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Inositol-tetrakisphosphate 1-kinase (EC 2.7.1.134) (Inositol 1,3,4-trisphosphate 5/6-kinase) (Inositol-triphosphate 5/6-kinase) (Ins(1,3,4)P(3) 5/6-kinase) (EC 2.7.1.159)

 ITPK1_ENTHI             Reviewed;         319 AA.
Q9XYQ1; Q50XK5;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
10-MAY-2017, entry version 81.
RecName: Full=Inositol-tetrakisphosphate 1-kinase;
EC=2.7.1.134;
AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase;
Short=Inositol-triphosphate 5/6-kinase;
Short=Ins(1,3,4)P(3) 5/6-kinase;
EC=2.7.1.159;
Name=ITPK1; ORFNames=151.t00008;
Entamoeba histolytica.
Eukaryota; Amoebozoa; Archamoebae; Entamoebidae; Entamoeba.
NCBI_TaxID=5759;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ENZYME ACTIVITY.
STRAIN=ATCC 30459 / HM-1:IMSS;
PubMed=10802324; DOI=10.1016/S0166-6851(00)00197-3;
Field J., Wilson M.P., Mai Z., Majerus P.W., Samuelson J.;
"An Entamoeba histolytica inositol 1,3,4-trisphosphate 5/6-kinase has
a novel 3-kinase activity.";
Mol. Biochem. Parasitol. 108:119-123(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 30459 / HM-1:IMSS;
PubMed=15729342; DOI=10.1038/nature03291;
Loftus B.J., Anderson I., Davies R., Alsmark U.C., Samuelson J.,
Amedeo P., Roncaglia P., Berriman M., Hirt R.P., Mann B.J., Nozaki T.,
Suh B., Pop M., Duchene M., Ackers J., Tannich E., Leippe M.,
Hofer M., Bruchhaus I., Willhoeft U., Bhattacharya A.,
Chillingworth T., Churcher C.M., Hance Z., Harris B., Harris D.,
Jagels K., Moule S., Mungall K.L., Ormond D., Squares R.,
Whitehead S., Quail M.A., Rabbinowitsch E., Norbertczak H., Price C.,
Wang Z., Guillen N., Gilchrist C., Stroup S.E., Bhattacharya S.,
Lohia A., Foster P.G., Sicheritz-Ponten T., Weber C., Singh U.,
Mukherjee C., El-Sayed N.M.A., Petri W.A., Clark C.G., Embley T.M.,
Barrell B.G., Fraser C.M., Hall N.;
"The genome of the protist parasite Entamoeba histolytica.";
Nature 433:865-868(2005).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 30459 / HM-1:IMSS;
Lorenzi H., Amedeo P., Inman J., Schobel S., Caler E.;
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
[4]
X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH INOSITOL
POLYPHOSPHATES, MAGNESIUM AND ADP, AND SUBSTRATE SPECIFICITY.
PubMed=15837423; DOI=10.1016/j.molcel.2005.03.016;
Miller G.J., Wilson M.P., Majerus P.W., Hurley J.H.;
"Specificity determinants in inositol polyphosphate synthesis: crystal
structure of inositol 1,3,4-trisphosphate 5/6-kinase.";
Mol. Cell 18:201-212(2005).
-!- FUNCTION: Kinase that can phosphorylate various inositol
polyphosphate such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3.
Phosphorylates Ins(3,4,5,6)P4 at position 1 to form
Ins(1,3,4,5,6)P5. This reaction is thought to have regulatory
importance, since Ins(3,4,5,6)P4 is an inhibitor of plasma
membrane Ca(2+)-activated Cl(-) channels, while Ins(1,3,4,5,6)P5
is not. Also phosphorylates Ins(1,3,4)P3 on O-5 and O-6 to form
Ins(1,3,4,6)P4, an essential molecule in the hexakisphosphate
(InsP6) pathway. May also act as an isomerase that interconverts
the inositol tetrakisphosphate isomers Ins(1,3,4,5)P4 and
Ins(1,3,4,6)P4 in the presence of ADP and magnesium.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 3,4,5,6-
tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-
pentakisphosphate. {ECO:0000269|PubMed:10802324}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1,3,4-trisphosphate =
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate.
{ECO:0000269|PubMed:10802324}.
-!- CATALYTIC ACTIVITY: ATP + 1D-myo-inositol 1,3,4-trisphosphate =
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate.
{ECO:0000269|PubMed:10802324}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Binds 2 magnesium ions per subunit.;
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15837423}.
-!- SIMILARITY: Belongs to the ITPK1 family. {ECO:0000305}.
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EMBL; AF118848; AAD22969.1; -; Genomic_DNA.
EMBL; DS571201; EAL46318.1; -; Genomic_DNA.
RefSeq; XP_651704.1; XM_646612.1.
PDB; 1Z2N; X-ray; 1.20 A; X=1-319.
PDB; 1Z2O; X-ray; 1.24 A; X=1-319.
PDB; 1Z2P; X-ray; 1.22 A; X=1-319.
PDBsum; 1Z2N; -.
PDBsum; 1Z2O; -.
PDBsum; 1Z2P; -.
ProteinModelPortal; Q9XYQ1; -.
SMR; Q9XYQ1; -.
STRING; 5759.rna_EHI_100310-1; -.
GeneID; 3406022; -.
KEGG; ehi:EHI_100310; -.
EuPathDB; AmoebaDB:EHI_100310; -.
eggNOG; ENOG410IHA6; Eukaryota.
eggNOG; ENOG4110KIK; LUCA.
InParanoid; Q9XYQ1; -.
KO; K00913; -.
OMA; ENSANRF; -.
BRENDA; 2.7.1.159; 2080.
EvolutionaryTrace; Q9XYQ1; -.
Proteomes; UP000001926; Partially assembled WGS sequence.
GO; GO:0005622; C:intracellular; IEA:InterPro.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0047325; F:inositol tetrakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
GO; GO:0052726; F:inositol-1,3,4-trisphosphate 5-kinase activity; IEA:UniProtKB-EC.
GO; GO:0052725; F:inositol-1,3,4-trisphosphate 6-kinase activity; IEA:UniProtKB-EC.
GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:InterPro.
Gene3D; 3.30.1490.20; -; 1.
InterPro; IPR011761; ATP-grasp.
InterPro; IPR013815; ATP_grasp_subdomain_1.
InterPro; IPR008656; Inositol_tetrakis-P_1-kinase.
PANTHER; PTHR14217; PTHR14217; 1.
Pfam; PF05770; Ins134_P3_kin; 1.
PIRSF; PIRSF038186; ITPK; 1.
PROSITE; PS50975; ATP_GRASP; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Isomerase; Kinase;
Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
Transferase.
CHAIN 1 319 Inositol-tetrakisphosphate 1-kinase.
/FTId=PRO_0000220838.
DOMAIN 98 317 ATP-grasp. {ECO:0000255|PROSITE-
ProRule:PRU00409}.
NP_BIND 168 179 ATP.
METAL 275 275 Magnesium 1.
METAL 289 289 Magnesium 1.
METAL 289 289 Magnesium 2.
METAL 291 291 Magnesium 2.
BINDING 17 17 1D-myo-inositol 1,3,4-trisphosphate.
BINDING 57 57 1D-myo-inositol 1,3,4-trisphosphate.
BINDING 94 94 ATP.
BINDING 136 136 ATP.
BINDING 141 141 1D-myo-inositol 1,3,4-trisphosphate.
BINDING 147 147 1D-myo-inositol 1,3,4-trisphosphate.
BINDING 179 179 1D-myo-inositol 1,3,4-trisphosphate.
BINDING 194 194 ATP.
BINDING 210 210 ATP.
BINDING 291 291 1D-myo-inositol 1,3,4-trisphosphate.
BINDING 295 295 1D-myo-inositol 1,3,4-trisphosphate.
STRAND 6 12 {ECO:0000244|PDB:1Z2N}.
HELIX 15 21 {ECO:0000244|PDB:1Z2N}.
STRAND 22 24 {ECO:0000244|PDB:1Z2N}.
STRAND 27 33 {ECO:0000244|PDB:1Z2N}.
STRAND 36 45 {ECO:0000244|PDB:1Z2N}.
STRAND 52 56 {ECO:0000244|PDB:1Z2N}.
STRAND 61 63 {ECO:0000244|PDB:1Z2N}.
HELIX 64 75 {ECO:0000244|PDB:1Z2N}.
STRAND 79 82 {ECO:0000244|PDB:1Z2N}.
HELIX 85 91 {ECO:0000244|PDB:1Z2N}.
HELIX 94 103 {ECO:0000244|PDB:1Z2N}.
STRAND 111 116 {ECO:0000244|PDB:1Z2N}.
HELIX 117 125 {ECO:0000244|PDB:1Z2N}.
STRAND 131 139 {ECO:0000244|PDB:1Z2N}.
STRAND 141 144 {ECO:0000244|PDB:1Z2N}.
HELIX 145 147 {ECO:0000244|PDB:1Z2N}.
STRAND 148 152 {ECO:0000244|PDB:1Z2N}.
HELIX 155 158 {ECO:0000244|PDB:1Z2N}.
STRAND 163 169 {ECO:0000244|PDB:1Z2N}.
STRAND 177 183 {ECO:0000244|PDB:1Z2N}.
STRAND 186 192 {ECO:0000244|PDB:1Z2N}.
STRAND 205 209 {ECO:0000244|PDB:1Z2N}.
HELIX 213 218 {ECO:0000244|PDB:1Z2N}.
HELIX 226 233 {ECO:0000244|PDB:1Z2N}.
TURN 234 237 {ECO:0000244|PDB:1Z2N}.
TURN 245 249 {ECO:0000244|PDB:1Z2N}.
HELIX 253 267 {ECO:0000244|PDB:1Z2N}.
STRAND 270 277 {ECO:0000244|PDB:1Z2N}.
HELIX 279 281 {ECO:0000244|PDB:1Z2N}.
STRAND 286 293 {ECO:0000244|PDB:1Z2N}.
STRAND 298 300 {ECO:0000244|PDB:1Z2P}.
HELIX 302 314 {ECO:0000244|PDB:1Z2N}.
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


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