ID C7JC79_ACEP3 Unreviewed; 275 AA.
AC C7JC79;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN OrderedLocusNames=APA01_17820 {ECO:0000313|EMBL:BAH99907.1};
OS Acetobacter pasteurianus (strain NBRC 105184 / IFO 3283-01).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=634452 {ECO:0000313|EMBL:BAH99907.1, ECO:0000313|Proteomes:UP000000948};
RN [1] {ECO:0000313|EMBL:BAH99907.1, ECO:0000313|Proteomes:UP000000948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105184 / IFO 3283-01 {ECO:0000313|Proteomes:UP000000948};
RX PubMed=19638423; DOI=10.1093/nar/gkp612;
RA Azuma Y., Hosoyama A., Matsutani M., Furuya N., Horikawa H., Harada T.,
RA Hirakawa H., Kuhara S., Matsushita K., Fujita N., Shirai M.;
RT "Whole-genome analyses reveal genetic instability of Acetobacter
RT pasteurianus.";
RL Nucleic Acids Res. 37:5768-5783(2009).
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}.
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DR EMBL; AP011121; BAH99907.1; -; Genomic_DNA.
DR AlphaFoldDB; C7JC79; -.
DR STRING; 634452.APA01_17820; -.
DR KEGG; apt:APA01_17820; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_0_0_5; -.
DR BioCyc; APAS634452:APA01_RS09030-MONOMER; -.
DR Proteomes; UP000000948; Chromosome.
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:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
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:SF50; NUS FACTOR SUHB; 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|RuleBase:RU364068};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364068}.
SQ SEQUENCE 275 AA; 30299 MW; 9A491DA439A0A2D1 CRC64;
MRLSPVMMVM QTAAQKAAKR LLRDFNEVEQ LQVSIKGPGD FVSQADLRAE QTLREELERA
RPGYAFFMEE SGKSGSDNWT WRWVVDPLDG TTNFLHGIPH WAISIGLQRR LPDGRIELAA
GLVYNPAAGE MFWAEKGTGA YLNERRIRVS ARRDMQESLF ATGIPFAKVP ARMRLPFARV
LGALMPRVAG VRRFGAAALD LAWVAAGRYE GYWEFGIKPW DCAAGALIVR EAGGQATDPA
GVDLDDLPDD VMIVAGNGNL HSKLLEVVAD SLKEG
//
