ID INM1_YEAST Reviewed; 295 AA.
AC P38710; D3DKZ4;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 29-MAY-2013, entry version 102.
DE RecName: Full=Inositol monophosphatase 1;
DE Short=IMP 1;
DE Short=IMPase 1;
DE EC=3.1.3.25;
DE AltName: Full=Inositol-1(or 4)-monophosphatase 1;
GN Name=INM1; Synonyms=IMP1; OrderedLocusNames=YHR046C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J.,
RA Du Z., Favello A., Fulton L., Gattung S., Geisel C., Kirsten J.,
RA Kucaba T., Hillier L.W., Jier M., Johnston L., Langston Y.,
RA Latreille P., Louis E.J., Macri C., Mardis E., Menezes S., Mouser L.,
RA Nhan M., Rifkin L., Riles L., St Peter H., Trevaskis E., Vaughan K.,
RA Vignati D., Wilcox L., Wohldman P., Waterston R., Wilson R.,
RA Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RG Saccharomyces Genome Database;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10096091; DOI=10.1046/j.1365-2958.1999.01267.x;
RA Lopez F., Leube M., Gil-Mascarell R., Navarro-Avino J.P., Serrano R.;
RT "The yeast inositol monophosphatase is a lithium- and sodium-sensitive
RT enzyme encoded by a non-essential gene pair.";
RL Mol. Microbiol. 31:1255-1264(1999).
RN [4]
RP FUNCTION.
RX PubMed=12593845; DOI=10.1016/S0006-291X(03)00051-2;
RA Navarro-Avino J.P., Belles J.M., Serrano R.;
RT "Yeast inositol mono- and trisphosphate levels are modulated by
RT inositol monophosphatase activity and nutrients.";
RL Biochem. Biophys. Res. Commun. 302:41-45(2003).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA Dephoure N., O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Responsible for the provision of inositol required for
CC synthesis of phosphatidylinositol and polyphosphoinositides (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
CC + phosphate.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Inhibited by Li(+) and Na(+).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.08 mM for inositol 1-phosphate;
CC Vmax=20 umol/min/mg enzyme for inositol 1-phosphate;
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-
CC inositol from D-glucose 6-phosphate: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- MISCELLANEOUS: Present with 2440 molecules/cell in log phase SD
CC medium.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase family.
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DR EMBL; U00062; AAB68918.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06738.1; -; Genomic_DNA.
DR PIR; S46749; S46749.
DR RefSeq; NP_011912.1; NM_001179176.1.
DR ProteinModelPortal; P38710; -.
DR SMR; P38710; 4-285.
DR DIP; DIP-6506N; -.
DR IntAct; P38710; 1.
DR MINT; MINT-2734649; -.
DR STRING; 4932.YHR046C; -.
DR PaxDb; P38710; -.
DR PeptideAtlas; P38710; -.
DR EnsemblFungi; YHR046C; YHR046C; YHR046C.
DR GeneID; 856442; -.
DR KEGG; sce:YHR046C; -.
DR CYGD; YHR046c; -.
DR SGD; S000001088; INM1.
DR eggNOG; COG0483; -.
DR GeneTree; ENSGT00390000014699; -.
DR HOGENOM; HOG000282238; -.
DR KO; K01092; -.
DR OMA; GYYEPHM; -.
DR OrthoDB; EOG40312B; -.
DR BioCyc; YEAST:YHR046C-MONOMER; -.
DR UniPathway; UPA00823; UER00788.
DR NextBio; 982054; -.
DR Genevestigator; P38710; -.
DR GermOnline; YHR046C; Saccharomyces cerevisiae.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:SGD.
DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:EC.
DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:SGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR PANTHER; PTHR20854; PTHR20854; 1.
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 Complete proteome; Cytoplasm; Hydrolase; Lithium; Magnesium;
KW Metal-binding; Nucleus; Reference proteome.
FT CHAIN 1 295 Inositol monophosphatase 1.
FT /FTId=PRO_0000142585.
FT REGION 94 97 Substrate binding (By similarity).
FT METAL 73 73 Magnesium 1 (By similarity).
FT METAL 92 92 Magnesium 1 (By similarity).
FT METAL 92 92 Magnesium 2 (By similarity).
FT METAL 94 94 Magnesium 1; via carbonyl oxygen (By
FT similarity).
FT METAL 95 95 Magnesium 2 (By similarity).
FT METAL 231 231 Magnesium 2 (By similarity).
FT BINDING 73 73 Substrate (By similarity).
FT BINDING 231 231 Substrate (By similarity).
SQ SEQUENCE 295 AA; 32823 MW; 1DF052114912C6CB CRC64;
MTIDLASIEK FLCELATEKV GPIIKSKSGT QKDYDLKTGS RSVDIVTAID KQVEKLIWES
VKTQYPTFKF IGEESYVKGE TVITDDPTFI IDPIDGTTNF VHDFPFSCTS LGLTVNKEPV
VGVIYNPHIN LLVSASKGNG MRVNNKDYDY KSKLESMGSL ILNKSVVALQ PGSAREGKNF
QTKMATYEKL LSCDYGFVHG FRNLGSSAMT MAYIAMGYLD SYWDGGCYSW DVCAGWCILK
EVGGRVVGAN PGEWSIDVDN RTYLAVRGTI NNESDEQTKY ITDFWNCVDG HLKYD
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