ID   IPK1_CANAL              Reviewed;         361 AA.
AC   Q59KN8; A0A1D8PLT1; Q59KN1;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=CAALFM_C403330WA;
GN   ORFNames=CaO19.1439, CaO19.9013;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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}.
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; CP017626; AOW29092.1; -; Genomic_DNA.
DR   RefSeq; XP_710307.1; XM_705215.1.
DR   AlphaFoldDB; Q59KN8; -.
DR   SMR; Q59KN8; -.
DR   STRING; 237561.Q59KN8; -.
DR   PRIDE; Q59KN8; -.
DR   GeneID; 3648091; -.
DR   KEGG; cal:CAALFM_C403330WA; -.
DR   CGD; CAL0000194997; IPK1.
DR   VEuPathDB; FungiDB:C4_03330W_A; -.
DR   eggNOG; ENOG502S7VH; Eukaryota.
DR   HOGENOM; CLU_046294_1_0_1; -.
DR   InParanoid; Q59KN8; -.
DR   OMA; NDYLRHK; -.
DR   OrthoDB; 1195478at2759; -.
DR   PRO; PR:Q59KN8; -.
DR   Proteomes; UP000000559; Chromosome 4.
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   Gene3D; 3.30.200.110; -; 1.
DR   InterPro; IPR009286; Ins_P5_2-kin.
DR   InterPro; IPR043001; IP5_2-K_N_lobe.
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..361
FT                   /note="Inositol-pentakisphosphate 2-kinase"
FT                   /id="PRO_0000110522"
FT   REGION          285..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           138..142
FT                   /note="EXKPK motif"
SQ   SEQUENCE   361 AA;  42920 MW;  101A8FC6F0C0FFE5 CRC64;
     MEISKITSPE DWEYFAKGAA NILFKYTGNN DYLKRKLLRL RLLKQEEEYI STCELYDFIE
     LRCKDLFPNQ IIDIQLTVLD SNFTNKLNSQ GNKLMLNERY GLLLPNILDG DYRKISLSQK
     CQLYFNDNDQ DINSVIFEIK PKWLYDNYTD NYCRTCSLNQ LKKVPRHFCP LDLLYTETIE
     QGLNDLFAPI PQDIYAKIEK LIPLKKLTTI YFNNPDNVFQ KLKQYQKINN KNDLIKNLTS
     YSDVSQNLSL VMTLRDVGLF IKIEKFDKNN HIHTSHNNIK NVYRINDNKS NGTKDQDQEI
     GTNDEEDNDE KFLITCNIYD LDLKSKMKYK HWLKVENDLQ EIYNSSNPNW RYCIKYDQIH
     H