(data stored in ACNUC7421 zone)

SWISSPROT: B8IB11_METNO

ID   B8IB11_METNO            Unreviewed;       270 AA.
AC   B8IB11;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   30-AUG-2017, entry version 50.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   OrderedLocusNames=Mnod_0361 {ECO:0000313|EMBL:ACL55404.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55404.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55404.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol
CC       + phosphate. {ECO:0000256|RuleBase:RU364068}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364068};
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase family.
CC       {ECO:0000256|RuleBase:RU364068}.
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DR   EMBL; CP001349; ACL55404.1; -; Genomic_DNA.
DR   RefSeq; WP_015927115.1; NC_011894.1.
DR   ProteinModelPortal; B8IB11; -.
DR   STRING; 460265.Mnod_0361; -.
DR   EnsemblBacteria; ACL55404; ACL55404; Mnod_0361.
DR   KEGG; mno:Mnod_0361; -.
DR   eggNOG; ENOG4105ERR; Bacteria.
DR   eggNOG; COG0483; LUCA.
DR   HOGENOM; HOG000282238; -.
DR   KO; K01092; -.
DR   OMA; FAGGQSR; -.
DR   OrthoDB; POG091H03HH; -.
DR   Proteomes; UP000008207; Chromosome.
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:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR   InterPro; IPR033942; IMPase.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
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   3: Inferred from homology;
DR   PRODOM; B8IB11.
DR   SWISS-2DPAGE; B8IB11.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
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:UP000008207}.
SQ   SEQUENCE   270 AA;  28508 MW;  CEFDD3D3543F3895 CRC64;
     MPSSVDARAL LPQVRATVRE AALLALPFFN VGERTSARVW SKSGGSPVTE ADVAVDTFLK
     IRLSELAPGA AWLSEETRDD PVRLDHDLVW IVDPIDGTRA FLSGDPDWSI AIALLSGGEP
     VLGIVAAPVT GLVYEAVVGQ GARKNGEPIR VTAPESLAGA RVAGPKPMVD HLERNLGLGG
     TPDALIRLRR IPSLALRVAR VAEGLVDVGL ISSDARDWDL AGADLILREA GGVVLDLAGR
     APAYNRREPV HGELVAAPRA VQETLLAAMR
//

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