ID B2IWE0_NOSP7 Unreviewed; 270 AA. AC B2IWE0; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 04-NOV-2026, entry version 79. DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068}; DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068}; GN OrderedLocusNames=Npun_F1159 {ECO:0000313|EMBL:ACC79885.1}; OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102). OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Nostocales; OC Nostocaceae; Nostoc. OX NCBI_TaxID=63737 {ECO:0000313|EMBL:ACC79885.1, ECO:0000313|Proteomes:UP000001191}; RN [1] {ECO:0000313|Proteomes:UP000001191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191}; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Meeks J.C., Elhai J., RA Campbell E.L., Thiel T., Longmire J., Potts M., Atlas R.; RT "Complete sequence of chromosome of Nostoc punctiforme ATCC 29133."; RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACC79885.1, ECO:0000313|Proteomes:UP000001191} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29133 / PCC 73102 {ECO:0000313|Proteomes:UP000001191}; RX PubMed=23463784; DOI=10.1104/pp.112.213116; RA Ekman M., Picossi S., Campbell E.L., Meeks J.C., Flores E.; RT "A Nostoc punctiforme Sugar Transporter Necessary to Establish a RT Cyanobacterium-Plant Symbiosis."; RL Plant Physiol. 161:1984-1992(2013). 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 -!- 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; CP001037; ACC79885.1; -; Genomic_DNA. DR RefSeq; WP_012407906.1; NC_010628.1. DR AlphaFoldDB; B2IWE0; -. DR STRING; 63737.Npun_F1159; -. DR EnsemblBacteria; ACC79885; ACC79885; Npun_F1159. DR KEGG; npu:Npun_F1159; -. DR eggNOG; COG0483; Bacteria. DR HOGENOM; CLU_044118_0_4_3; -. DR OMA; AAAMNMC; -. DR OrthoDB; 9772456at2; -. DR PhylomeDB; B2IWE0; -. DR Proteomes; UP000001191; Chromosome. DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:InterPro. DR GO; GO:0006020; P:inositol metabolic process; IEA:TreeGrafter. DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IEA:InterPro. DR GO; GO:0007165; P:signal transduction; IEA:TreeGrafter. DR CDD; cd01639; IMPase; 1. DR FunFam; 3.30.540.10:FF:000003; Inositol-1-monophosphatase; 1. DR FunFam; 3.40.190.80:FF:000002; Inositol-1-monophosphatase; 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; IPR000760; Inositol_monophosphatase-like. DR InterPro; IPR020550; Inositol_monophosphatase_CS. DR InterPro; IPR022337; Inositol_monophosphatase_SuhB. 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; PR01959; SBIMPHPHTASE. DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1. DR PROSITE; PS00629; IMP_1; 1. DR PROSITE; PS00630; IMP_2; 1. PE 3: Inferred from homology; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364068}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR600760-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR600760-2}; KW Reference proteome {ECO:0000313|Proteomes:UP000001191}. FT BINDING 70 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 70 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-1" FT BINDING 87 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 89..92 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-1" FT BINDING 89 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 90 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-2" FT BINDING 189..191 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-1" FT BINDING 208 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-1" FT BINDING 215 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 215 FT /ligand="substrate" FT /evidence="ECO:0000256|PIRSR:PIRSR600760-1" SQ SEQUENCE 270 AA; 29295 MW; 0EA5F4238CDB53B5 CRC64; MTNIQIFLDI ATEAALAAGA ILQGYLGKLE DAIIEKGRPG DLVTAADKAS EELILEILHR HFPQHSILAE ESGKLGNQEN EYLWAIDPLD GTTNYAHQYP FFAVSIGLLI NGVPEVGVIY DPFHNELFSA ATGLGATRNR RPINVSATSE LSKSLLVTGF AYDRRETSDN NYAEFSHLTH LTQGVRRSGS ASLDLAYVAC GRVDGYWERG LSPWDIAAGI ILLQEAGGKV TAYNGTPVKI ESGRILATNG YIHDSLSNEL LQVPPLSAWV //