MIK_ARATH
ID MIK_ARATH Reviewed; 353 AA.
AC Q93Z01; Q9LUY8;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Inositol 3-kinase {ECO:0000305};
DE EC=2.7.1.64 {ECO:0000250|UniProtKB:Q5GA22};
DE AltName: Full=Myo-inositol kinase {ECO:0000305};
DE Short=AtMIK {ECO:0000303|PubMed:21698461};
GN OrderedLocusNames=At5g58730 {ECO:0000312|Araport:AT5G58730};
GN ORFNames=MZN1.17 {ECO:0000312|EMBL:BAA97341.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21698461; DOI=10.1007/s00438-011-0631-2;
RA Kim S.I., Tai T.H.;
RT "Identification of genes necessary for wild-type levels of seed phytic acid
RT in Arabidopsis thaliana using a reverse genetics approach.";
RL Mol. Genet. Genomics 286:119-133(2011).
CC -!- FUNCTION: Kinase that phosphorylates myo-inositol to produce multiple
CC myo-inositol monophosphates. Participates in phytic acid biosynthesis
CC in developing seeds. Phytic acid is the primary storage form of
CC phosphorus in cereal grains and other plant seeds.
CC {ECO:0000269|PubMed:21698461}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + myo-inositol = 1D-myo-inositol 3-phosphate + ADP + H(+);
CC Xref=Rhea:RHEA:21804, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58401, ChEBI:CHEBI:456216;
CC EC=2.7.1.64; Evidence={ECO:0000250|UniProtKB:Q5GA22};
CC -!- DISRUPTION PHENOTYPE: Low inositol hexakisphosphate (phytate) levels in
CC seed tissue. {ECO:0000269|PubMed:21698461}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase pfkB family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA97341.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB020755; BAA97341.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED97092.1; -; Genomic_DNA.
DR EMBL; AY058873; AAL24260.1; -; mRNA.
DR EMBL; AY103302; AAM65354.1; -; mRNA.
DR EMBL; AY084481; AAM61052.1; -; mRNA.
DR RefSeq; NP_200681.1; NM_125260.3.
DR AlphaFoldDB; Q93Z01; -.
DR SMR; Q93Z01; -.
DR IntAct; Q93Z01; 1.
DR STRING; 3702.AT5G58730.1; -.
DR iPTMnet; Q93Z01; -.
DR PaxDb; Q93Z01; -.
DR PRIDE; Q93Z01; -.
DR ProteomicsDB; 238291; -.
DR EnsemblPlants; AT5G58730.1; AT5G58730.1; AT5G58730.
DR GeneID; 835987; -.
DR Gramene; AT5G58730.1; AT5G58730.1; AT5G58730.
DR KEGG; ath:AT5G58730; -.
DR Araport; AT5G58730; -.
DR TAIR; locus:2178883; AT5G58730.
DR eggNOG; KOG2855; Eukaryota.
DR HOGENOM; CLU_061466_0_0_1; -.
DR InParanoid; Q93Z01; -.
DR OMA; ESGFFHL; -.
DR OrthoDB; 1230087at2759; -.
DR PhylomeDB; Q93Z01; -.
DR BioCyc; ARA:AT5G58730-MON; -.
DR PRO; PR:Q93Z01; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q93Z01; baseline and differential.
DR Genevisible; Q93Z01; AT.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019140; F:inositol 3-kinase activity; ISS:UniProtKB.
DR GO; GO:0010264; P:myo-inositol hexakisphosphate biosynthetic process; IMP:TAIR.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR031094; MIK.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR43085:SF13; PTHR43085:SF13; 1.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..353
FT /note="Inositol 3-kinase"
FT /id="PRO_0000431868"
FT ACT_SITE 250
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q53W83"
FT BINDING 197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q53W83"
FT BINDING 247..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q53W83"
FT BINDING 274
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q53W83"
SQ SEQUENCE 353 AA; 38646 MW; 6195D215E37530BF CRC64;
MTLNPPPSQQ TSHSPRRIPN RRVLIVGNYC HDVLIQNGSV VAETLGGAAS FISNVLDSSS
VSCDLVSKVG HDFRYEVTHS PIVAPEKETT VFEAYFDLGI DGIGHADRVL KRVSACDPIL
PSDIPDSRFD FGMAVGVGGE ILPETLEKMV EICDVVAVDI QALIRVFDPV DGAVKLVDLK
ESGFYHILHR IGFLKASSDE ALFMDVEQMK HLCCVVVTNG EKGCRIYHKD DEMTVPPFLA
KQVDPTGAGD SFLGGLIVGL VEGLTVPDAA LLGNLFGSIT VEHIGQPKFD LMMLQKVKDE
VQRRKKQCNI SSSHNNDHNE FHERLSPARF SCVDSQLQPK LLVNGHSCDD RSL
