ID W4UVL5_9BACE Unreviewed; 219 AA.
AC W4UVL5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN ORFNames=JCM10512_3242 {ECO:0000313|EMBL:GAE84867.1};
OS Bacteroides reticulotermitis JCM 10512.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1445607 {ECO:0000313|EMBL:GAE84867.1, ECO:0000313|Proteomes:UP000019131};
RN [1] {ECO:0000313|EMBL:GAE84867.1, ECO:0000313|Proteomes:UP000019131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10512 {ECO:0000313|EMBL:GAE84867.1,
RC ECO:0000313|Proteomes:UP000019131};
RA Yuki M., Oshima K., Suda W., Sakamoto M., Iida T., Hattori M., Ohkuma M.;
RT "Draft Genome Sequence of Bacteroides reticulotermitis Strain JCM 10512T,
RT Isolated from the Gut of a Termite.";
RL Genome Announc. 2:e00072-14(2014).
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}.
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:GAE84867.1}.
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DR EMBL; BAIV01000020; GAE84867.1; -; Genomic_DNA.
DR AlphaFoldDB; W4UVL5; -.
DR STRING; 1445607.JCM10512_3242; -.
DR Proteomes; UP000019131; 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 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; 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.
PE 3: Inferred from homology;
KW Hydrolase {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:UP000019131}.
SQ SEQUENCE 219 AA; 24491 MW; C83DFE8FC6DECF5E CRC64;
MLDLKQLTAD VCRIATEAGC FLREERKGFR RESVVEKHAH DYVSYVDKES EIRLVKALSA
LLPEAGFIAE EGSATYKDEP YCWVIDPLDG TTNYIHDYAP YCVCIALRSR DELLLGVVYE
VSRDECFYAW KGGKAFLNGT EIQASDVKDI KDAFLIVELP YNSEQYKLTA LHLIDQLYGK
VGGIRMNGSA AAAICYVASG RIDGWVEAFI GKWDYSAAA
//
