SUHB_BACSU
ID SUHB_BACSU Reviewed; 265 AA.
AC Q45499;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000303|PubMed:27784292};
DE Short=I-1-Pase;
DE Short=IMPase;
DE Short=Inositol-1-phosphatase;
DE EC=3.1.3.25 {ECO:0000269|PubMed:27784292};
DE EC=3.1.3.5 {ECO:0000269|PubMed:27784292};
GN Name=suhB {ECO:0000305}; Synonyms=yktC {ECO:0000303|PubMed:27784292};
GN OrderedLocusNames=BSU14670;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969500; DOI=10.1099/13500872-142-11-3033;
RA Winters P., Caldwell R.M., Enfield L., Ferrari E.;
RT "The ampS-nprE (124 degrees-127 degrees) region of the Bacillus subtilis
RT 168 chromosome: sequencing of a 27 kb segment and identification of several
RT genes in the area.";
RL Microbiology 142:3033-3037(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Caldwell R.M., Ferrari E.;
RT "Sequence analysis of the mobA-ampS region of the Bacillus subtilis
RT chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=27784292; DOI=10.1186/s12866-016-0866-5;
RA Terakawa A., Natsume A., Okada A., Nishihata S., Kuse J., Tanaka K.,
RA Takenaka S., Ishikawa S., Yoshida K.I.;
RT "Bacillus subtilis 5'-nucleotidases with various functions and substrate
RT specificities.";
RL BMC Microbiol. 16:249-249(2016).
CC -!- FUNCTION: Hydrolyzes myo-inositol monophosphate. Catalyzes the
CC dephosphorylation of GMP and IMP. {ECO:0000269|PubMed:27784292}.
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:0000269|PubMed:27784292};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside +
CC phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5;
CC Evidence={ECO:0000269|PubMed:27784292};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=76 uM for myo-inositol phosphate {ECO:0000269|PubMed:27784292};
CC KM=490 uM for beta-glycerophosphate {ECO:0000269|PubMed:27784292};
CC KM=1100 uM for IMP {ECO:0000269|PubMed:27784292};
CC KM=1900 uM for GMP {ECO:0000269|PubMed:27784292};
CC Vmax=0.82 umol/min/mg enzyme for myo-inositol phosphate
CC {ECO:0000269|PubMed:27784292};
CC Vmax=1.2 umol/min/mg enzyme for beta-glycerophosphate
CC {ECO:0000269|PubMed:27784292};
CC Vmax=0.78 umol/min/mg enzyme for IMP {ECO:0000269|PubMed:27784292};
CC Vmax=0.169 umol/min/mg enzyme for GMP {ECO:0000269|PubMed:27784292};
CC -!- DISRUPTION PHENOTYPE: No visible phenotype during 5 hours of growth,
CC decreased resistance to oxidative stress caused by diamide.
CC {ECO:0000269|PubMed:27784292}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; AF012285; AAC24940.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13340.1; -; Genomic_DNA.
DR PIR; E69864; E69864.
DR RefSeq; NP_389350.1; NC_000964.3.
DR RefSeq; WP_003232297.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; Q45499; -.
DR SMR; Q45499; -.
DR STRING; 224308.BSU14670; -.
DR PaxDb; Q45499; -.
DR PRIDE; Q45499; -.
DR EnsemblBacteria; CAB13340; CAB13340; BSU_14670.
DR GeneID; 935986; -.
DR KEGG; bsu:BSU14670; -.
DR PATRIC; fig|224308.179.peg.1600; -.
DR eggNOG; COG0483; Bacteria.
DR InParanoid; Q45499; -.
DR OMA; RVDGYWE; -.
DR PhylomeDB; Q45499; -.
DR BioCyc; BSUB:BSU14670-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IBA:GO_Central.
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:0106411; F:XMP 5'-nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..265
FT /note="Inositol-1-monophosphatase"
FT /id="PRO_0000142554"
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 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 89..92
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 90
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 265 AA; 29760 MW; 7362668104FEA7FF CRC64;
MTNWTEIDEI AKKWIREAGA RITQSMHESL TIETKSNPND LVTNIDKETE KFFIDRIQET
FPGHRILGEE GQGDKIHSLE GVVWIIDPID GTMNFVHQQR NFAISIGIFE NGEGKIGLIY
DVVHDELYHA FSGRGAYMNE TKLAPLKETV IEEAILAINA TWVTENRRID QSVLAPLVKR
VRGTRSYGSA ALELANVAAG RIDAYITMRL APWDYAAGCV LLNEVGGTYT TIEGEPFTFL
ENHSVLAGNP SIHKTIFEEY LHARK
