ID   A9L3R4_SHEB9            Unreviewed;       267 AA.
AC   A9L3R4;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   OrderedLocusNames=Sbal195_2506 {ECO:0000313|EMBL:ABX49674.1};
OS   Shewanella baltica (strain OS195).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=399599 {ECO:0000313|EMBL:ABX49674.1, ECO:0000313|Proteomes:UP000000770};
RN   [1] {ECO:0000313|EMBL:ABX49674.1, ECO:0000313|Proteomes:UP000000770}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS195 {ECO:0000313|EMBL:ABX49674.1,
RC   ECO:0000313|Proteomes:UP000000770};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA   Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS195.";
RL   Submitted (NOV-2007) 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}.
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DR   EMBL; CP000891; ABX49674.1; -; Genomic_DNA.
DR   RefSeq; WP_006081861.1; NC_009997.1.
DR   AlphaFoldDB; A9L3R4; -.
DR   GeneID; 11772612; -.
DR   KEGG; sbn:Sbal195_2506; -.
DR   HOGENOM; CLU_044118_0_4_6; -.
DR   Proteomes; UP000000770; 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   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: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};
KW   Transcription {ECO:0000256|ARBA:ARBA00022814};
KW   Transcription antitermination {ECO:0000256|ARBA:ARBA00022814};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00022814}.
SQ   SEQUENCE   267 AA;  29374 MW;  A16DBA2E878982DC CRC64;
     MHPMLTIAVR AARAAGQNIM RAYTELDRIE VSSKGINDFV TSVDKEAEAT ITYQIRKSYP
     DHTIVGEEKG ENRGENNDYV WIVDPLDGTN NFVRGIPHFA ISIALQHKGK TEVAVVYDPV
     REELFTAVRG KGAKLNDFRL RVTNVNELAP TMIGTGFPFK ARQHTETYMA IFGEVFGQCA
     DLRRAGSAAL DLAYVAAGRL DGFFEIGLKP WDIAAGDLIC REAGGTVTDF TGNHNYLISG
     NIVAGSPKVT TELVKIMRPL LNEALKR
//