Entry sw:SUHB_VIBCH

ID   SUHB_VIBCH              Reviewed;         267 AA.
AC   Q9KTY5;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2002, sequence version 2.
DT   30-NOV-2016, entry version 86.
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   OrderedLocusNames=VC_0745;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A.,
RA   Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
RA   Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
RA   Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
RA   Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
RA   Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
CC       + phosphate.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF93910.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE003852; AAF93910.1; ALT_INIT; Genomic_DNA.
DR   PIR; D82285; D82285.
DR   RefSeq; NP_230394.2; NC_002505.1.
DR   RefSeq; WP_000553435.1; NC_002505.1.
DR   ProteinModelPortal; Q9KTY5; -.
DR   STRING; 243277.VC0745; -.
DR   DNASU; 2615754; -.
DR   EnsemblBacteria; AAF93910; AAF93910; VC_0745.
DR   GeneID; 2615754; -.
DR   KEGG; vch:VC0745; -.
DR   PATRIC; 20080601; VBIVibCho83274_0709.
DR   eggNOG; ENOG4105ECY; Bacteria.
DR   eggNOG; COG0483; LUCA.
DR   KO; K01092; -.
DR   OMA; YDPSRND; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003824; F:catalytic activity; ISS:TIGR.
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:0000287; F:magnesium ion binding; IBA:GO_Central.
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 phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; ISS:TIGR.
DR   CDD; cd01639; IMPase; 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; PTHR20854; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   PRINTS; PR01959; SBIMPHPHTASE.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Hydrolase; Magnesium; Metal-binding;
KW   Reference proteome.
FT   CHAIN         1    267       Inositol-1-monophosphatase.
FT                                /FTId=PRO_0000142575.
FT   REGION       86     89       Substrate binding. {ECO:0000250}.
FT   METAL        67     67       Magnesium 1. {ECO:0000250}.
FT   METAL        84     84       Magnesium 1. {ECO:0000250}.
FT   METAL        84     84       Magnesium 2. {ECO:0000250}.
FT   METAL        86     86       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL        87     87       Magnesium 2. {ECO:0000250}.
FT   METAL       212    212       Magnesium 2. {ECO:0000250}.
FT   BINDING      67     67       Substrate. {ECO:0000250}.
FT   BINDING     183    183       Substrate. {ECO:0000250}.
FT   BINDING     212    212       Substrate. {ECO:0000250}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT         2    259       ipfam:Inositol_P [T]
FT   MYHIT       211    225       ipat:IMP_2 [T]
FT   MYHIT        81     94       ipat:IMP_1 [T]
SQ   SEQUENCE   267 AA;  29088 MW;  88AD8CDF78A7AD87 CRC64;
     MHPMLNIAIR AARKAGNHIA KSLENAEKIQ TTQKGSNDFV TNVDKEAEAI IVSTIKSSYP
     EHCIIAEEGG LIEGKDKEVQ WIIDPLDGTT NFVKGFPHFA VSIAVRFRGK TEVACVYDPM
     TNELFTAQRG AGAQLNNARI RVQPIKDLQG AVLATAFPFK QKQHSESFMK ILSAMFVECA
     DFRRTGSAAL DLCYLAANRV DGYFELGLKP WDMAAGELIA REAGAIVTDF AGGTDYMQSG
     NIVASSPRGV KAILQHIREN GNSAILK
//