ITPK2_ORYSI
ID ITPK2_ORYSI Reviewed; 349 AA.
AC B8AJL9;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Inositol-tetrakisphosphate 1-kinase 2 {ECO:0000305};
DE EC=2.7.1.134 {ECO:0000305};
DE AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase 2 {ECO:0000305};
DE Short=Inositol-triphosphate 5/6-kinase 2 {ECO:0000305};
DE Short=Ins(1,3,4)P(3) 5/6-kinase 2 {ECO:0000305};
DE Short=OsITP5/6K-2 {ECO:0000305};
DE Short=OsITPK2 {ECO:0000305};
DE EC=2.7.1.159 {ECO:0000305};
GN Name=ITPK2; ORFNames=OsI_10626 {ECO:0000312|EMBL:EEC74810.1};
OS Oryza sativa subsp. indica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39946;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. 93-11;
RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT "The genomes of Oryza sativa: a history of duplications.";
RL PLoS Biol. 3:266-281(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 and participates in phytic acid
CC biosynthesis in developing seeds. Phytic acid is the primary storage
CC form of phosphorus in cereal grains and other plant seeds.
CC {ECO:0000250|UniProtKB:Q84Y01}.
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:0000305};
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:0000305};
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:0000305};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q13572};
CC Note=Binds 2 magnesium ions per subunit.
CC {ECO:0000250|UniProtKB:Q13572};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q13572}.
CC -!- SIMILARITY: Belongs to the ITPK1 family. {ECO:0000305}.
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DR EMBL; CM000128; EEC74810.1; -; Genomic_DNA.
DR AlphaFoldDB; B8AJL9; -.
DR SMR; B8AJL9; -.
DR STRING; 39946.B8AJL9; -.
DR EnsemblPlants; BGIOSGA012174-TA; BGIOSGA012174-PA; BGIOSGA012174.
DR Gramene; BGIOSGA012174-TA; BGIOSGA012174-PA; BGIOSGA012174.
DR HOGENOM; CLU_041857_0_0_1; -.
DR OMA; FLAYDQC; -.
DR Proteomes; UP000007015; Chromosome 3.
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 GO; GO:0047484; P:regulation of response to osmotic stress; IEA:EnsemblPlants.
DR InterPro; IPR008656; Inositol_tetrakis-P_1-kinase.
DR InterPro; IPR040464; InsP(3)kin_ATP-grasp.
DR InterPro; IPR041429; ITPK1_N.
DR PANTHER; PTHR14217; PTHR14217; 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; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..349
FT /note="Inositol-tetrakisphosphate 1-kinase 2"
FT /id="PRO_0000431872"
FT BINDING 48
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 90
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 125
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 175
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 186
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 207..218
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 218
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
FT BINDING 315
FT /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT /ligand_id="ChEBI:CHEBI:58414"
FT /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q13572"
SQ SEQUENCE 349 AA; 38800 MW; 6759CDB676A83E67 CRC64;
MRLHGEVSFD EDEEEVVMVP AAALSSSPLN GGAVPVTRLV VGYALTKKKV KSFLQPNLLL
LARKKGINLV AIDDTRPLAE QGPFDVILHK ITSKEWQQVL EDYHEEHPEV TVLDPPNAIN
HLNNRQSMLA EVSDLNLSSF YGEVCTPRQL VIMRDPSSIP TAVAMAGLTL PLVAKPLVVD
GTSKSHELSL AYDEASLSML DPPLVLQEFV NHGGILFKVY IIGETIQVVR RFSLPDVNTY
DLLNNVGVYR FPRVSCAAAS ADHADLDPHI SELPPRPLLE KLGKELRGRL GLRLFNIDMI
RELGTKDRYY IIDINYFPGF GKMPGYEHIF TDFLLNLAQS KYKKCLSGG
