ID T0IAC4_9SPHN Unreviewed; 271 AA.
AC T0IAC4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, 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=L288_07510 {ECO:0000313|EMBL:EQB08645.1};
OS Sphingobium quisquiliarum P25.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1329909 {ECO:0000313|EMBL:EQB08645.1, ECO:0000313|Proteomes:UP000015525};
RN [1] {ECO:0000313|EMBL:EQB08645.1, ECO:0000313|Proteomes:UP000015525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P25 {ECO:0000313|EMBL:EQB08645.1,
RC ECO:0000313|Proteomes:UP000015525};
RX PubMed=24029763;
RA Kumar Singh A., Sangwan N., Sharma A., Gupta V., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of Sphingobium quisquiliarum Strain P25T, a Novel
RT Hexachlorocyclohexane (HCH)-Degrading Bacterium Isolated from an HCH
RT Dumpsite.";
RL Genome Announc. 1:e00717-13(2013).
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:EQB08645.1}.
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DR EMBL; ATHO01000066; EQB08645.1; -; Genomic_DNA.
DR RefSeq; WP_021237786.1; NZ_ATHO01000066.1.
DR AlphaFoldDB; T0IAC4; -.
DR PATRIC; fig|1329909.3.peg.1453; -.
DR Proteomes; UP000015525; 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 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}.
SQ SEQUENCE 271 AA; 29770 MW; DD31E5670CB37B23 CRC64;
MVSHSGLLTV MERAARKAGA KLRRDFGEVE HLQVSRKGPA DFVSKADQQA ERTLVEELQK
ARPDWGFLLE EGGVIEGDPT KPRWIIDPLD GTTNFLHGIP HFAISIAVEE PLYGGNKREV
TTGLIYQPVT DESYWAEKSR GAWRHDQRLR VSARRDLGDC LIATGIPFLG HGDFAQWTRV
FGAVGPSVAG IRRFGAAALD LAHVASGRYD GYWESGLQPW DVAAGILLVR EAGGFVTDFR
GGDQPIERRE VIAGNDAIHS KLHKLVAGAL R
//
