ID   Q2YRC3_BRUA2            Unreviewed;       263 AA.
AC   Q2YRC3;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   02-SEP-2026, entry version 93.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|ARBA:ARBA00019784, ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|ARBA:ARBA00013106, ECO:0000256|RuleBase:RU364068};
GN   OrderedLocusNames=BAB1_1723 {ECO:0000313|EMBL:CAJ11679.1};
OS   Brucella abortus (strain 2308).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group; Brucella;
OC   Brucella melitensis group.
OX   NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ11679.1, ECO:0000313|Proteomes:UP000002719};
RN   [1] {ECO:0000313|EMBL:CAJ11679.1, ECO:0000313|Proteomes:UP000002719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308 {ECO:0000313|EMBL:CAJ11679.1,
RC   ECO:0000313|Proteomes:UP000002719};
RX   PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG   Microbial Genomics Group;
RG   Lawrence Livermore National Laboratory;
RG   and the Genome Analysis Group;
RG   Oak Ridge National Laboratory;
RA   Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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}.
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DR   EMBL; AM040264; CAJ11679.1; -; Genomic_DNA.
DR   RefSeq; WP_002964800.1; NC_007618.1.
DR   AlphaFoldDB; Q2YRC3; -.
DR   STRING; 359391.BAB1_1723; -.
DR   GeneID; 93017927; -.
DR   KEGG; bmf:BAB1_1723; -.
DR   PATRIC; fig|359391.11.peg.237; -.
DR   HOGENOM; CLU_044118_0_0_5; -.
DR   PhylomeDB; Q2YRC3; -.
DR   Proteomes; UP000002719; Chromosome I.
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:0007165; P:signal transduction; IEA:TreeGrafter.
DR   CDD; cd01639; IMPase; 1.
DR   FunFam; 3.30.540.10:FF:000003; 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; 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.
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:UP000002719}.
FT   BINDING         69
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         86
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         88
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
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         214
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"
SQ   SEQUENCE   263 AA;  28635 MW;  B8F3E8832754F5AA CRC64;
     MARSALLNVM VQAAMKAGRS LARDFGEVQN LQVSLKGPGD YVSQADRRAE QIVYTELSRA
     RPDFRFLMEE SGEVEAKDGQ HRWLVDPLDG TTNFLHGIPV FAVSIALERQ GQIVAGVIYN
     PAMDELYTAE RGGGAFLNDR RLRVSSRNKL VDSVIGTGIP HLGRGHHGHY LVELRNVMAE
     TAGIRRMGAV ALDLAYVAGG RLDGFWEEGM HPWDLGAGIL MVREAGGFVS DKKGGQDIFS
     TQSIVAGNEA IHGALLKTLK KPI
//