ID C1LK27_SCHJA Unreviewed; 283 AA.
AC C1LK27;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN Name=IMPA2 {ECO:0000313|EMBL:CAX75055.1};
GN ORFNames=EWB00_009508 {ECO:0000313|EMBL:TNN05240.1};
OS Schistosoma japonicum (Blood fluke).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX NCBI_TaxID=6182 {ECO:0000313|EMBL:CAX75055.1};
RN [1] {ECO:0000313|EMBL:CAX75055.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Anhui {ECO:0000313|EMBL:CAX75055.1};
RX DOI=10.1038/nature08140;
RA Liu F., Zhou Y., Wang Z.Q., Lu G., Zheng H., Brindley P.J., McManus D.P.,
RA Blair D., Zhang Q.H., Zhong Y., Wang S., Han Z.G., Chen Z.;
RT "The Schistosoma japonicum genome reveals features of host-parasite
RT interplay.";
RL Nature 460:345-351(2009).
RN [2] {ECO:0000313|EMBL:CAX75055.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Anhui {ECO:0000313|EMBL:CAX75055.1};
RA Gang L.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:TNN05240.1, ECO:0000313|Proteomes:UP000311919}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HuSjv2 {ECO:0000313|EMBL:TNN05240.1};
RC TISSUE=Worms {ECO:0000313|EMBL:TNN05240.1};
RA Hu W., Luo F., Yin M., Mo X., Sun C., Wu Q., Zhu B., Xiang M., Wang J.,
RA Wang Y., Zhang T., Xu B., Zheng H., Feng Z.;
RT "An improved genome assembly of the fluke Schistosoma japonicum.";
RL Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00005152,
CC ECO:0000256|RuleBase:RU364068}.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759, ECO:0000256|RuleBase:RU364068}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FN319327; CAX75055.1; -; mRNA.
DR EMBL; SKCS01000564; TNN05240.1; -; Genomic_DNA.
DR AlphaFoldDB; C1LK27; -.
DR UniPathway; UPA00823; UER00788.
DR Proteomes; UP000311919; 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; IPR020552; Inositol_monoPase_Li-sen.
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 PRINTS; PR00378; LIIMPHPHTASE.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|RuleBase:RU364068, ECO:0000313|EMBL:CAX75055.1};
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:UP000311919}.
SQ SEQUENCE 283 AA; 31620 MW; 9785504C32DA2C99 CRC64;
MVFKVPHHYE IMVDILFIRD LAMKAGKMIE TGFSKSIPYD KKESYADLVT EVDKAVESYI
CQEILASFPS HKIIAEEGYS GNAELTCSPT WIIDPIDGTS NFVSRFPFVC VSIAYYVNKE
PEVAVVYNPI LKWMFHAIRN QGAFLNDKQI CTSSLQDLSQ ALVLTDWGGD RNPSVLDIKS
SNIRQIISKV RGVRTMGSAA LHMCQIAAGN GDIFFEFGIH CWDYAAAVLI VREAGGYCCN
FDGCYIFLFV NESEISHISH SCQLLPPSHI ATLSCLKIQA CFR
//
