ID C5WQI3_SORBI Unreviewed; 357 AA. AC C5WQI3; DT 01-SEP-2009, integrated into UniProtKB/TrEMBL. DT 01-SEP-2009, sequence version 1. DT 27-MAR-2024, entry version 81. DE RecName: Full=Inositol-tetrakisphosphate 1-kinase {ECO:0000256|PIRNR:PIRNR038186}; DE EC=2.7.1.134 {ECO:0000256|PIRNR:PIRNR038186}; GN ORFNames=SORBI_3001G278700 {ECO:0000313|EMBL:EER91837.1}; OS Sorghum bicolor (Sorghum) (Sorghum vulgare). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade; OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum. OX NCBI_TaxID=4558 {ECO:0000313|EMBL:EER91837.1, ECO:0000313|Proteomes:UP000000768}; RN [1] {ECO:0000313|EMBL:EER91837.1, ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=19189423; DOI=10.1038/nature07723; RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J., RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J., RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J., RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M., RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L., RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P., RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman, RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.; RT "The Sorghum bicolor genome and the diversification of grasses."; RL Nature 457:551-556(2009). RN [2] {ECO:0000313|Proteomes:UP000000768} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768}; RX PubMed=29161754; DOI=10.1111/tpj.13781; RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D., RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A., RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.; RT "The Sorghum bicolor reference genome: improved assembly, gene annotations, RT a transcriptome atlas, and signatures of genome organization."; RL Plant J. 93:338-354(2018). CC -!- FUNCTION: Kinase that can phosphorylate various inositol polyphosphate CC such as Ins(3,4,5,6)P4 or Ins(1,3,4)P3. CC {ECO:0000256|PIRNR:PIRNR038186}. 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:0000256|ARBA:ARBA00000680}; 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:0000256|ARBA:ARBA00000399}; 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:0000256|PIRNR:PIRNR038186}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|PIRNR:PIRNR038186, CC ECO:0000256|PIRSR:PIRSR038186-2}; CC Note=Binds 2 magnesium ions per subunit. CC {ECO:0000256|PIRNR:PIRNR038186, ECO:0000256|PIRSR:PIRSR038186-2}; CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245, CC ECO:0000256|PIRNR:PIRNR038186}. CC -!- SIMILARITY: Belongs to the ITPK1 family. CC {ECO:0000256|ARBA:ARBA00009601, ECO:0000256|PIRNR:PIRNR038186}. 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; CM000760; EER91837.1; -; Genomic_DNA. DR RefSeq; XP_002464839.1; XM_002464794.1. DR AlphaFoldDB; C5WQI3; -. DR STRING; 4558.C5WQI3; -. DR EnsemblPlants; EER91837; EER91837; SORBI_3001G278700. DR GeneID; 8055098; -. DR Gramene; EER91837; EER91837; SORBI_3001G278700. DR KEGG; sbi:8055098; -. DR eggNOG; ENOG502QQS1; Eukaryota. DR HOGENOM; CLU_041857_0_0_1; -. DR InParanoid; C5WQI3; -. DR OMA; IDPCIAE; -. DR OrthoDB; 315387at2759; -. DR Proteomes; UP000000768; Chromosome 1. 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: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; 3.30.1490.220; -; 1. DR Gene3D; 3.40.50.11370; -; 1. 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 InterPro; IPR041429; ITPK1_N. DR PANTHER; PTHR14217; INOSITOL-TETRAKISPHOSPHATE 1-KINASE; 1. DR PANTHER; PTHR14217:SF39; INOSITOL-TETRAKISPHOSPHATE 1-KINASE 3; 1. DR Pfam; PF05770; Ins134_P3_kin; 1. DR Pfam; PF17927; Ins134_P3_kin_N; 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|PIRNR:PIRNR038186}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR038186}; KW Magnesium {ECO:0000256|PIRNR:PIRNR038186, ECO:0000256|PIRSR:PIRSR038186-2}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRNR:PIRNR038186}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|PIRNR:PIRNR038186}; KW Reference proteome {ECO:0000313|Proteomes:UP000000768}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR038186}. FT DOMAIN 48..127 FT /note="Inositol-tetrakisphosphate 1-kinase N-terminal" FT /evidence="ECO:0000259|Pfam:PF17927" FT DOMAIN 149..343 FT /note="Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp" FT /evidence="ECO:0000259|Pfam:PF05770" FT BINDING 57 FT /ligand="1D-myo-inositol 1,3,4-trisphosphate" FT /ligand_id="ChEBI:CHEBI:58414" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 98 FT /ligand="1D-myo-inositol 1,3,4-trisphosphate" FT /ligand_id="ChEBI:CHEBI:58414" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 133 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 183 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 194 FT /ligand="1D-myo-inositol 1,3,4-trisphosphate" FT /ligand_id="ChEBI:CHEBI:58414" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 215..226 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 226 FT /ligand="1D-myo-inositol 1,3,4-trisphosphate" FT /ligand_id="ChEBI:CHEBI:58414" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 241 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 306 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-2" FT BINDING 321 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-2" FT BINDING 321 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-2" FT BINDING 323 FT /ligand="1D-myo-inositol 1,3,4-trisphosphate" FT /ligand_id="ChEBI:CHEBI:58414" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" FT BINDING 323 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-2" FT BINDING 327 FT /ligand="1D-myo-inositol 1,3,4-trisphosphate" FT /ligand_id="ChEBI:CHEBI:58414" FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1" SQ SEQUENCE 357 AA; 39514 MW; AB11A6373F018020 CRC64; MRVHGEVSDD EAGAAAAAVT VVGETVVPSS PPPASAAGQQ QQQPQQLVVG YALTKKKVKS FLQPKLLALA RKKGIHFVSI DETCPLSEQG PFDIILHKLT SKEWQQVLED YREEHPEVTV LDPPNAIQHL HNRQSMLQEV ADLNLSDGYG EVCAPRQLVI MKDPSSIPDA VAKAGLSLPL VAKPLVADGT SKSHELSLAY VEASLPLLDP PLVLQEFVNH GGILFKVYIV GETIQVVRRF SLPDVNTYDL GNNDGIFRFP RVSCATNNAE DADVDPCIAE LPPKPLLEKL GKELRRRLGL RLFNIDIIRE HGRKDRYYVI DINYFPGYGK MPGYEHIFTD FLLSLVQSKY KRHLSGS //