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Database: UniProt
Entry: N6YD54_9RHOO
LinkDB: N6YD54_9RHOO
Original site: N6YD54_9RHOO 
ID   N6YD54_9RHOO            Unreviewed;       270 AA.
AC   N6YD54;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   ORFNames=C664_00085 {ECO:0000313|EMBL:ENO80093.1};
OS   Thauera sp. 63.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC   Thauera.
OX   NCBI_TaxID=497321 {ECO:0000313|EMBL:ENO80093.1, ECO:0000313|Proteomes:UP000013007};
RN   [1] {ECO:0000313|EMBL:ENO80093.1, ECO:0000313|Proteomes:UP000013007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=63 {ECO:0000313|EMBL:ENO80093.1,
RC   ECO:0000313|Proteomes:UP000013007};
RA   Liu B., Shapleigh J.P., Frostegard A.H.;
RT   "Draft Genome Sequences of 6 Strains from Genus Thauera.";
RL   Submitted (SEP-2012) 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}.
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:ENO80093.1}.
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DR   EMBL; AMXC01000001; ENO80093.1; -; Genomic_DNA.
DR   RefSeq; WP_004251031.1; NZ_AMXC01000001.1.
DR   AlphaFoldDB; N6YD54; -.
DR   eggNOG; COG0483; Bacteria.
DR   OrthoDB; 9785695at2; -.
DR   Proteomes; UP000013007; 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   270 AA;  29230 MW;  CC86DBC70684174C CRC64;
     MHPTLNIAVK AARRAATVIN RASTQLDLLT VQSKSPNDFV TEVDRAAEQA IIEVLRDAFP
     GHGILAEESG ESGPLNGQES EFNWIIDPLD GTTNFIHGFP QYAISIAQTK NGALEHAVVY
     DPCTNELFTA SRGSGAFLND RRIRVSRRTR LNDSLIGTGF PFRQFDNVDA YLAMFKELTQ
     KTAGIRRPGA ASLDLAYVAC GRLDGFWEMG LSPWDMAAGV LLIQEAGGLV SDLSGEADFM
     ATGNVVAGTP KIFGQLLPII QAYRPANMQA
//
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