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Database: UniProt
Entry: E4T8F5_PALPW
LinkDB: E4T8F5_PALPW
Original site: E4T8F5_PALPW 
ID   E4T8F5_PALPW            Unreviewed;       265 AA.
AC   E4T8F5;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   OrderedLocusNames=Palpr_2870 {ECO:0000313|EMBL:ADQ80999.1};
OS   Paludibacter propionicigenes (strain DSM 17365 / JCM 13257 / WB4).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC   Paludibacter.
OX   NCBI_TaxID=694427 {ECO:0000313|EMBL:ADQ80999.1, ECO:0000313|Proteomes:UP000008718};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WB4;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Gronow S., Wellnitz S., Brambilla E.,
RA   Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Paludibacter propionicigenes DSM 17365.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADQ80999.1, ECO:0000313|Proteomes:UP000008718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17365 / JCM 13257 / WB4
RC   {ECO:0000313|Proteomes:UP000008718};
RX   PubMed=21475585; DOI=10.4056/sigs.1503846;
RA   Gronow S., Munk C., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brambilla E., Rohde M., Goker M., Detter J.C., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Paludibacter propionicigenes type strain
RT   (WB4).";
RL   Stand. Genomic Sci. 4:36-44(2011).
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|RuleBase:RU364068}.
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DR   EMBL; CP002345; ADQ80999.1; -; Genomic_DNA.
DR   RefSeq; WP_013446368.1; NC_014734.1.
DR   AlphaFoldDB; E4T8F5; -.
DR   STRING; 694427.Palpr_2870; -.
DR   GeneID; 78492341; -.
DR   KEGG; ppn:Palpr_2870; -.
DR   eggNOG; COG0483; Bacteria.
DR   HOGENOM; CLU_044118_0_4_10; -.
DR   Proteomes; UP000008718; 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   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; 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; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364068};
KW   Magnesium {ECO:0000256|RuleBase:RU364068};
KW   Metal-binding {ECO:0000256|RuleBase:RU364068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008718}.
SQ   SEQUENCE   265 AA;  29292 MW;  46DF9D0ABAF34D17 CRC64;
     MIPTYKELCD FTCEVARSTG KYLSEERVNF DASKIESKGL HDLVSYVDKE SEKRIVRALQ
     AVLPESGFIA EEGTTKKRGE RFNWVIDPLD GTTNFVQGVP VYAVSIGLLD GDELVLGVVY
     EVGRDECFYA WKGGGAFLNG EPIHVSDRNA MNDALLATGF PYSNFGLLDE YIAVLKWAIV
     EARGMRRMGS AAVDLSYVAC GRFDAFWEYD LKSWDVAAGA LILMEAGGTV TDFLGGKNYL
     FDKEIVASNT LLHGVLQHKI AELMK
//
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