IPK1_ORYSI
ID IPK1_ORYSI Reviewed; 445 AA.
AC B8AVX5; Q01JL1;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Inositol-pentakisphosphate 2-kinase IPK1 {ECO:0000305};
DE EC=2.7.1.158 {ECO:0000305};
DE AltName: Full=Inositol-1,3,4,5,6-pentakisphosphate 2-kinase IPK1 {ECO:0000305};
DE Short=OsIPK1 {ECO:0000305};
DE AltName: Full=Ins(1,3,4,5,6)P5 2-kinase {ECO:0000305};
DE Short=InsP5 2-kinase;
GN Name=IPK1 {ECO:0000305}; ORFNames=OsI_17777 {ECO:0000312|EMBL:EEC78180.1};
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 {ECO:0000312|EMBL:EEC78180.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Guang-Lu-Ai No.4;
RX PubMed=12447439; DOI=10.1038/nature01183;
RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y.,
RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q.,
RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T.,
RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R.,
RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G.,
RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C.,
RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J.,
RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J.,
RA Li J., Hong G., Xue Y., Han B.;
RT "Sequence and analysis of rice chromosome 4.";
RL Nature 420:316-320(2002).
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: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form
CC Ins(1,2,3,4,5,6)P6 (InsP6 or phytate). Phytate is a regulator of
CC intracellular signaling, a highly abundant animal antinutrient, and a
CC phosphate store in plant seeds. Also phosphorylates Ins(1,3,4,6)P4 and
CC Ins(1,4,5,6)P4 to produce Ins(1,2,3,4,6)P5 and Ins(1,2,4,5,6)P5.
CC {ECO:0000250|UniProtKB:Q93YN9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-
CC inositol hexakisphosphate + ADP + H(+); Xref=Rhea:RHEA:20313,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733,
CC ChEBI:CHEBI:58130, ChEBI:CHEBI:456216; EC=2.7.1.158;
CC Evidence={ECO:0000250|UniProtKB:Q93YN9};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q93YN9};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q93YN9};
CC -!- DOMAIN: The EXKPK motif is conserved in inositol-pentakisphosphate 2-
CC kinases of both family 1 and 2. {ECO:0000250|UniProtKB:Q93YN9}.
CC -!- SIMILARITY: Belongs to the IPK1 type 2 family. {ECO:0000305}.
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DR EMBL; CR855168; CAH67064.1; -; Genomic_DNA.
DR EMBL; CM000129; EEC78180.1; -; Genomic_DNA.
DR AlphaFoldDB; B8AVX5; -.
DR SMR; B8AVX5; -.
DR STRING; 39946.B8AVX5; -.
DR EnsemblPlants; BGIOSGA014173-TA; BGIOSGA014173-PA; BGIOSGA014173.
DR Gramene; BGIOSGA014173-TA; BGIOSGA014173-PA; BGIOSGA014173.
DR HOGENOM; CLU_033188_1_0_1; -.
DR OMA; NCVHCGE; -.
DR Proteomes; UP000007015; Chromosome 4.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035299; F:inositol pentakisphosphate 2-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.200.110; -; 1.
DR InterPro; IPR009286; Ins_P5_2-kin.
DR InterPro; IPR043001; IP5_2-K_N_lobe.
DR PANTHER; PTHR14456; PTHR14456; 1.
DR Pfam; PF06090; Ins_P5_2-kin; 1.
PE 3: Inferred from homology;
KW ATP-binding; Kinase; Metal-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Zinc.
FT CHAIN 1..445
FT /note="Inositol-pentakisphosphate 2-kinase IPK1"
FT /id="PRO_0000431882"
FT MOTIF 162..166
FT /note="EXKPK motif"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 19..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 144..146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 162..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 196
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 341
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 363
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 406
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 410
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT BINDING 414
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q93YN9"
FT CONFLICT 205
FT /note="T -> A (in Ref. 1; CAH67064)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 49336 MW; 211AAED5EA6C5EF5 CRC64;
MEVVLHEGDA KDWVYKGEGA ANLILSYTGS SPSMLGKVLR VKKILKDKGQ PAPNCIVFSS
HEEHLWGKIP GLLESVKNDC LPQAYATIVM SQHLGANHVD GGVRVRVSKN FFELAGKNVL
DNRPAWRVNA SAIDAGADSA LLISDHTLFS GNPRGSSCIA VEIKAKCGFL PSSEYISKEN
SIKKQVTRYK MHQHLKFHLG EISKTSEYDP LDLFSGSKER IHMAIKSFFS TPQNNFRIFV
DGSLVFGGMG GGADSVHPNE TEKCLEDLSK VTGLQLSDFI ELLSEAIFKS GVLGKLLATQ
KLDDHDIEGA IHLYYNIISQ PCLVCKSITD TELLRKYSTL HSLPLDKSEK IVRDFLISAT
AKDCSLMISF RPRQSGTTDS EYDSVFLDSV NQSYDYKAYF IDLDVKPLDK MVHYFKLDQK
IVNFYTRNGE VGGDPRDPPK GCGPR
