ITPK1_ENTHI
ID ITPK1_ENTHI Reviewed; 319 AA.
AC Q9XYQ1; Q50XK5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Inositol-tetrakisphosphate 1-kinase;
DE EC=2.7.1.134;
DE AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase;
DE Short=Inositol-triphosphate 5/6-kinase;
DE Short=Ins(1,3,4)P(3) 5/6-kinase;
DE EC=2.7.1.159;
GN Name=ITPK1; ORFNames=151.t00008;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ENZYME ACTIVITY.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=10802324; DOI=10.1016/s0166-6851(00)00197-3;
RA Field J., Wilson M.P., Mai Z., Majerus P.W., Samuelson J.;
RT "An Entamoeba histolytica inositol 1,3,4-trisphosphate 5/6-kinase has a
RT novel 3-kinase activity.";
RL Mol. Biochem. Parasitol. 108:119-123(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=15729342; DOI=10.1038/nature03291;
RA Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J., Amedeo P.,
RA Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T., Suh B., Pop M.,
RA Duchene M., Ackers J., Tannich E., Leippe M., Hofer M., Bruchhaus I.,
RA Willhoeft U., Bhattacharya A., Chillingworth T., Churcher C.M., Hance Z.,
RA Harris B., Harris D., Jagels K., Moule S., Mungall K.L., Ormond D.,
RA Squares R., Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H.,
RA Price C., Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S.,
RA Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U.,
RA Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M.,
RA Barrell B.G., Fraser C.M., Hall N.;
RT "The genome of the protist parasite Entamoeba histolytica.";
RL Nature 433:865-868(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RA Lorenzi H., Amedeo P., Inman J., Schobel S., Caler E.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH INOSITOL
RP POLYPHOSPHATES, MAGNESIUM AND ADP, AND SUBSTRATE SPECIFICITY.
RX PubMed=15837423; DOI=10.1016/j.molcel.2005.03.016;
RA Miller G.J., Wilson M.P., Majerus P.W., Hurley J.H.;
RT "Specificity determinants in inositol polyphosphate synthesis: crystal
RT structure of inositol 1,3,4-trisphosphate 5/6-kinase.";
RL Mol. Cell 18:201-212(2005).
CC -!- FUNCTION: Kinase that can phosphorylate various inositol polyphosphate
CC such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. Phosphorylates Ins(3,4,5,6)P4
CC at position 1 to form Ins(1,3,4,5,6)P5. This reaction is thought to
CC have regulatory importance, since Ins(3,4,5,6)P4 is an inhibitor of
CC plasma membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5
CC is not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form
CC Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate (InsP6)
CC pathway. May also act as an isomerase that interconverts the inositol
CC tetrakisphosphate isomers Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the
CC presence of ADP and magnesium.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 3,4,5,6-tetrakisphosphate + ATP = 1D-myo-
CC inositol 1,3,4,5,6-pentakisphosphate + ADP + H(+);
CC Xref=Rhea:RHEA:12452, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57539, ChEBI:CHEBI:57733, ChEBI:CHEBI:456216;
CC EC=2.7.1.134; Evidence={ECO:0000269|PubMed:10802324};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol
CC 1,3,4,5-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:13253,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57895,
CC ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159;
CC Evidence={ECO:0000269|PubMed:10802324};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4-trisphosphate + ATP = 1D-myo-inositol
CC 1,3,4,6-tetrakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20940,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57660,
CC ChEBI:CHEBI:58414, ChEBI:CHEBI:456216; EC=2.7.1.159;
CC Evidence={ECO:0000269|PubMed:10802324};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Note=Binds 2 magnesium ions per subunit.;
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15837423}.
CC -!- SIMILARITY: Belongs to the ITPK1 family. {ECO:0000305}.
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; AF118848; AAD22969.1; -; Genomic_DNA.
DR EMBL; DS571201; EAL46318.1; -; Genomic_DNA.
DR RefSeq; XP_651704.1; XM_646612.1.
DR PDB; 1Z2N; X-ray; 1.20 A; X=1-319.
DR PDB; 1Z2O; X-ray; 1.24 A; X=1-319.
DR PDB; 1Z2P; X-ray; 1.22 A; X=1-319.
DR PDBsum; 1Z2N; -.
DR PDBsum; 1Z2O; -.
DR PDBsum; 1Z2P; -.
DR AlphaFoldDB; Q9XYQ1; -.
DR SMR; Q9XYQ1; -.
DR STRING; 5759.rna_EHI_100310-1; -.
DR GeneID; 3406022; -.
DR KEGG; ehi:EHI_100310; -.
DR VEuPathDB; AmoebaDB:EHI5A_055940; -.
DR VEuPathDB; AmoebaDB:EHI7A_038980; -.
DR VEuPathDB; AmoebaDB:EHI8A_037840; -.
DR VEuPathDB; AmoebaDB:EHI_100310; -.
DR VEuPathDB; AmoebaDB:KM1_069380; -.
DR eggNOG; ENOG502RD8I; Eukaryota.
DR InParanoid; Q9XYQ1; -.
DR OMA; QQGPFHC; -.
DR BRENDA; 2.7.1.159; 2080.
DR EvolutionaryTrace; Q9XYQ1; -.
DR Proteomes; UP000001926; Partially assembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047325; F:inositol tetrakisphosphate 1-kinase activity; IBA:GO_Central.
DR GO; GO:0052726; F:inositol-1,3,4-trisphosphate 5-kinase activity; IBA:GO_Central.
DR GO; GO:0052725; F:inositol-1,3,4-trisphosphate 6-kinase activity; IBA:GO_Central.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0052746; P:inositol phosphorylation; IBA:GO_Central.
DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:InterPro.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR008656; Inositol_tetrakis-P_1-kinase.
DR InterPro; IPR040464; InsP(3)kin_ATP-grasp.
DR PANTHER; PTHR14217; PTHR14217; 1.
DR Pfam; PF05770; Ins134_P3_kin; 1.
DR PIRSF; PIRSF038186; ITPK; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Isomerase; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..319
FT /note="Inositol-tetrakisphosphate 1-kinase"
FT /id="PRO_0000220838"
FT DOMAIN 98..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 17
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT BINDING 57
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT BINDING 94
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 136
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 141
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT BINDING 147
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT BINDING 168..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 179
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT BINDING 194
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 289
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT BINDING 289
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 291
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT BINDING 291
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT BINDING 295
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:1Z2N"
FT HELIX 15..21
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 36..45
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1Z2N"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:1Z2N"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:1Z2N"
FT HELIX 94..103
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:1Z2N"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:1Z2N"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 148..152
FT /evidence="ECO:0007829|PDB:1Z2N"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1Z2N"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:1Z2N"
FT HELIX 226..233
FT /evidence="ECO:0007829|PDB:1Z2N"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:1Z2N"
FT TURN 245..249
FT /evidence="ECO:0007829|PDB:1Z2N"
FT HELIX 253..267
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 270..277
FT /evidence="ECO:0007829|PDB:1Z2N"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 286..293
FT /evidence="ECO:0007829|PDB:1Z2N"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:1Z2P"
FT HELIX 302..314
FT /evidence="ECO:0007829|PDB:1Z2N"
SQ SEQUENCE 319 AA; 36480 MW; D526DBF2E897305D CRC64;
MTTKQTVSLF IWLPESKQKT LFISTKNHTQ FELNNIIFDV TLSTELPDKE PNAIITKRTH
PVGKMADEMR KYEKDHPKVL FLESSAIHDM MSSREEINAL LIKNNIPIPN SFSVKSKEEV
IQLLQSKQLI LPFIVKPENA QGTFNAHQMK IVLEQEGIDD IHFPCLCQHY INHNNKIVKV
FCIGNTLKWQ TRTSLPNVHR CGIKSVDFNN QHLEDILSWP EGVIDKQDII ENSANRFGSK
ILEDPILLNL TSEAEMRDLA YKVRCALGVQ LCGIDFIKEN EQGNPLVVDV NVFPSYGGKV
DFDWFVEKVA LCYTEVAKI
