ID K0JJZ1_BRAPL Unreviewed; 291 AA.
AC K0JJZ1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN Name=suhB {ECO:0000313|EMBL:CCG57262.1};
GN ORFNames=WESB_1797 {ECO:0000313|EMBL:CCG57262.1};
OS Brachyspira pilosicoli WesB.
OC Bacteria; Spirochaetota; Spirochaetia; Brachyspirales; Brachyspiraceae;
OC Brachyspira.
OX NCBI_TaxID=1161918 {ECO:0000313|EMBL:CCG57262.1, ECO:0000313|Proteomes:UP000003759};
RN [1] {ECO:0000313|EMBL:CCG57262.1, ECO:0000313|Proteomes:UP000003759}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WesB {ECO:0000313|EMBL:CCG57262.1};
RX PubMed=22947175; DOI=10.1186/1471-2164-13-454;
RA Mappley L.J., Black M.L., Abuoun M., Darby A.C., Woodward M.J.,
RA Parkhill J., Turner A.K., Bellgard M.I., La T., Phillips N.D.,
RA La Ragione R.M., Hampson D.J.;
RT "Comparative genomics of Brachyspira pilosicoli strains: genome
RT rearrangements, reductions and correlation of genetic compliment with
RT phenotypic diversity.";
RL BMC Genomics 13:454-454(2012).
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; HE793032; CCG57262.1; -; Genomic_DNA.
DR RefSeq; WP_014933477.1; NC_018604.1.
DR AlphaFoldDB; K0JJZ1; -.
DR KEGG; bpw:WESB_1797; -.
DR PATRIC; fig|1161918.5.peg.1309; -.
DR HOGENOM; CLU_044118_0_2_12; -.
DR OrthoDB; 9772456at2; -.
DR Proteomes; UP000003759; 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; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR PANTHER; PTHR20854:SF4; INOSITOL-1-MONOPHOSPHATASE-RELATED; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|RuleBase:RU364068};
KW Lithium {ECO:0000256|ARBA:ARBA00022671};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364068};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364068}.
FT COILED 4..31
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 291 AA; 33219 MW; 0B8785105A7385B9 CRC64;
MPIFKKLSDE KKEEIREKKE IESKINKISK SSLNRCIKDA EYIAIKAGKY SLKFFSSPKM
ISHKGKTDLF TEIDVKNEKT IREYLTKKYP KFGFYGEESG KTDNDKDFNW IVDPIDGTTN
FIHGYPFYCV SIGLAYKNIP ILGVVYNPIT DTVYKAHIKS KAYKNKKVIS VSNNNKLIDS
LIITGFYYNT STDDDFLNNR MIDFANMVKR SLAVRRDGSA ALDICMVAEG IADGFFEYGL
SPWDICAGSI ILKQAGGLVT NINMKEYDIF SKKQYIASNK KIHKEMIKVL E
//
