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Database: UniProt
Entry: M7ZFQ9_TRIUA
LinkDB: M7ZFQ9_TRIUA
Original site: M7ZFQ9_TRIUA 
ID   M7ZFQ9_TRIUA            Unreviewed;       411 AA.
AC   M7ZFQ9;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Inositol-tetrakisphosphate 1-kinase 2 {ECO:0000313|EMBL:EMS58471.1};
GN   ORFNames=TRIUR3_28152 {ECO:0000313|EMBL:EMS58471.1};
OS   Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS58471.1};
RN   [1] {ECO:0000313|EMBL:EMS58471.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23535596; DOI=10.1038/nature11997;
RA   Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA   Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA   Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA   Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA   Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA   Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA   Wang D., Zhang A., Wang J.;
RT   "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL   Nature 496:87-90(2013).
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|ARBA:ARBA00000084};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC   -!- SIMILARITY: Belongs to the ITPK1 family.
CC       {ECO:0000256|ARBA:ARBA00009601}.
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DR   EMBL; KD132673; EMS58471.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7ZFQ9; -.
DR   STRING; 4572.M7ZFQ9; -.
DR   eggNOG; ENOG502QQS1; Eukaryota.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
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   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:SF7; INOSITOL-TETRAKISPHOSPHATE 1-KINASE 2; 1.
DR   Pfam; PF05770; Ins134_P3_kin; 1.
DR   Pfam; PF17927; Ins134_P3_kin_N; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EMS58471.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          36..113
FT                   /note="Inositol-tetrakisphosphate 1-kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17927"
FT   DOMAIN          112..283
FT                   /note="Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp"
FT                   /evidence="ECO:0000259|Pfam:PF05770"
SQ   SEQUENCE   411 AA;  46818 MW;  0178B4A58262EF67 CRC64;
     MEGRGGGEGS LPPFVLHGEE KSKCTLRGWV LEFKVYILAH LRKFSRFVYV NHVTACGKKG
     ISFISIDETR PLSEQGPFDI ILHKKTSKEW QRFLEDYHEV HPEVTVLDPP NAIEHLNNRQ
     SMLEEVADLN LSSFYVAKPL VVDGTSKSHE LSLAYDEASL PMLDPPLVLQ EFVNHGGILF
     KVYIIGEAIQ VVRRFSLPDV NTYDLLNNVG IYRLPRVSCA AASADHADLD PRIAELPPRP
     LLEKLGRELR GRLGLRLFNI DMIRELGAND RYYIIDINYF PGQFNTVQVG VSSLLHYPRL
     FLTITGYGKM PGYEHIFTDF LQSLGQNKYQ SLVSNAFIKQ DQHHQPTMYD IDQLSYIRCI
     TGEIQSDCKA SNLQSENLDK LKQFLAAADW THKECLHVPA FPVNLFLFVR Q
//
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