ID   SUHB_ECOL6              Reviewed;         267 AA.
AC   P0ADG5; P22783; P77511; Q8X2E6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   16-JUN-2009, entry version 25.
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; OrderedLocusNames=c3059;
OS   Escherichia coli O6.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=217992;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O6:H1 / CFT073 / ATCC 700928 / UPEC;
RX   MEDLINE=22388234; PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA   Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA   Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA   Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence
RT   of uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
CC       + phosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- SUBUNIT: Monomer (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; AE014075; AAN81509.1; -; Genomic_DNA.
DR   RefSeq; NP_754941.1; -.
DR   HSSP; P29218; 1IMF.
DR   GeneID; 1038758; -.
DR   GenomeReviews; AE014075_GR; c3059.
DR   KEGG; ecc:c3059; -.
DR   HOGENOM; P0ADG5; -.
DR   OMA; P0ADG5; KGINDYV.
DR   BRENDA; 3.1.3.25; 292881.
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    267       Inositol-1-monophosphatase.
FT                                /FTId=PRO_0000142561.
FT   METAL        67     67       Magnesium 1 (By similarity).
FT   METAL        84     84       Magnesium 1 (By similarity).
FT   METAL        84     84       Magnesium 2 (By similarity).
FT   METAL        86     86       Magnesium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        87     87       Magnesium 2 (By similarity).
FT   METAL       212    212       Magnesium 2 (By similarity).
FT   BINDING      87     87       Substrate (By similarity).
FT   BINDING     183    183       Substrate (By similarity).
SQ   SEQUENCE   267 AA;  29172 MW;  8FEC3508BD111301 CRC64;
     MHPMLNIAVR AARKAGNLIA KNYETPDAVE ASQKGSNDFV TNVDKAAEAV IIDTIRKSYP
     QHTIITEESG ELEGTDQDVQ WVIDPLDGTT NFIKRLPHFA VSIAVRIKGR TEVAVVYDPM
     RNELFTATRG QGAQLNGYRL RGSTARDLDG TILATGFPFK AKQYATTYIN IVGKLFNECA
     DFRRTGSAAL DLAYVAAGRV DGFFEIGLRP WDFAAGELLV REAGGIVSDF TGGHNYMLTG
     NIVAGNPRVV KAMLANMRDE LSDALKR
//