ID A0A7Z0T2Z3_9GAMM Unreviewed; 275 AA. AC A0A7Z0T2Z3; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 22-FEB-2023, entry version 6. DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068}; DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068}; GN ORFNames=HFK18_11615 {ECO:0000313|EMBL:NYT99132.1}; OS Stenotrophomonas sp. SbOxS2. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas. OX NCBI_TaxID=2723885 {ECO:0000313|EMBL:NYT99132.1, ECO:0000313|Proteomes:UP000587907}; RN [1] {ECO:0000313|EMBL:NYT99132.1, ECO:0000313|Proteomes:UP000587907} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SbOxS2 {ECO:0000313|EMBL:NYT99132.1, RC ECO:0000313|Proteomes:UP000587907}; RA Hamamura N., Nakajima N., Yamamura S.; RT "Draft genome sequence of an antimony-oxidizing Stenotrophomonas sp. strain RT S2 isolated from antimony mine tailing soil."; RL Submitted (APR-2020) 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|RuleBase:RU364068}; CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. CC {ECO:0000256|ARBA:ARBA00009759, ECO:0000256|RuleBase:RU364068}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NYT99132.1}. 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; JAAVXD010000005; NYT99132.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7Z0T2Z3; -. DR Proteomes; UP000587907; Unassembled WGS sequence. DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro. DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro. DR GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-KW. 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; 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|RuleBase:RU364068}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364068}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|RuleBase:RU364068}; KW Transcription {ECO:0000256|ARBA:ARBA00022814}; KW Transcription antitermination {ECO:0000256|ARBA:ARBA00022814}; KW Transcription regulation {ECO:0000256|ARBA:ARBA00022814}. SQ SEQUENCE 275 AA; 29902 MW; 7DD5D8840F0FB415 CRC64; MQKPAVTVMV KAARLAGNVL LRNINKLEAL NVVQKGRMDY ASEVDADAEK VIVKELKRAY PEYGIFGEEG GVQSERRHMW VIDPLDGTSN YLRGVPHYCV SIALVENGEP TDAVIFDPLR NELFTASRGA GAVLNDRRIR VADRKDLEGT MIHTGFAPRE RARASAQLKS VDALLVHAED IRRSGSAALD LAYVACGRAD AYFEAGVKAW DIAAGVLLVR EAGGKVCDFK GATPARMDNR GPDTQQIVAG NLKVAESLQK VLVNTGYAAE FDAKF //