(data stored in SCRATCH zone)

SWISSPROT: C6B2L5_RHILS

ID   C6B2L5_RHILS            Unreviewed;       269 AA.
AC   C6B2L5;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   30-AUG-2017, entry version 48.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   OrderedLocusNames=Rleg_0530 {ECO:0000313|EMBL:ACS54835.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54835.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54835.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54835.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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; CP001622; ACS54835.1; -; Genomic_DNA.
DR   RefSeq; WP_012756219.1; NC_012850.1.
DR   ProteinModelPortal; C6B2L5; -.
DR   EnsemblBacteria; ACS54835; ACS54835; Rleg_0530.
DR   KEGG; rlg:Rleg_0530; -.
DR   HOGENOM; HOG000282238; -.
DR   KO; K01092; -.
DR   OMA; FAGGQSR; -.
DR   OrthoDB; POG091H03HH; -.
DR   BioCyc; RLEG395491:GHX2-531-MONOMER; -.
DR   Proteomes; UP000002256; 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; 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; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B2L5.
DR   SWISS-2DPAGE; C6B2L5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Hydrolase {ECO:0000256|RuleBase:RU364068};
KW   Magnesium {ECO:0000256|RuleBase:RU364068};
KW   Metal-binding {ECO:0000256|RuleBase:RU364068}.
SQ   SEQUENCE   269 AA;  29442 MW;  75B629F2836A2EE4 CRC64;
     MSDMEKARWQ SDLTLIADAA KEAGAVAFGF FNQSPEVWWK NEDRSPVSAA DFAANKTLET
     ILRKARPDYG WLSEETDDDA DRLSRETLFI IDPIDGTRAF LGGQKVWCVS VAVVHRGRPV
     AGVLYAPALE EFYEAVEGGV ALKNGVPFTV SAAGPEEMSR LAIGEDLLKT FPTEFRDRVT
     REKYIPSLAY RIAMVADGRL DGTFVKGNSH DWDLAAADLI LVCAGGGLVD IEGRPIVYNR
     AEVTHNVLCA APTPRISEFL AAFAGRRDS
//

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