ID Q5U789_ACTDE Unreviewed; 270 AA. AC Q5U789; DT 07-DEC-2004, integrated into UniProtKB/TrEMBL. DT 07-DEC-2004, sequence version 1. DT 24-JUL-2024, entry version 51. DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068}; DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068}; OS Actinidia deliciosa (Kiwi). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; Ericales; Actinidiaceae; Actinidia. OX NCBI_TaxID=3627 {ECO:0000313|EMBL:AAV49506.1}; RN [1] {ECO:0000313|EMBL:AAV49506.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=15550539; DOI=10.1073/pnas.0407453101; RA Laing W.A., Bulley S., Wright M., Cooney J., Jensen D., Barraclough D., RA MacRae E.; RT "A highly specific L-galactose-1-phosphate phosphatase on the path to RT ascorbate biosynthesis."; RL Proc. Natl. Acad. Sci. U.S.A. 101:16976-16981(2004). RN [2] {ECO:0000313|EMBL:AAV49506.1} RP NUCLEOTIDE SEQUENCE. RA Beuning L., Crowhurst R., Gleave A., Janssen B., Klages K., Martinus R., RA Marsh K., MacRae E., McNeilage M., Newcomb R., Richardson A., Ross G., RA Schroeder R., Snowden K., Walton E., Wei R., Yauk Y.; RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases. 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:0000256|ARBA:ARBA00001033, CC ECO:0000256|RuleBase:RU364068}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|PIRSR:PIRSR600760-2, ECO:0000256|RuleBase:RU364068}; CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol CC from D-glucose 6-phosphate: step 2/2. {ECO:0000256|ARBA:ARBA00005152, CC ECO:0000256|RuleBase:RU364068}. CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. CC {ECO:0000256|ARBA:ARBA00009759, ECO:0000256|RuleBase:RU364068}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY787585; AAV49506.1; -; mRNA. DR AlphaFoldDB; Q5U789; -. DR KEGG; ag:AAV49506; -. DR BRENDA; 3.1.3.93; 121. DR BRENDA; 3.1.3.B9; 121. DR SABIO-RK; Q5U789; -. 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:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; IEA:TreeGrafter. DR CDD; cd01639; IMPase; 1. DR Gene3D; 3.40.190.80; -; 1. DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 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 PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1. DR PANTHER; PTHR20854:SF4; INOSITOL-1-MONOPHOSPHATASE-RELATED; 1. DR Pfam; PF00459; Inositol_P; 1. DR PRINTS; PR00377; IMPHPHTASES. DR PRINTS; PR00378; LIIMPHPHTASE. DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1. DR PROSITE; PS00629; IMP_1; 1. DR PROSITE; PS00630; IMP_2; 1. PE 2: Evidence at transcript level; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364068}; KW Lithium {ECO:0000256|ARBA:ARBA00022671}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR600760-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR600760-2}. FT BINDING 71 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" FT BINDING 91 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" FT BINDING 93 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" FT BINDING 94 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" FT BINDING 221 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" SQ SEQUENCE 270 AA; 29226 MW; F01368ACE8D3AE84 CRC64; MAKNDSYSEF LAIAIDAAKE AGEVIRKGFY QTKHVEHKGQ VDLVTETDKA CEDLIFNHLK LHFPDHKFIG EETTAACGIT ELTDEPTWIV DPLDGTTNFV HGYPFVCVSI GLTIGKVPTV GVVYNPIMNE LFTGIHGQGA FLNGNPIKVS SQSELVKSLL STEVGTKRDK LTVDATTNRI KSLLFKVRSL RMSGSCALNL CGIACGRLDV FYELGFGGPW DVAGGAVIVK EAGGVLFDPS GKEFDISAQR IAASNPLLKD AFIEALRESE //