ID   IPK1_YARLI              Reviewed;         292 AA.
AC   Q6C6Q7;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Inositol-pentakisphosphate 2-kinase;
DE            EC=2.7.1.158;
DE   AltName: Full=Inositol-1,3,4,5,6-pentakisphosphate 2-kinase;
DE   AltName: Full=Ins(1,3,4,5,6)P5 2-kinase;
DE            Short=InsP5 2-kinase;
GN   Name=IPK1; OrderedLocusNames=YALI0E07161g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Has kinase activity and phosphorylates inositol-1,3,4,5,6-
CC       pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-
CC       hexakisphosphate (InsP6), also known as phytate. {ECO:0000250}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: The EXKPK motif is conserved in inositol-pentakisphosphate 2-
CC       kinases of both family 1 and 2.
CC   -!- SIMILARITY: Belongs to the IPK1 type 1 family. {ECO:0000305}.
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DR   EMBL; CR382131; CAG79237.1; -; Genomic_DNA.
DR   RefSeq; XP_503655.1; XM_503655.1.
DR   AlphaFoldDB; Q6C6Q7; -.
DR   SMR; Q6C6Q7; -.
DR   STRING; 4952.CAG79237; -.
DR   EnsemblFungi; CAG79237; CAG79237; YALI0_E07161g.
DR   GeneID; 2912429; -.
DR   KEGG; yli:YALI0E07161g; -.
DR   VEuPathDB; FungiDB:YALI0_E07161g; -.
DR   HOGENOM; CLU_031304_0_0_1; -.
DR   InParanoid; Q6C6Q7; -.
DR   OMA; REKPRIC; -.
DR   Proteomes; UP000001300; Chromosome E.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0035299; F:inositol pentakisphosphate 2-kinase activity; IBA:GO_Central.
DR   GO; GO:0032958; P:inositol phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0052746; P:inositol phosphorylation; IBA:GO_Central.
DR   InterPro; IPR009286; Ins_P5_2-kin.
DR   PANTHER; PTHR14456; PTHR14456; 1.
DR   Pfam; PF06090; Ins_P5_2-kin; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW   Transferase.
FT   CHAIN           1..292
FT                   /note="Inositol-pentakisphosphate 2-kinase"
FT                   /id="PRO_0000110527"
FT   MOTIF           128..132
FT                   /note="EXKPK motif"
SQ   SEQUENCE   292 AA;  32942 MW;  26464BEB9FD241EA CRC64;
     MSSLPTPLPP YKWTLLTAGN ANVVYKSDET DLLLRLRRNR NAPSTAEVDE YLTGTIRPAI
     GPFLFHYTVV NLPLGFLESL PEAENLDLGE PLGLLMENLG PKPNETNVLK SHAVKINYSD
     NWESYTVELK PKWLLQSPTA PKDSINCRTC ALQLKREKPR ICPLKLFNED EQTSLQALED
     VFPGTQKQFE PLAKFFSNSE LFAEIRHMQH GDELGILGYA NYVQVPPQFV TAMTMRDVSL
     FVHVQGDSVN GKIVDADLKS VSEKRDYWAS LETDLIEGGW YEKPGTNCLL RN