(data stored in ACNUC7421 zone)

SWISSPROT: D4YX35_SPHJU

ID   D4YX35_SPHJU            Unreviewed;       265 AA.
AC   D4YX35;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   30-AUG-2017, entry version 41.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   Name=cysQ {ECO:0000313|EMBL:BAI94917.1};
GN   OrderedLocusNames=SJA_C1-00830 {ECO:0000313|EMBL:BAI94917.1};
OS   Sphingobium japonicum (strain NBRC 101211 / UT26S).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI94917.1, ECO:0000313|Proteomes:UP000007753};
RN   [1] {ECO:0000313|EMBL:BAI94917.1, ECO:0000313|Proteomes:UP000007753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101211 / UT26S {ECO:0000313|Proteomes:UP000007753};
RX   PubMed=20817768; DOI=10.1128/JB.00961-10;
RA   Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA   Fukui S., Fujita N., Tsuda M.;
RT   "Complete genome sequence of the representative gamma-
RT   hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT   UT26.";
RL   J. Bacteriol. 192:5852-5853(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; AP010803; BAI94917.1; -; Genomic_DNA.
DR   RefSeq; WP_007687384.1; NC_014006.1.
DR   ProteinModelPortal; D4YX35; -.
DR   STRING; 452662.SJA_C1-00830; -.
DR   EnsemblBacteria; BAI94917; BAI94917; SJA_C1-00830.
DR   GeneID; 29271796; -.
DR   KEGG; sjp:SJA_C1-00830; -.
DR   eggNOG; ENOG4105ERR; Bacteria.
DR   eggNOG; COG0483; LUCA.
DR   HOGENOM; HOG000282238; -.
DR   KO; K01092; -.
DR   OMA; FAGGQSR; -.
DR   OrthoDB; POG091H03HH; -.
DR   Proteomes; UP000007753; Chromosome 1.
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; D4YX35.
DR   SWISS-2DPAGE; D4YX35.
KW   Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW   Hydrolase {ECO:0000256|RuleBase:RU364068,
KW   ECO:0000313|EMBL:BAI94917.1};
KW   Magnesium {ECO:0000256|RuleBase:RU364068};
KW   Metal-binding {ECO:0000256|RuleBase:RU364068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007753}.
SQ   SEQUENCE   265 AA;  28478 MW;  2B89D1526DEB6170 CRC64;
     MPAADISLRD VVTAASDAAD RALTLWAGGQ TRVRQWEKVP GHPVCEADLE LDAMLRERLY
     AIDPSAGWLS EETADTVHRL DLPRVWVVDP IDGTRDYLRG RPGWAVSVAL VEHGEARFGI
     LAAPARNELW IAQAGAGATR NGRTLRAGSR SILRGSRVPA DQLPRHDRDL VTVDKPNSIA
     LRMAMVAADE ADLVATVRWG NEWDVAAAAL IAQEAGAIVT DALSNPFSFN RPQPTAFGLL
     CAAPGIHAAA AERLAPRARK ILGRG
//

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