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Database: UniProt
Entry: V5B4K7_TRYCR
LinkDB: V5B4K7_TRYCR
Original site: V5B4K7_TRYCR 
ID   V5B4K7_TRYCR            Unreviewed;       363 AA.
AC   V5B4K7;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   ORFNames=TCDM_03084 {ECO:0000313|EMBL:ESS68120.1};
OS   Trypanosoma cruzi Dm28c.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX   NCBI_TaxID=1416333 {ECO:0000313|EMBL:ESS68120.1, ECO:0000313|Proteomes:UP000017861};
RN   [1] {ECO:0000313|EMBL:ESS68120.1, ECO:0000313|Proteomes:UP000017861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Dm28c {ECO:0000313|EMBL:ESS68120.1,
RC   ECO:0000313|Proteomes:UP000017861};
RX   PubMed=24482508;
RA   Grisard E.C., Teixeira S.M., de Almeida L.G., Stoco P.H., Gerber A.L.,
RA   Talavera-Lopez C., Lima O.C., Andersson B., de Vasconcelos A.T.;
RT   "Trypanosoma cruzi Clone Dm28c Draft Genome Sequence.";
RL   Genome Announc. 2:e01114-13(2014).
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         ECO:0000256|RuleBase:RU364068};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|RuleBase:RU364068};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 2/2. {ECO:0000256|RuleBase:RU364068}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|ARBA:ARBA00009759, ECO:0000256|RuleBase:RU364068}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESS68120.1}.
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DR   EMBL; AYLP01000023; ESS68120.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5B4K7; -.
DR   EnsemblProtists; ESS68120; ESS68120; TCDM_03084.
DR   VEuPathDB; TriTrypDB:TCDM_03084; -.
DR   UniPathway; UPA00823; UER00788.
DR   Proteomes; UP000017861; Unassembled WGS sequence.
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:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   CDD; cd01639; IMPase; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
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; INOSITOL MONOPHOSPHATASE; 1.
DR   PANTHER; PTHR20854:SF4; INOSITOL-1-MONOPHOSPHATASE-RELATED; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU364068};
KW   Lithium {ECO:0000256|ARBA:ARBA00022671};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU364068};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017861}.
SQ   SEQUENCE   363 AA;  39417 MW;  5C4694364163D900 CRC64;
     MQEQVDLEKA LVVAIKAAQS AGNIMLEFYQ LRREDTAAKM MRLLKEGGSH TTGELAASPK
     PTPVDLLDIK TKSSSTDLVT YYDKLCDETI MKILQRFNAK VEDEKRNEPS EAFSFHFITE
     ELTPDTPLTD EPTWIVDPID GTMSFVHGGC DCCISIGLAI RKQTVLAVVY CPFLSIVQHS
     VEDLRSTSAV AGELYTAIRG KGTFLNGQPI RVSADALPNT ALVAFNYPMG ARLSAAEMPS
     DSAQVGDLKG QKHRKVVEAA GHIREQLAMH PVQGIRSYGS CALILAQVAA GRIDLYMEPA
     GMVWDVCAGS LLITEAGGVV KNMWGGDFGL EGTTTIIAAA NETLADYGVQ LCTQVNYGDY
     WKK
//
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