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ITPK5_ORYSI
ID   ITPK5_ORYSI             Reviewed;         342 AA.
AC   A0JJZ6; A2ZAJ2;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 63.
DE   RecName: Full=Inositol-tetrakisphosphate 1-kinase 5 {ECO:0000305};
DE            EC=2.7.1.134 {ECO:0000305};
DE   AltName: Full=Inositol 1,3,4-trisphosphate 5/6-kinase 5 {ECO:0000305};
DE            Short=Inositol-triphosphate 5/6-kinase 5 {ECO:0000305};
DE            Short=Ins(1,3,4)P(3) 5/6-kinase 5 {ECO:0000305};
DE            Short=OsITP5/6K-5 {ECO:0000305};
DE            Short=OsITPK5 {ECO:0000305};
DE            EC=2.7.1.159 {ECO:0000305};
GN   Name=ITPK5 {ECO:0000305}; Synonyms=ipk {ECO:0000303|PubMed:17531407};
GN   ORFNames=OsI_34771 {ECO:0000312|EMBL:EAY79626.1};
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] {ECO:0000312|EMBL:CAL69001.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17531407; DOI=10.1016/j.gene.2007.04.018;
RA   Josefsen L., Bohn L., Sorensen M.B., Rasmussen S.K.;
RT   "Characterization of a multifunctional inositol phosphate kinase from rice
RT   and barley belonging to the ATP-grasp superfamily.";
RL   Gene 397:114-125(2007).
RN   [2]
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAY79626.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AM410634; CAL69001.1; -; Genomic_DNA.
DR   EMBL; CM000135; EAY79626.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; A0JJZ6; -.
DR   SMR; A0JJZ6; -.
DR   STRING; 39946.A0JJZ6; -.
DR   HOGENOM; CLU_041857_0_0_1; -.
DR   Proteomes; UP000007015; Chromosome 10.
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   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..342
FT                   /note="Inositol-tetrakisphosphate 1-kinase 5"
FT                   /id="PRO_0000431878"
FT   BINDING         25
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT   BINDING         67
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT   BINDING         102
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         165
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT   BINDING         186..197
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         197
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT   BINDING         212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         283
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
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         298
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
FT   BINDING         300
FT                   /ligand="1D-myo-inositol 1,3,4-trisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58414"
FT                   /evidence="ECO:0000250|UniProtKB:Q9XYQ1"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13572"
SQ   SEQUENCE   342 AA;  38072 MW;  3B99D2AB5E46FB93 CRC64;
     MAGDEPLPGD GQRRRYLIGY ALAPKKQQSF IQPSLVSRAA GRGMDLVPVD PSRPLPEQGP
     FHLLIHKLYG EEWRGQLDAF SAAHPAVPVV DPPHAIDRLH NRISMLQVVS ELDVPLHAHH
     HHTFGIPSQV VVYDAAALSD SGLLAALRFP LIAKPLVADG TAKSHKMSLV YHREGLRKLR
     PPLVLQEFVN HGGVIFKVYV VGAHVTCVKR RSLPDVSSDV LQDASAEGSL SFSQVSNLPN
     ERTAQEYYDD MRLEDAIMPP TAFINDIAAA LRRALGLHLF NFDMIRDARA GDRYLVIDIN
     YFPGYAKMPG YETVLTDFFW EMVHKDDDTP NLNPNPNDED VK
 
 
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