ID   IPPK_CRYNB              Reviewed;         414 AA.
AC   P0CO35; Q55U88; Q5KI57;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 28.
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=CNBD2180;
OS   Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS   (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=283643;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-3501A;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
CC   -!- FUNCTION: Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form
CC       Ins(1,2,3,4,5,6)P6 (InsP6 or 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   -!- 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 2 family. {ECO:0000305}.
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DR   EMBL; AAEY01000019; EAL21524.1; -; Genomic_DNA.
DR   RefSeq; XP_776171.1; XM_771078.1.
DR   AlphaFoldDB; P0CO35; -.
DR   SMR; P0CO35; -.
DR   EnsemblFungi; AAW42830; AAW42830; CND04140.
DR   EnsemblFungi; EAL21524; EAL21524; CNBD2180.
DR   GeneID; 4935607; -.
DR   KEGG; cnb:CNBD2180; -.
DR   VEuPathDB; FungiDB:CNBD2180; -.
DR   HOGENOM; CLU_033188_1_0_1; -.
DR   Proteomes; UP000001435; Chromosome 4.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; Transferase.
FT   CHAIN           1..414
FT                   /note="Inositol-pentakisphosphate 2-kinase"
FT                   /id="PRO_0000410122"
FT   MOTIF           150..154
FT                   /note="EXKPK motif"
SQ   SEQUENCE   414 AA;  46804 MW;  51475B11951CB623 CRC64;
     MNDGNHYRPA ISPNPSADTQ PSDWAYIAEG GAHIVFSYQG RSKTYATRAL RVRKPSATTE
     PLAQAEENDL FGQWRRNILP KLLPRQLLTT SREVILEDRW YKELLAMVDV VRPDQRKSGI
     DFAAKGDRRG VLLEDLTSSE DDGAIAVAIE IKPKWGFLPC TEHLHPPESV SIKSHVSRFR
     LHQHFRGCSD DPPYDPLDLF SGDKMRMRTA LDGLWTMWEI SRGKVNNWKV FVGGKEISPD
     DLQNGLLPIG GDDFVTKITQ LTLDTLQTSF ALPLLKNLQQ NLDPIDISSL AALFQAEYPN
     SPPFDPDLIP DVSAVELNGF VDIYISDPQA GQRMDSWSLR ERIIAYALSA IFKDCSLFIR
     GFLKHAEDGV WRLVSGSDSV KVIDLDLKPI KNIQKWAETD EKVWKYWLET KGAR