ID B0KPH2_PSEPG Unreviewed; 272 AA.
AC B0KPH2;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN OrderedLocusNames=PputGB1_0881 {ECO:0000313|EMBL:ABY96791.1};
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869 {ECO:0000313|EMBL:ABY96791.1, ECO:0000313|Proteomes:UP000002157};
RN [1] {ECO:0000313|EMBL:ABY96791.1, ECO:0000313|Proteomes:UP000002157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1 {ECO:0000313|EMBL:ABY96791.1,
RC ECO:0000313|Proteomes:UP000002157};
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., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) 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; CP000926; ABY96791.1; -; Genomic_DNA.
DR RefSeq; WP_012270588.1; NC_010322.1.
DR AlphaFoldDB; B0KPH2; -.
DR GeneID; 45525919; -.
DR KEGG; ppg:PputGB1_0881; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_0_4_6; -.
DR Proteomes; UP000002157; 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 272 AA; 29828 MW; 686D279479A77E4C CRC64;
MQPMLNIALR AARSASELIF RSIERLDSIK VDEKEAKDYV SEVDRAAEQK IVDALRKAYP
NHSIQGEETG MHAGTGEEGK DYLWIIDPLD GTTNFLRGIP HFAVSIACKY RGRLEHAVVL
DPVRQEEFTA SRGRGAQLNG RRLRVSSRTS LEGALLGTGF PFRDGQMADM DNYLGMFRAL
TGQTAGIRRA GSASLDLAYV AAGRFDAFWE SGLSEWDMAA GVLLIQEAGG LVSDFNGGHD
FLDKGHIVAG NIKCFKAVLT AIQPHLPESM KR
//
