ID   IPK1_KLULA              Reviewed;         266 AA.
AC   Q6CNG8;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
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=KLLA0E12705g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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; CR382125; CAG99608.1; -; Genomic_DNA.
DR   RefSeq; XP_454521.1; XM_454521.1.
DR   AlphaFoldDB; Q6CNG8; -.
DR   STRING; 28985.XP_454521.1; -.
DR   EnsemblFungi; CAG99608; CAG99608; KLLA0_E12673g.
DR   GeneID; 2894555; -.
DR   KEGG; kla:KLLA0_E12673g; -.
DR   eggNOG; ENOG502S05I; Eukaryota.
DR   HOGENOM; CLU_046294_0_0_1; -.
DR   InParanoid; Q6CNG8; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0032958; P:inositol phosphate biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:EnsemblFungi.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   InterPro; IPR009286; Ins_P5_2-kin.
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..266
FT                   /note="Inositol-pentakisphosphate 2-kinase"
FT                   /id="PRO_0000110525"
FT   MOTIF           125..129
FT                   /note="EXKPK motif"
SQ   SEQUENCE   266 AA;  31066 MW;  B1577CF21BF972DF CRC64;
     MTLLFVGRGN ANVCYLLSGE VYRISLRHQK LSRNNAYVQD NFQFIDSKIR SLPMLADVVV
     SMRLEEVFVD TKWINVLKDE NILIDDSHMQ CIVMPLLHAK DSTCEQLDHF NQIYRCSLND
     AITWEFKPKW LYQSSDYCRN CTHNSLKGRD IEYCFLHDPE LIIETLFAGR QVPEEFLDDI
     LQYLQSSDSI TQRLYAAQRF VKDDLSTLMT LRDVTCFLTW SRNTRSVKAT IIDVDQKPAN
     KLRHWQSTES ALASFPGKKK AHFNHQ