ID   INM2_YEAST              Reviewed;         292 AA.
AC   Q05533;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 56.
DE   RecName: Full=Inositol monophosphatase 2;
DE            EC=3.1.3.25;
DE   AltName: Full=Inositol-1(or 4)-monophosphatase 2;
DE            Short=IMPase 2;
DE            Short=IMP 2;
GN   Name=INM2; Synonyms=IMP2; OrderedLocusNames=YDR287W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   MEDLINE=97313263; PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
RA   Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
RA   Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
RA   Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
RA   Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
RA   Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
RA   Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
RA   Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
RA   Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
RA   Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
RA   Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
RA   Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
RA   Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
RA   Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
RA   Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
RA   Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
RA   Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
RA   Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
RA   Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
RA   Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
RA   Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
RA   Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
RA   Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
RA   Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
RA   Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
RA   Kolodner R.D., LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-
RT   encoding clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
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).
CC   -!- FUNCTION: Responsible for the provision of inositol required for
CC       synthesis of phosphatidylinositol and polyphosphoinositides and
CC       involved in the inositol cycle of calcium signaling.
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=0.12 mM for inositol 1-phosphate;
CC         Vmax=16 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   -!- SIMILARITY: Belongs to the inositol monophosphatase family.
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DR   EMBL; U51031; AAB64472.1; -; Genomic_DNA.
DR   EMBL; AY557746; AAS56072.1; -; Genomic_DNA.
DR   PIR; S70117; S70117.
DR   RefSeq; NP_010573.1; -.
DR   HSSP; P29218; 1IMF.
DR   DIP; DIP:5626N; -.
DR   IntAct; Q05533; 1.
DR   Ensembl; YDR287W; Saccharomyces cerevisiae.
DR   GeneID; 851881; -.
DR   GenomeReviews; Z71256_GR; YDR287W.
DR   KEGG; sce:YDR287W; -.
DR   NMPDR; fig|4932.3.peg.1335; -.
DR   CYGD; YDR287w; -.
DR   SGD; S000002695; INM2.
DR   HOGENOM; Q05533; -.
DR   OMA; Q05533; STMQKIL.
DR   BRENDA; 3.1.3.25; 250.
DR   NextBio; 969850; -.
DR   GermOnline; YDR287W; Saccharomyces cerevisiae.
DR   GO; GO:0008934; F:inositol-1(or 4)-monophosphatase activity; IDA:SGD.
DR   GO; GO:0031403; F:lithium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:SGD.
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   1: Evidence at protein level;
KW   Complete proteome; Hydrolase; Lithium; Magnesium; Metal-binding.
FT   CHAIN         1    292       Inositol monophosphatase 2.
FT                                /FTId=PRO_0000245568.
FT   METAL        75     75       Magnesium 1 (By similarity).
FT   METAL        94     94       Magnesium 1 (By similarity).
FT   METAL        94     94       Magnesium 2 (By similarity).
FT   METAL        96     96       Magnesium 1; via carbonyl oxygen (By
FT                                similarity).
FT   METAL        97     97       Magnesium 2 (By similarity).
FT   METAL       231    231       Magnesium 2 (By similarity).
FT   BINDING      97     97       Substrate (By similarity).
FT   BINDING     231    231       Substrate (By similarity).
SQ   SEQUENCE   292 AA;  32093 MW;  CEA9D943F69E2082 CRC64;
     MVLTRQVLEE VENTFIELLR SKIGPLVKSH AGTNFCSYDD KANGVDLVTA LDKQIESIIK
     ENLTAKYPSF KFIGEETYVK GVTKITNGPT FIVDPIDGTT NFIHGYPYSC TSLGLAEMGK
     PVVGVVFNPH LNQLFHASKG NGAFLNDQEI KVSKRPLILQ KSLIALEGGS ERTEGSQGNF
     DKKMNTYKNL LSESGAFVHG FRSAGSAAMN ICYVASGMLD AYWEGGCWAW DVCAGWCILE
     EAGGIMVGGN CGEWNIPLDR RCYLAIRGGC ESMEQKRFAE SFWPHVAGEL EY
//