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Database: UniProt
Entry: A0A0G0HEI6_9BACT
LinkDB: A0A0G0HEI6_9BACT
Original site: A0A0G0HEI6_9BACT 
ID   A0A0G0HEI6_9BACT        Unreviewed;       256 AA.
AC   A0A0G0HEI6;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   ORFNames=US53_C0031G0012 {ECO:0000313|EMBL:KKQ36965.1};
OS   Candidatus Woesebacteria bacterium GW2011_GWA1_37_7.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1618545 {ECO:0000313|EMBL:KKQ36965.1, ECO:0000313|Proteomes:UP000034591};
RN   [1] {ECO:0000313|EMBL:KKQ36965.1, ECO:0000313|Proteomes:UP000034591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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|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:KKQ36965.1}.
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DR   EMBL; LBTI01000031; KKQ36965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0HEI6; -.
DR   STRING; 1618545.US53_C0031G0012; -.
DR   Proteomes; UP000034591; Unassembled WGS sequence.
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   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; IPR000760; Inositol_monophosphatase-like.
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   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU364068};
KW   Magnesium {ECO:0000256|RuleBase:RU364068};
KW   Metal-binding {ECO:0000256|RuleBase:RU364068}.
SQ   SEQUENCE   256 AA;  28335 MW;  3D8C5CE3E88218AD CRC64;
     MSEMLEVAKK AANEAGEVVL KLRDNLKVKT KSNDSDVLTQ ADLASEKIIL TILKSSFPKH
     NYLSEEMGKE DNKSEFTWVI DPIDGTLSYV AGLPFFGISI GLLKRKEPYL GVINLPALNS
     IYWAEEGKGS YLNGKRIKVS TLREISKSIV IFDYHFAGTR QKDINKILVR LVDKVRYTPT
     FACSVVSLAY VAQGICHANI HTAFPWDFVA GTAIITEAGG KVTDFEGKAI DWSRSLIDLL
     ASNGILHDQI LTLIKP
//
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