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Database: UniProt
Entry: A4HWI6_LEIIN
LinkDB: A4HWI6_LEIIN
Original site: A4HWI6_LEIIN 
ID   A4HWI6_LEIIN            Unreviewed;       473 AA.
AC   A4HWI6; A0A2K4YQF4; A0A381MDZ6;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=inositol-phosphate phosphatase {ECO:0000256|ARBA:ARBA00013106};
DE            EC=3.1.3.25 {ECO:0000256|ARBA:ARBA00013106};
GN   ORFNames=LINJ_15_0940 {ECO:0000313|EMBL:CAM66814.1};
OS   Leishmania infantum.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX   NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM66814.1, ECO:0000313|Proteomes:UP000008153};
RN   [1] {ECO:0000313|EMBL:CAM66814.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM66814.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=17572675; DOI=10.1038/ng2053;
RA   Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA   Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA   Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA   Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA   Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA   Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA   Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA   Mottram J.C., Smith D.F., Berriman M.;
RT   "Comparative genomic analysis of three Leishmania species that cause
RT   diverse human disease.";
RL   Nat. Genet. 39:839-847(2007).
RN   [2] {ECO:0000313|EMBL:CAM66814.1, ECO:0000313|Proteomes:UP000008153}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JPCM5 {ECO:0000313|EMBL:CAM66814.1,
RC   ECO:0000313|Proteomes:UP000008153};
RX   PubMed=22038252; DOI=10.1101/gr.122945.111;
RA   Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA   Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA   Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA   Hertz-Fowler C., Mottram J.C.;
RT   "Chromosome and gene copy number variation allow major structural change
RT   between species and strains of Leishmania.";
RL   Genome Res. 21:2129-2142(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC         Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC         Evidence={ECO:0000256|ARBA:ARBA00001033};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|ARBA:ARBA00009759}.
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DR   EMBL; FR796447; CAM66814.1; -; Genomic_DNA.
DR   RefSeq; XP_001464427.1; XM_001464390.1.
DR   AlphaFoldDB; A4HWI6; -.
DR   STRING; 5671.A4HWI6; -.
DR   GeneID; 5067820; -.
DR   KEGG; lif:LINJ_15_0940; -.
DR   VEuPathDB; TriTrypDB:LINF_150016900; -.
DR   eggNOG; KOG2951; Eukaryota.
DR   InParanoid; A4HWI6; -.
DR   OMA; PDCCISI; -.
DR   OrthoDB; 151755at2759; -.
DR   Proteomes; UP000008153; Chromosome 15.
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:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR   PANTHER; PTHR20854:SF4; INOSITOL-1-MONOPHOSPHATASE-RELATED; 1.
DR   Pfam; PF00459; Inositol_P; 2.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 2.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:CAM66814.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008153}.
SQ   SEQUENCE   473 AA;  49784 MW;  E77DDDB9F0DB36C3 CRC64;
     MSISVMSTPV PASSSADTGD MSLIEALGVA IEAADKGSRI IWQCVEKRRL AMAAAATFHT
     TSALAAGGAA SVECENKTSA TNLVTQHSKQ CRETIIRILR QYSEEVQREK PHLRFAFLTE
     ELNPGTPLSD DYTWVVDPID GAASFVHGLP DCCISIGLTY RKQPVLAVVF TPFISSGVRL
     TVAAAAVLNV AQQQQQQQYQ HQQQQLVMSP TLSVTAPAIS GTMCGSVAAA PLTPMDVSKT
     KMLDEHGTAA APTTALPPTP PTPPFPSLRA AAAATAAASA SPHSVPIITH TTPSVVPECN
     GELFTAIKGF GAFVNGRQVR VNAKVVPATS VVVFNHPCGV MLSTAEAASP DGAAIRRRKC
     DAAIDCSMAM RKELLRLPVA ALRCYGSCAA TLAQVAAGRV DAYLEPAGKA WDVCAGSLLV
     TEAGGVVCNM LGRPLDMAHD TTIVAAATQE MADLMTEKCV RHGFGQYWLV EKE
//
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