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Reviewed, UniProtKB/Swiss-Prot Q05533 (INM2_YEAST)

Last modified February 9, 2010. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Inositol monophosphatase 2
      Short name=IMPase 2
      Short name=IMP 2
    EC=3.1.3.25
Alternative name(s):
    Inositol-1(or 4)-monophosphatase 2
Gene names
Name: INM2
Synonyms: IMP2
Ordered Locus Names: YDR287W
OrganismSaccharomyces cerevisiae (Baker's yeast) [Complete proteome]
Taxonomic identifier4932 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and involved in the inositol cycle of calcium signaling. Ref.3 Ref.4

Catalytic activity

Myo-inositol phosphate + H2O = myo-inositol + phosphate.

Cofactor

Magnesium.

Enzyme regulation

Inhibited by Li+ and Na+. Ref.3

Pathway

Polyol metabolism; myo-inositol biosynthesis; myo-inositol from D-glucose 6-phosphate: step 2/2.

Sequence similarities

Belongs to the inositol monophosphatase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.12 mM for inositol 1-phosphate

Vmax=16 µmol/min/mg enzyme for inositol 1-phosphate

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 292292Inositol monophosphatase 2
PRO_0000245568

Regions

Region96 – 994Substrate binding By similarity

Sites

Metal binding751Magnesium 1 By similarity
Metal binding941Magnesium 1 By similarity
Metal binding941Magnesium 2 By similarity
Metal binding961Magnesium 1; via carbonyl oxygen By similarity
Metal binding971Magnesium 2 By similarity
Metal binding2311Magnesium 2 By similarity
Binding site751Substrate By similarity
Binding site2311Substrate By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q05533-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: CEA9D943F69E2082

FASTA29232,093
        10         20         30         40         50         60 
MVLTRQVLEE VENTFIELLR SKIGPLVKSH AGTNFCSYDD KANGVDLVTA LDKQIESIIK 

        70         80         90        100        110        120 
ENLTAKYPSF KFIGEETYVK GVTKITNGPT FIVDPIDGTT NFIHGYPYSC TSLGLAEMGK 

       130        140        150        160        170        180 
PVVGVVFNPH LNQLFHASKG NGAFLNDQEI KVSKRPLILQ KSLIALEGGS ERTEGSQGNF 

       190        200        210        220        230        240 
DKKMNTYKNL LSESGAFVHG FRSAGSAAMN ICYVASGMLD AYWEGGCWAW DVCAGWCILE 

       250        260        270        280        290 
EAGGIMVGGN CGEWNIPLDR RCYLAIRGGC ESMEQKRFAE SFWPHVAGEL EY

« Hide

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References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T. expand/collapse author list , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
Nature 387:75-78(1997) [PubMed: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The yeast inositol monophosphatase is a lithium- and sodium-sensitive enzyme encoded by a non-essential gene pair."
Lopez F., Leube M., Gil-Mascarell R., Navarro-Avino J.P., Serrano R.
Mol. Microbiol. 31:1255-1264(1999) [PubMed: 10096091] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]"Yeast inositol mono- and trisphosphate levels are modulated by inositol monophosphatase activity and nutrients."
Navarro-Avino J.P., Belles J.M., Serrano R.
Biochem. Biophys. Res. Commun. 302:41-45(2003) [PubMed: 12593845] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U51031 Genomic DNA. Translation: AAB64472.1.
AY557746 Genomic DNA. Translation: AAS56072.1.
PIRS70117.
RefSeqNP_010573.1.

3D structure databases

SMRQ05533. Positions 22-259.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-5626N.
IntActQ05533. 1 interaction.
STRINGQ05533.

Genome annotation databases

EnsemblYDR287W; YDR287W; YDR287W; Saccharomyces cerevisiae. [Genome view]
GeneID851881.
KEGGsce:YDR287W.
NMPDRfig|4932.3.peg.1335.

Organism-specific databases

CYGDYDR287w.
SGDS000002695. INM2.

Phylogenomic databases

eggNOGfuNOG06264.
HOGENOMHBG730251.
OMALDAYWEG.
OrthoDBEOG9DJMCX.
PhylomeDBQ05533.

Enzyme and pathway databases

BRENDA3.1.3.25. 250.

Gene expression databases

ArrayExpressQ05533.
GenevestigatorQ05533.
GermOnlineYDR287W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR020583. Inositol_monoP_metal-BS.
IPR000760. Inositol_monophosphatase.
IPR020550. Inositol_monophosphatase_CS.
[Graphical view]
PANTHERPTHR20854. Inositol_P. 1 hit.
PfamPF00459. Inositol_P. 1 hit.
[Graphical view]
PRINTSPR00377. IMPHPHTASES.
PROSITEPS00629. IMP_1. 1 hit.
PS00630. IMP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio969850.

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Entry information

Entry nameINM2_YEAST
AccessionPrimary (citable) accession number: Q05533
Entry history
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: November 1, 1996
Last modified: February 9, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents