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   16-JUN-2009, entry version 61.
DE   RecName: Full=Inositol-1-monophosphatase;
DE            Short=IMPase;
DE            Short=Inositol-1-phosphatase;
DE            Short=I-1-Pase;
DE            EC=3.1.3.25;
GN   Name=suhB; Synonyms=yktC; OrderedLocusNames=BSU14670;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=97124187; PubMed=8969500;
RA   Winters P., Caldwell R.M., Enfield L., Ferrari E.;
RT   "The ampS-nprE (124 degrees-127 degrees) region of the Bacillus
RT   subtilis 168 chromosome: sequencing of a 27 kb segment and
RT   identification of several 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   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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).
CC   -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
CC       + phosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF012285; AAC24940.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13340.1; -; Genomic_DNA.
DR   PIR; E69864; E69864.
DR   RefSeq; NP_389350.1; -.
DR   HSSP; P29218; 1IMF.
DR   GeneID; 935986; -.
DR   GenomeReviews; AL009126_GR; BSU14670.
DR   KEGG; bsu:BSU14670; -.
DR   NMPDR; fig|224308.1.peg.1469; -.
DR   SubtiList; BG11818; suhB.
DR   HOGENOM; Q45499; -.
DR   OMA; Q45499; NIDKETE.
DR   BioCyc; BSUB224308:BSU1469-MON; -.
DR   BRENDA; 3.1.3.25; 150.
DR   GO; GO:0008934; F:inositol-1(or 4)-monophosphatase activity; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   InterPro; IPR000760; Inositol_P.
DR   PANTHER; PTHR20854; Inositol_P; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00378; INOSPHPHTASE.
DR   ProDom; PD023420; Inositol_P; 1.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Magnesium; Metal-binding.
FT   CHAIN         1    265       Inositol-1-monophosphatase.
FT                                /FTId=PRO_0000142554.
FT   METAL        69     69       Magnesium 1 (By similarity).
FT   METAL        87     87       Magnesium 1 (By similarity).
FT   METAL        87     87       Magnesium 2 (By similarity).
FT   METAL        89     89       Magnesium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        90     90       Magnesium 2 (By similarity).
FT   METAL       214    214       Magnesium 2 (By similarity).
FT   BINDING      90     90       Substrate (By similarity).
FT   BINDING     185    185       Substrate (By similarity).
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
//