ID W6PK38_9BACE Unreviewed; 267 AA.
AC W6PK38;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN ORFNames=BN890_19800 {ECO:0000313|EMBL:CDM04405.1};
OS Bacteroides xylanisolvens SD CC 1b.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=702447 {ECO:0000313|EMBL:CDM04405.1, ECO:0000313|Proteomes:UP000019380};
RN [1] {ECO:0000313|EMBL:CDM04405.1, ECO:0000313|Proteomes:UP000019380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ramaraj T., Sundararajan A., Mudge J., Schilkey F.D., Delvecchio V.,
RA Donlon M., Ziemer C.;
RT "Improved hybrid genome assemblies of Bacteroides xylanisolvens SD CC 1b
RT and Bacteroides xylanisolvens SD CC 2a using Illumina and 454 Sequencing.";
RL Submitted (DEC-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|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:CDM04405.1}.
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DR EMBL; CBXG010000020; CDM04405.1; -; Genomic_DNA.
DR RefSeq; WP_004317517.1; NZ_ADKP01000056.1.
DR AlphaFoldDB; W6PK38; -.
DR Proteomes; UP000019380; 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, ECO:0000313|EMBL:CDM04405.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364068};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364068}.
SQ SEQUENCE 267 AA; 30101 MW; C41C00B385D46050 CRC64;
MLDLKQLTAD VCRIATEVGS FLKEERKNFR RERVVEKHAH DYVSYVDKES EVRVVKALTA
LLPEAGFITE EGSATYQDEP YCWVIDPLDG TTNYIHDEAP YCVSIALRSR TELLLGVVYE
VCRDECFYAW KGGKAFMNGE EIHVSNVEDI KDAFVITELP YNHLQYKQTA LHLIDQLYGV
VGGIRMNGSA AAAICYVAIG RFDAWMEAFL GKWDYSAAAL IVQEAGGKVT DFYGEDHFIE
GHHIIATNGN LHPVFQKLLL EVPPLNM
//
