ID B0EHN7_ENTDS Unreviewed; 287 AA. AC B0EHN7; DT 26-FEB-2008, integrated into UniProtKB/TrEMBL. DT 26-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 67. DE RecName: Full=inositol-1,3,4-trisphosphate 5/6-kinase {ECO:0000256|ARBA:ARBA00012017}; DE EC=2.7.1.159 {ECO:0000256|ARBA:ARBA00012017}; GN ORFNames=EDI_256970 {ECO:0000313|EMBL:EDR25971.1}; OS Entamoeba dispar (strain ATCC PRA-260 / SAW760). OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae; OC Entamoeba. OX NCBI_TaxID=370354 {ECO:0000313|Proteomes:UP000008076}; RN [1] {ECO:0000313|Proteomes:UP000008076} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC PRA-260 / SAW760 {ECO:0000313|Proteomes:UP000008076}; RA Lorenzi H., Inman J., Schobel S., Amedeo P., Caler E.; RT "Annotation of Entamoeba dispar SAW760."; RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRSR:PIRSR038186-2}; CC Note=Binds 2 magnesium ions per subunit. CC {ECO:0000256|PIRSR:PIRSR038186-2}; CC -!- SIMILARITY: Belongs to the ITPK1 family. CC {ECO:0000256|ARBA:ARBA00009601}. 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; DS549342; EDR25971.1; -; Genomic_DNA. DR RefSeq; XP_001737742.1; XM_001737690.1. DR AlphaFoldDB; B0EHN7; -. DR EnsemblProtists; EDR25971; EDR25971; EDI_256970. DR GeneID; 5882794; -. DR KEGG; edi:EDI_256970; -. DR VEuPathDB; AmoebaDB:EDI_256970; -. DR eggNOG; ENOG502QQS1; Eukaryota. DR OMA; VGERTCC; -. DR OrthoDB; 180652at2759; -. DR Proteomes; UP000008076; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0047325; F:inositol tetrakisphosphate 1-kinase activity; IEA:InterPro. DR GO; GO:0052726; F:inositol-1,3,4-trisphosphate 5-kinase activity; IEA:UniProtKB-EC. DR GO; GO:0052725; F:inositol-1,3,4-trisphosphate 6-kinase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0032957; P:inositol trisphosphate metabolic process; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR InterPro; IPR008656; Inositol_tetrakis-P_1-kinase. DR InterPro; IPR040464; InsP(3)kin_ATP-grasp. DR PANTHER; PTHR14217; INOSITOL-TETRAKISPHOSPHATE 1-KINASE; 1. DR PANTHER; PTHR14217:SF1; INOSITOL-TETRAKISPHOSPHATE 1-KINASE; 1. DR Pfam; PF05770; Ins134_P3_kin; 1. DR PIRSF; PIRSF038186; ITPK; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR038186- KW 1}; Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EDR25971.1}; KW Magnesium {ECO:0000256|PIRSR:PIRSR038186-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR038186-2}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRSR:PIRSR038186-1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDR25971.1}. FT DOMAIN 97..273 FT /note="Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp" FT /evidence="ECO:0000259|Pfam:PF05770" FT BINDING 12 FT /ligand="1D-myo-inositol 1,3,4-trisphosphate" FT /ligand_id="ChEBI:CHEBI:58414" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 50 FT /ligand="1D-myo-inositol 1,3,4-trisphosphate" FT /ligand_id="ChEBI:CHEBI:58414" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 85 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 128 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 139 FT /ligand="1D-myo-inositol 1,3,4-trisphosphate" FT /ligand_id="ChEBI:CHEBI:58414" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 160..171 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 171 FT /ligand="1D-myo-inositol 1,3,4-trisphosphate" FT /ligand_id="ChEBI:CHEBI:58414" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 247 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-2" FT BINDING 261 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-2" FT BINDING 261 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-2" FT BINDING 263 FT /ligand="1D-myo-inositol 1,3,4-trisphosphate" FT /ligand_id="ChEBI:CHEBI:58414" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 263 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-2" FT BINDING 267 FT /ligand="1D-myo-inositol 1,3,4-trisphosphate" FT /ligand_id="ChEBI:CHEBI:58414" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" SQ SEQUENCE 287 AA; 33124 MW; 38671CE984499016 CRC64; MKKVIIHISD SKKKKMGWNE NNISFCYKNK IINVYCGSDL TQPFDILLPK IINDHDCQQI LDSIKNNPNA LVVDPIQNQK IIQSRKLTYE RLIQCGIACP QFIIIQSYQE MMRFLNKHQT IHLPVITKPI PSQGSHESHE MTIINHPNGF NHINYPCVIQ EYINHNGQLT KVFCIGKKII SSTIQESMGN IDSSCKLEYF NFNNEDPESK KKYFLTSSQM KPFTTIELQN FCDLLSKAFN ITLFGFDIIR ENGTGKPYII DVNHFPSYNK SFSLQSFTEE LLNECGL //