monophosphate phosphatase activity; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0006021; P:inositol biosynthetic process; IDA:UniProtKB.
GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
GO; GO:0007165; P:signal transduction; IBA:GO_Central.
CDD; cd01639; IMPase; 1.
InterPro; IPR033942; IMPase.
InterPro; IPR020583; Inositol_monoP_metal-BS.
InterPro; IPR020552; Inositol_monoPase_Li-sen.
InterPro; IPR000760; Inositol_monophosphatase-like.
InterPro; IPR020550; Inositol_monophosphatase_CS.
Pfam; PF00459; Inositol_P; 1.
PRINTS; PR00377; IMPHPHTASES.
PRINTS; PR00378; LIIMPHPHTASE.
PROSITE; PS00629; IMP_1; 1.
PROSITE; PS00630; IMP_2; 1.
1: Evidence at protein level;
Complete proteome; Hydrolase; Lithium; Magnesium; Metal-binding;
Reference proteome.
CHAIN 1 273 Inositol monophosphatase 1.
/FTId=PRO_0000142523.
REGION 93 96 Substrate binding. {ECO:0000250}.
REGION 194 196 Substrate binding. {ECO:0000250}.
METAL 71 71 Magnesium 1. {ECO:0000250}.
METAL 91 91 Magnesium 1. {ECO:0000250}.
METAL 91 91 Magnesium 2. {ECO:0000250}.
METAL 93 93 Magnesium 1; via carbonyl oxygen.
{ECO:0000250}.
METAL 94 94 Magnesium 2. {ECO:0000250}.
METAL 221 221 Magnesium 2. {ECO:0000250}.
BINDING 71 71 Substrate. {ECO:0000250}.
BINDING 221 221 Substrate. {ECO:0000250}.
CONFLICT 12 12 G -> A (in Ref. 3; AEKE02000440).
{ECO:0000305}.
CONFLICT 37 37 H -> Q (in Ref. 2; AAP15454).
{ECO:0000305}.
CONFLICT 216 216 Y -> YG (in Ref. 2; AAP15454).
{ECO:0000305}.
CONFLICT 226 226 A -> T (in Ref. 3; AEKE02000440).
{ECO:0000305}.
CONFLICT 226 226 A -> V (in Ref. 2; AAP15454).
{ECO:0000305}.
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


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