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Database: UniProt
Entry: G4MFQ5_9BURK
LinkDB: G4MFQ5_9BURK
Original site: G4MFQ5_9BURK 
ID   G4MFQ5_9BURK            Unreviewed;       264 AA.
AC   G4MFQ5;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   ORFNames=BKIR_c6_3105 {ECO:0000313|EMBL:CCD39984.1};
OS   Candidatus Paraburkholderia kirkii UZHbot1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1055526 {ECO:0000313|EMBL:CCD39984.1, ECO:0000313|Proteomes:UP000003511};
RN   [1] {ECO:0000313|EMBL:CCD39984.1, ECO:0000313|Proteomes:UP000003511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot1 {ECO:0000313|EMBL:CCD39984.1,
RC   ECO:0000313|Proteomes:UP000003511};
RA   Carlier A.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCD39984.1, ECO:0000313|Proteomes:UP000003511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot1 {ECO:0000313|EMBL:CCD39984.1,
RC   ECO:0000313|Proteomes:UP000003511};
RA   Carlier A.L., Eberl L.;
RT   "Draft genome sequence of Candidatus Burkholderia kirkii.";
RL   Submitted (OCT-2011) 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:CCD39984.1}.
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DR   EMBL; CAFE01000231; CCD39984.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4MFQ5; -.
DR   STRING; 1055526.BKIR_c6_3105; -.
DR   HOGENOM; CLU_044118_0_4_4; -.
DR   BioCyc; CBUR1055526:G10QW-481-MONOMER; -.
DR   Proteomes; UP000003511; 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   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: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|RuleBase:RU364068};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003511}.
SQ   SEQUENCE   264 AA;  29063 MW;  26A447837567C42C CRC64;
     MLNMAVKAAR RAGQIINRAS LDLDRIQVSK KQHNDFVTEV DKASEAAIIE TLHTAYPDHS
     ILAEESGETD RESEYQWLID PLDGTTNFIH GFPYYCVSIA LAHKGVVQQA VVYDPTRNDL
     YTASRGRGAY LNERRIRVGK LDRLSDALIG TGFPFRDGQG LNAYMRLFSE MTLSCAGLRR
     PGAAALDLAN VAAGRLDGFF EQGIHPWDVA AGALIVTEAG GLVGNYTGES DFLFQNEIVA
     ANPKVYAQMV KILDMYSRTR LTGE
//
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