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Database: UniProt
Entry: A0A0Q0JDM1_9GAMM
LinkDB: A0A0Q0JDM1_9GAMM
Original site: A0A0Q0JDM1_9GAMM 
ID   A0A0Q0JDM1_9GAMM        Unreviewed;       267 AA.
AC   A0A0Q0JDM1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, 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   Name=suhB {ECO:0000313|EMBL:KPZ70488.1};
GN   ORFNames=AN944_02236 {ECO:0000313|EMBL:KPZ70488.1};
OS   Shewanella sp. P1-14-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=1723761 {ECO:0000313|EMBL:KPZ70488.1, ECO:0000313|Proteomes:UP000050414};
RN   [1] {ECO:0000313|EMBL:KPZ70488.1, ECO:0000313|Proteomes:UP000050414}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1-14-1 {ECO:0000313|EMBL:KPZ70488.1,
RC   ECO:0000313|Proteomes:UP000050414};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) 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:KPZ70488.1}.
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DR   EMBL; LKTL01000013; KPZ70488.1; -; Genomic_DNA.
DR   RefSeq; WP_055024672.1; NZ_LKTL01000013.1.
DR   AlphaFoldDB; A0A0Q0JDM1; -.
DR   PATRIC; fig|1723761.3.peg.2286; -.
DR   Proteomes; UP000050414; 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   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: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:UP000050414};
KW   Transcription {ECO:0000256|ARBA:ARBA00022814};
KW   Transcription antitermination {ECO:0000256|ARBA:ARBA00022814};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00022814}.
SQ   SEQUENCE   267 AA;  29228 MW;  4553B2623B50331D CRC64;
     MHPMLTIATR AARAAGQTIM RAYTELDKVE VDSKGLNDFV TSVDKEAEAT ITYQIRKSYP
     DHTIVGEEAG ENRGTNKDYV WIVDPLDGTN NFVRGIPHFA VSIAVQYKGK IEVAVIYDPV
     REELFSAVRG QGAKLNEFRL RVTGVNELTN TVIGTGFPFK SRQHTETYMN ILGEVFPVCA
     DIRRAGSAAL DLAYVAAGRL DGFFEIGLKP WDIAAGDLIC RESGGTVTDF TGNHNYLASG
     NVVAGSPKVT SELVKIMRPL LNEGLKR
//
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