ID A0A0D3C969_BRAOL Unreviewed; 769 AA.
AC A0A0D3C969;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Phosphatidylinositol 4-phosphate 5-kinase {ECO:0000256|PIRNR:PIRNR037274};
DE EC=2.7.1.68 {ECO:0000256|PIRNR:PIRNR037274};
GN Name=106294811 {ECO:0000313|EnsemblPlants:Bo5g013350.1};
OS Brassica oleracea var. oleracea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo5g013350.1, ECO:0000313|Proteomes:UP000032141};
RN [1] {ECO:0000313|EnsemblPlants:Bo5g013350.1, ECO:0000313|Proteomes:UP000032141}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA Chalhoub B., Sharpe A.G.;
RT "Transcriptome and methylome profiling reveals relics of genome dominance
RT in the mesopolyploid Brassica oleracea.";
RL Genome Biol. 15:R77-R77(2014).
RN [2] {ECO:0000313|EnsemblPlants:Bo5g013350.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-
CC phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
CC inositol-4,5-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:14425,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58178,
CC ChEBI:CHEBI:58456, ChEBI:CHEBI:456216; EC=2.7.1.68;
CC Evidence={ECO:0000256|PIRNR:PIRNR037274};
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 RefSeq; XP_013585932.1; XM_013730478.1.
DR RefSeq; XP_013585933.1; XM_013730479.1.
DR AlphaFoldDB; A0A0D3C969; -.
DR STRING; 109376.A0A0D3C969; -.
DR EnsemblPlants; Bo5g013350.1; Bo5g013350.1; Bo5g013350.
DR GeneID; 106294811; -.
DR Gramene; Bo5g013350.1; Bo5g013350.1; Bo5g013350.
DR KEGG; boe:106294811; -.
DR eggNOG; KOG0229; Eukaryota.
DR HOGENOM; CLU_004312_6_4_1; -.
DR OMA; MWTDGAL; -.
DR OrthoDB; 340426at2759; -.
DR Proteomes; UP000032141; Chromosome C5.
DR GO; GO:0016020; C:membrane; IEA:UniProt.
DR GO; GO:0016308; F:1-phosphatidylinositol-4-phosphate 5-kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046488; P:phosphatidylinositol metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd17302; PIPKc_AtPIP5K_like; 1.
DR Gene3D; 3.30.810.10; 2-Layer Sandwich; 1.
DR Gene3D; 2.20.110.10; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 3.
DR Gene3D; 3.30.800.10; Phosphatidylinositol Phosphate Kinase II Beta; 1.
DR InterPro; IPR003409; MORN.
DR InterPro; IPR017163; PIno-4-P-5_kinase_pln.
DR InterPro; IPR027483; PInositol-4-P-4/5-kinase_C_sf.
DR InterPro; IPR002498; PInositol-4-P-4/5-kinase_core.
DR InterPro; IPR027484; PInositol-4-P-5-kinase_N.
DR InterPro; IPR023610; PInositol-4/5-P-5/4-kinase.
DR PANTHER; PTHR23086:SF104; PHOSPHATIDYLINOSITOL 4-PHOSPHATE 5-KINASE 7; 1.
DR PANTHER; PTHR23086; PHOSPHATIDYLINOSITOL-4-PHOSPHATE 5-KINASE; 1.
DR Pfam; PF02493; MORN; 8.
DR Pfam; PF01504; PIP5K; 1.
DR PIRSF; PIRSF037274; PIP5K_plant_prd; 1.
DR SMART; SM00698; MORN; 8.
DR SMART; SM00330; PIPKc; 1.
DR SUPFAM; SSF82185; Histone H3 K4-specific methyltransferase SET7/9 N-terminal domain; 2.
DR SUPFAM; SSF56104; SAICAR synthase-like; 1.
DR PROSITE; PS51455; PIPK; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|PIRNR:PIRNR037274, ECO:0000256|PROSITE-
KW ProRule:PRU00781};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR037274};
KW Nucleotide-binding {ECO:0000256|PIRNR:PIRNR037274, ECO:0000256|PROSITE-
KW ProRule:PRU00781}; Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR037274}.
FT DOMAIN 344..765
FT /note="PIPK"
FT /evidence="ECO:0000259|PROSITE:PS51455"
FT REGION 260..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..291
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 769 AA; 87153 MW; 25DFF9E14683CE0E CRC64;
MFLDHLEAKA EMDTSILSPP EERREFSNGD FYSGEVKGLL PHGKGKYSWS DGTVYEGDWD
QGKISGKGKL IWSSGAKYEG DFSGGYLHGI GTMTSPDQSV YSGAWRMNVR HGLGRKEYCN
SDLYDGSWRE GSQEGRGSYS WTNGNRYIGS WKKGKMCGRG VMRWGNGDLF DGFWLNGCRH
GSGVYKFADG SLYFGTWSRG VKDGKGIFYP AGSKHPSLKK WCRSLEYDDT GKFVLSRSSS
IDVDELRSLS LSTVNRSLSM RTSTSGMSDH PRELTSKSAR TLGSGQSEGQ DKKNRVAYER
EYMQGVLIRE SVTTSSVDRS LKIRPPSTLS KQVSARTFLT FLTGEHNYHL MLNLQLGIRY
TVGKITPVPR RDVRGSDFGK KARTVMFFPK DGSNFTPPHK SIDFSWKDYC PMVFRNLREM
FKLDAAEYMM SICGDDGLTE ICSPGKSGSI FYLSHDDRFV IKTLKKSELK VLLRMLPRYY
KHVGDHENTL ITKFFGVHRI TLKWGKKVRF VVMGNMFCTE LKIHRRYDLK GSSHGRFTEK
IKIQEKTTLK DLDLAYEFHM DKLLREALFK QIYLDCAFLE SLQIIDYSLL LGLHFRAPGQ
LNDILEPPNA MSDQESVSSV DVGVTQELSI PPKGLLLVTH EPNSVSTAPG PHIRGSTLRA
FSVGEQEVDL ILPGTARLRV QLGVNMPAQA HHKLDEDKEE SATIELFEVY DVVVYMGIID
ILQEYNTKKK VEHKCKSLQY DPMTISVTEP TIYSKRFVNF LHKVFPEEM
//
