INM2_YEAST
ID INM2_YEAST Reviewed; 292 AA.
AC Q05533; D6VSR7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Inositol monophosphatase 2;
DE Short=IMP 2;
DE Short=IMPase 2;
DE EC=3.1.3.25;
DE AltName: Full=Inositol-1(or 4)-monophosphatase 2;
GN Name=INM2; Synonyms=IMP2; OrderedLocusNames=YDR287W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX 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., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., 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 GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
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., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, ACTIVITY 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 [5]
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 inositol
RT 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 {ECO:0000269|PubMed:10096091, ECO:0000269|PubMed:12593845}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Inhibited by Li(+) and Na(+).
CC {ECO:0000269|PubMed:10096091}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.12 mM for inositol 1-phosphate {ECO:0000269|PubMed:10096091};
CC Vmax=16 umol/min/mg enzyme for inositol 1-phosphate
CC {ECO:0000269|PubMed:10096091};
CC -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC from D-glucose 6-phosphate: step 2/2.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; U51031; AAB64472.1; -; Genomic_DNA.
DR EMBL; AY557746; AAS56072.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12127.1; -; Genomic_DNA.
DR PIR; S70117; S70117.
DR RefSeq; NP_010573.3; NM_001180595.3.
DR AlphaFoldDB; Q05533; -.
DR SMR; Q05533; -.
DR BioGRID; 32340; 58.
DR DIP; DIP-5626N; -.
DR MINT; Q05533; -.
DR STRING; 4932.YDR287W; -.
DR MaxQB; Q05533; -.
DR PaxDb; Q05533; -.
DR PRIDE; Q05533; -.
DR EnsemblFungi; YDR287W_mRNA; YDR287W; YDR287W.
DR GeneID; 851881; -.
DR KEGG; sce:YDR287W; -.
DR SGD; S000002695; INM2.
DR VEuPathDB; FungiDB:YDR287W; -.
DR eggNOG; KOG2951; Eukaryota.
DR GeneTree; ENSGT00940000169763; -.
DR HOGENOM; CLU_044118_1_2_1; -.
DR InParanoid; Q05533; -.
DR OMA; RVDGYWE; -.
DR BioCyc; YEAST:G3O-29851-MON; -.
DR Reactome; R-SCE-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR SABIO-RK; Q05533; -.
DR UniPathway; UPA00823; UER00788.
DR PRO; PR:Q05533; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q05533; protein.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IDA:SGD.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IDA:SGD.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 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 Hydrolase; Lithium; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..292
FT /note="Inositol monophosphatase 2"
FT /id="PRO_0000245568"
FT BINDING 75
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 96..99
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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
