ID SUHB_RHIME Reviewed; 266 AA.
AC Q92M71;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE RecName: Full=Inositol-1-monophosphatase;
DE Short=I-1-Pase;
DE Short=IMPase;
DE Short=Inositol-1-phosphatase;
DE EC=3.1.3.25;
GN Name=suhB; OrderedLocusNames=R02778; ORFNames=SMc03994;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AL591688; CAC47357.1; -; Genomic_DNA.
DR RefSeq; NP_386884.1; NC_003047.1.
DR RefSeq; WP_003536018.1; NC_003047.1.
DR AlphaFoldDB; Q92M71; -.
DR SMR; Q92M71; -.
DR EnsemblBacteria; CAC47357; CAC47357; SMc03994.
DR GeneID; 61604239; -.
DR KEGG; sme:SMc03994; -.
DR PATRIC; fig|266834.11.peg.4290; -.
DR eggNOG; COG0483; Bacteria.
DR HOGENOM; CLU_044118_0_0_5; -.
DR OrthoDB; 9785695at2; -.
DR Proteomes; UP000001976; 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 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; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..266
FT /note="Inositol-1-monophosphatase"
FT /id="PRO_0000142571"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 88..91
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 266 AA; 28685 MW; 542590D938397BC7 CRC64;
MARSALLNVM VQAVFKAGKS LARDFGEVQN LQVSLKGPAD YVSQADRKAE RIIREELMKA
RPTYGFLGEE GEEIKGTDGA HRWIVDPLDG TTNFLHGIPH FAISVALERQ GEIVGAVVFN
PATDELYTAE RGGGAFLNDR RLRVGARKAL SDAVIGTGTP HLGRGNHGKY LVELRHVMGE
VAGIRRMGSA SLDLAYVAAG RFDGFWERDL AAWDMAAGLL LIREAGGWST DAEGGGKPLE
AGSIVCGNEH IAKALREVIQ RPIPSK
//
