MIK_MAIZE
ID MIK_MAIZE Reviewed; 379 AA.
AC Q5GA22; B6TDQ7;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Inositol 3-kinase {ECO:0000305};
DE EC=2.7.1.64 {ECO:0000269|PubMed:15918884};
DE AltName: Full=Myo-inositol kinase {ECO:0000303|PubMed:15918884};
DE AltName: Full=Protein LOW PHYTIC ACID 3 {ECO:0000303|PubMed:15918884};
GN Name=MIK {ECO:0000303|PubMed:15918884};
GN Synonyms=LPA3 {ECO:0000303|PubMed:15918884};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15659640; DOI=10.1105/tpc.104.025627;
RA Brunner S., Fengler K., Morgante M., Tingey S., Rafalski A.;
RT "Evolution of DNA sequence nonhomologies among maize inbreds.";
RL Plant Cell 17:343-360(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. B73;
RX PubMed=15918884; DOI=10.1111/j.1365-313x.2005.02412.x;
RA Shi J., Wang H., Hazebroek J., Ertl D.S., Harp T.;
RT "The maize low-phytic acid 3 encodes a myo-inositol kinase that plays a
RT role in phytic acid biosynthesis in developing seeds.";
RL Plant J. 42:708-719(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
CC -!- FUNCTION: Kinase that phosphorylates myo-inositol to produce multiple
CC myo-inositol monophosphates, Ins(1)P, Ins(3)P, Ins(4)P, Ins(5)P and
CC Ins(6)P. Participates in phytic acid biosynthesis in developing seeds.
CC Phytic acid is the primary storage form of phosphorus in cereal grains
CC and other plant seeds. {ECO:0000269|PubMed:15918884}.
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:0000269|PubMed:15918884};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=53.1 uM for myo-inositol {ECO:0000269|PubMed:15918884};
CC KM=36 uM for ATP {ECO:0000269|PubMed:15918884};
CC Vmax=0.49 umol/min/mg enzyme {ECO:0000269|PubMed:15918884};
CC -!- DISRUPTION PHENOTYPE: Strong reduction in seed phytic acid, and strong
CC increase of inorganic phosphate and myo-inositol levels in seeds.
CC {ECO:0000269|PubMed:15918884}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase pfkB family.
CC {ECO:0000305}.
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DR EMBL; AY691949; AAU93530.1; -; Genomic_DNA.
DR EMBL; AY772410; AAX14809.1; -; mRNA.
DR EMBL; EU963122; ACG35240.1; -; mRNA.
DR EMBL; BT033394; ACF78399.1; -; mRNA.
DR EMBL; BT041512; ACF86517.1; -; mRNA.
DR RefSeq; NP_001105790.1; NM_001112320.1.
DR AlphaFoldDB; Q5GA22; -.
DR SMR; Q5GA22; -.
DR STRING; 4577.GRMZM2G361593_P01; -.
DR PaxDb; Q5GA22; -.
DR EnsemblPlants; Zm00001eb056490_T002; Zm00001eb056490_P002; Zm00001eb056490.
DR GeneID; 606457; -.
DR Gramene; Zm00001eb056490_T002; Zm00001eb056490_P002; Zm00001eb056490.
DR KEGG; zma:606457; -.
DR eggNOG; KOG2855; Eukaryota.
DR OrthoDB; 1230087at2759; -.
DR BioCyc; MetaCyc:MON-10821; -.
DR SABIO-RK; Q5GA22; -.
DR Proteomes; UP000007305; Chromosome 1.
DR ExpressionAtlas; Q5GA22; baseline and differential.
DR Genevisible; Q5GA22; ZM.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019140; F:inositol 3-kinase activity; IDA:UniProtKB.
DR GO; GO:0010264; P:myo-inositol hexakisphosphate biosynthetic process; IMP:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..379
FT /note="Inositol 3-kinase"
FT /id="PRO_0000431866"
FT ACT_SITE 270
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q53W83"
FT BINDING 217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q53W83"
FT BINDING 267..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q53W83"
FT BINDING 294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q53W83"
FT CONFLICT 134
FT /note="V -> M (in Ref. 3; ACG35240)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 39898 MW; 8860A4457F37376F CRC64;
MPLAAEPDDA HEERENQQLL ITTKGGPGLE GLVVGSYCHD VLIRGGRIVG ETLGGAAAFV
SNVLDAASPQ GAALNETSPF VVVAKVGHDF IYARAPASAR HPPLLCSSPT TSFHAQFSET
AASAHAPDRE LRRVRACDPI YPADLPDRRF AYGLAVGVAG EVLPETLEQM IRLCRTVLVD
AQALIRAFDG DGAVGHVALG DTPYARLLPR VAFVKASSEE APYVGVETTR RQCCVIVTEG
RDGCRLYWDG GEAHVAPFPA VQVDPTGAGD SFLAGFAAGL LWGLSATDAA LLGNFFGAAA
VSQVGVPTFH PKMLQAVKEI LEEKTRKRSS PCMNGASFTL EKSNMHNELH AALQEAAVLM
SEQQQADPAN GSGGDICSA
