ID A0A0D2TTW4_GOSRA Unreviewed; 296 AA.
AC A0A0D2TTW4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Inositol-tetrakisphosphate 1-kinase {ECO:0000256|PIRNR:PIRNR038186};
DE EC=2.7.1.134 {ECO:0000256|PIRNR:PIRNR038186};
GN ORFNames=B456_009G224300 {ECO:0000313|EMBL:KJB58741.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB58741.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB58741.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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 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 Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000256|PIRNR:PIRNR038186};
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}.
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DR EMBL; CM001748; KJB58741.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2TTW4; -.
DR EnsemblPlants; KJB58741; KJB58741; B456_009G224300.
DR Gramene; KJB58741; KJB58741; B456_009G224300.
DR Proteomes; UP000032304; Chromosome 9.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047325; F:inositol tetrakisphosphate 1-kinase activity; IEA:UniProtKB-EC.
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; 3.30.1490.220; -; 1.
DR Gene3D; 3.40.50.11370; -; 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.
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};
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:UP000032304};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR038186}.
FT DOMAIN 41..120
FT /note="Inositol-tetrakisphosphate 1-kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17927"
FT DOMAIN 141..271
FT /note="Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp"
FT /evidence="ECO:0000259|Pfam:PF05770"
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 91
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1"
FT BINDING 126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1"
FT BINDING 176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1"
FT BINDING 187
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1"
FT BINDING 208..219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1"
FT BINDING 219
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1"
FT BINDING 234
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR038186-1"
SQ SEQUENCE 296 AA; 33048 MW; 2685BAE972361156 CRC64;
MRLEEEFSHC DNYDEEEEPK TMSQCSIGAL QQQQQQQKFV VVGYALTSKK IKSFLQPKFE
GLARNKGILF VAIDQNRPLS DQGPFDIVLH KLTGKEWRQI LEDYRQTHPE VTVLDPPDAI
QHLHNRQSML QCVADMNLST SYGRVGVPRQ LVIKKDASSI ADAVDKAGLI LPLVAKPLVA
DGSAKSHELS LAYDQYSLQK LEPPLVLQEF VNHGGVLFKV YIVGEAIKVV RRFSLPDVTK
RELSKVTGVF RFPRVSCAAA SADDADLDPS VAVVFGICLN KVSWLNQKRT SPSPFT
//
