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Database: UniProt
Entry: A0A2A3EA11_APICC
LinkDB: A0A2A3EA11_APICC
Original site: A0A2A3EA11_APICC 
ID   A0A2A3EA11_APICC        Unreviewed;       463 AA.
AC   A0A2A3EA11;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=inositol-phosphate phosphatase {ECO:0000256|ARBA:ARBA00013106};
DE            EC=3.1.3.25 {ECO:0000256|ARBA:ARBA00013106};
GN   ORFNames=APICC_02082 {ECO:0000313|EMBL:PBC28558.1};
OS   Apis cerana cerana (Oriental honeybee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Apis.
OX   NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC28558.1, ECO:0000313|Proteomes:UP000242457};
RN   [1] {ECO:0000313|EMBL:PBC28558.1, ECO:0000313|Proteomes:UP000242457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC28558.1};
RA   Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA   Wu J.;
RT   "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT   insights into honey bee biology.";
RL   Submitted (JUL-2014) 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 2/2. {ECO:0000256|ARBA:ARBA00005152}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|ARBA:ARBA00009759}.
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DR   EMBL; KZ288311; PBC28558.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A3EA11; -.
DR   STRING; 94128.A0A2A3EA11; -.
DR   UniPathway; UPA00823; UER00788.
DR   Proteomes; UP000242457; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:InterPro.
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   InterPro; IPR008699; NDUFB8.
DR   PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR   PANTHER; PTHR20854:SF25; INOSITOL-1-MONOPHOSPHATASE; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   Pfam; PF05821; NDUF_B8; 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   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000242457};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        421..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   463 AA;  53282 MW;  AE37A22BA73CAD21 CRC64;
     MYNISKFFRR NIFVIKSAIN LNKNVKSKGI DWDLVTEYDR KIENDLQKEL LNKYPNHRFI
     GEETTAEKNC LPKLTDEPTW IIDPIDGTTN FVHQFPHTCI SLALIINKSI EIGIVYNPLM
     MQFFSAKRQK GAFLNGHRIK TSKITDLSES LIAMEPWIAK NPNYLVNIYT RMHALIQRTH
     GIRSLGTAAL TLCYVAMGAI EAYHVESIDA WDVAAGKLII EEAGGTVIDT EGGELDLITP
     RVIAACNHQI ADQLLEIDKN ISLFKKRYIL IELILFTKSL ESMFLTSNFF TIDLTVIVLT
     LKKYDKIVDT PYEELLQNEL SVSQKKYMPG LYPKTKEEMK AAAEKYGLHP DEYKPCDPDT
     NYAGDYPDLP FISVEAKDPF YPWDFPALRR NFEEPFHKES NMLFGDRYEY GVRQIVEPHK
     AFPIFCAIMA VSALIFYYSW TISQPLMEKQ YPGEGVHYTF ELK
//
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