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Database: UniProt
Entry: N9PVQ4_9GAMM
LinkDB: N9PVQ4_9GAMM
Original site: N9PVQ4_9GAMM 
ID   N9PVQ4_9GAMM            Unreviewed;       276 AA.
AC   N9PVQ4;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   ORFNames=F895_00376 {ECO:0000313|EMBL:ENX18300.1};
OS   Acinetobacter sp. CIP 64.2.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1217694 {ECO:0000313|EMBL:ENX18300.1, ECO:0000313|Proteomes:UP000013107};
RN   [1] {ECO:0000313|EMBL:ENX18300.1, ECO:0000313|Proteomes:UP000013107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIP 64.2 {ECO:0000313|EMBL:ENX18300.1,
RC   ECO:0000313|Proteomes:UP000013107};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Cerqueira G., Feldgarden M., Courvalin P., Perichon B.,
RA   Grillot-Courvalin C., Clermont D., Rocha E., Yoon E.-J., Nemec A.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B.,
RA   Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA   Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M.,
RA   Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Acinetobacter sp. CIP 64.2.";
RL   Submitted (FEB-2013) 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:ENX18300.1}.
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DR   EMBL; APRT01000004; ENX18300.1; -; Genomic_DNA.
DR   RefSeq; WP_005238523.1; NZ_KB850120.1.
DR   AlphaFoldDB; N9PVQ4; -.
DR   STRING; 1217694.F895_00376; -.
DR   PATRIC; fig|1217694.3.peg.358; -.
DR   HOGENOM; CLU_044118_0_4_6; -.
DR   Proteomes; UP000013107; 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   PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR   PANTHER; PTHR20854:SF50; NUS FACTOR SUHB; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
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   276 AA;  30303 MW;  6546CB45555C2985 CRC64;
     MEPMVVMAAR AAQTVGQELL KAHQNRHKLD LQVEEKGIDG PVTRVDRYLE ELTIETLRKS
     YKNHSFLGEE FGMQEGKGHD ADWCWVIDPL DGTQNFINGF PHFCISIAVQ HKGVTQHGVI
     YDPVRDELFS ASRGRGAVMN QRRIRVNVKD SLENTFLAVG HPYRAKRNGE IVSYAEQHFA
     SLLAVTKAGA QIRRGGSAAL DLAYVAAGRF DGFFELGLKP WDIAAGELIV KEAGGVVVDA
     RGGSESFDNG QVLACSLKML KPLMQAVVPA WGDAAK
//
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