(data stored in ACNUC8465 zone)

SWISSPROT: C1E217_MICCC

ID   C1E217_MICCC            Unreviewed;       280 AA.
AC   C1E217;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   08-MAY-2019, entry version 37.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   ORFNames=MICPUN_79551 {ECO:0000313|EMBL:ACO61842.1};
OS   Micromonas commoda (strain RCC299 / NOUM17 / CCMP2709) (Picoplanktonic
OS   green alga).
OC   Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC   Mamiellaceae; Micromonas.
OX   NCBI_TaxID=296587 {ECO:0000313|EMBL:ACO61842.1, ECO:0000313|Proteomes:UP000002009};
RN   [1] {ECO:0000313|EMBL:ACO61842.1, ECO:0000313|Proteomes:UP000002009}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC299 / NOUM17 {ECO:0000313|Proteomes:UP000002009};
RX   PubMed=19359590; DOI=10.1126/science.1167222;
RA   Worden A.Z., Lee J.H., Mock T., Rouze P., Simmons M.P., Aerts A.L.,
RA   Allen A.E., Cuvelier M.L., Derelle E., Everett M.V., Foulon E.,
RA   Grimwood J., Gundlach H., Henrissat B., Napoli C., McDonald S.M.,
RA   Parker M.S., Rombauts S., Salamov A., Von Dassow P., Badger J.H.,
RA   Coutinho P.M., Demir E., Dubchak I., Gentemann C., Eikrem W.,
RA   Gready J.E., John U., Lanier W., Lindquist E.A., Lucas S., Mayer K.F.,
RA   Moreau H., Not F., Otillar R., Panaud O., Pangilinan J., Paulsen I.,
RA   Piegu B., Poliakov A., Robbens S., Schmutz J., Toulza E., Wyss T.,
RA   Zelensky A., Zhou K., Armbrust E.V., Bhattacharya D., Goodenough U.W.,
RA   Van de Peer Y., Grigoriev I.V.;
RT   "Green evolution and dynamic adaptations revealed by genomes of the
RT   marine picoeukaryotes Micromonas.";
RL   Science 324:268-272(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a myo-inositol phosphate + H2O = myo-inositol +
CC         phosphate; Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17268, ChEBI:CHEBI:43474, ChEBI:CHEBI:84139;
CC         EC=3.1.3.25; Evidence={ECO:0000256|RuleBase:RU364068};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364068};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-
CC       inositol from D-glucose 6-phosphate: step 2/2.
CC       {ECO:0000256|RuleBase:RU364068}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|RuleBase:RU364068}.
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DR   EMBL; CP001324; ACO61842.1; -; Genomic_DNA.
DR   RefSeq; XP_002500584.1; XM_002500538.1.
DR   STRING; 296587.XP_002500584.1; -.
DR   GeneID; 8242192; -.
DR   KEGG; mis:MICPUN_79551; -.
DR   HOGENOM; HOG000282238; -.
DR   InParanoid; C1E217; -.
DR   KO; K10047; -.
DR   OMA; YLWAIDP; -.
DR   OrthoDB; 915621at2759; -.
DR   UniPathway; UPA00823; UER00788.
DR   Proteomes; UP000002009; Chromosome 3.
DR   GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC.
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:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR   CDD; cd01639; IMPase; 1.
DR   InterPro; IPR033942; IMPase.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR020552; Inositol_monoPase_Li-sen.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   PRINTS; PR00378; LIIMPHPHTASE.
DR   PROSITE; PS00629; IMP_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; C1E217.
DR   SWISS-2DPAGE; C1E217.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002009};
KW   Hydrolase {ECO:0000256|RuleBase:RU364068};
KW   Magnesium {ECO:0000256|RuleBase:RU364068};
KW   Metal-binding {ECO:0000256|RuleBase:RU364068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002009}.
SQ   SEQUENCE   280 AA;  29226 MW;  52487A9223BFC952 CRC64;
     MAEIDHAACL VAAELAARAA GEEIKAAWDA ERDVEYKGTV DLVTATDKKC EDLIFDMLQS
     KFPTHAFVGE ESVAAADGKL PEIGDEPTWF VDPLDGTTNF VHAFPFSCVS IGLAVKKKPV
     IGVVFNPISN ECFTAVVGNG ARLNGKPISV SKVSDLGKAL IGTEIGVSRD AATVDAIMGR
     VRACVENARS LRCSGSCAMN MVGVAMGRLD GFYEIGFGGP WDCVGAAVIV TEAGGVVCDP
     SGKPFELTAR RVLCGNPDIA PALTKVLTAI PDGPLEPQAP
//

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