IPPK_USTMA
ID IPPK_USTMA Reviewed; 497 AA.
AC Q4P4C1; A0A0D1DTN9;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 2.
DT 25-MAY-2022, entry version 76.
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; ORFNames=UMAG_05042;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; CM003154; KIS67176.1; -; Genomic_DNA.
DR RefSeq; XP_011391331.1; XM_011393029.1.
DR AlphaFoldDB; Q4P4C1; -.
DR SMR; Q4P4C1; -.
DR STRING; 5270.UM05042P0; -.
DR EnsemblFungi; KIS67176; KIS67176; UMAG_05042.
DR GeneID; 23565042; -.
DR KEGG; uma:UMAG_05042; -.
DR VEuPathDB; FungiDB:UMAG_05042; -.
DR eggNOG; KOG4749; Eukaryota.
DR HOGENOM; CLU_033188_1_0_1; -.
DR InParanoid; Q4P4C1; -.
DR OrthoDB; 1195478at2759; -.
DR PHI-base; PHI:2384; -.
DR Proteomes; UP000000561; Chromosome 15.
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; Reference proteome; Transferase.
FT CHAIN 1..497
FT /note="Inositol-pentakisphosphate 2-kinase"
FT /id="PRO_0000110536"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 197..201
FT /note="EXKPK motif"
FT COMPBIAS 8..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 497 AA; 54729 MW; A3BA11F50D91190D CRC64;
MPPTRFQPSH QTPFKSTIST SQQSRIFHSP LQAGATANPV SISISDIDPS EWKYHAEGGK
NVLLSFDPVG GIQAGKSPFA TLTCTYALRI PKSLPSKSES NQEDEQEAEQ FTRHVVQPLL
GDATVLPKCM RIPIVTARDR HVIDMLSARI EMQRPAARRT HPARIRSEAL SYIYAVEDVA
APVSVSPSAQ RAVLCVEIKP KWGFLARIDS IPPSSPNVEI KARYSRYRMH RVAKHAAADH
AGQMSIEQFE RLYDPVDLYS CDSERKQKAI KALWDDWIDT KGKTNNLRLF WNGAVVDPQD
SVTLEAIAQF LGTDNSVQGR LKGALTQHLD KELSKRVLGE NDEWSTVSVL SRLAHLQSAL
DPLDVEGLAH LWLRRTQSHV LGQASSDVDL PPALTRNLAA AQLAAMLDSF LSGTTAEVSL
EDAVQAFLVS ASFKDCSMLL RFHQTESGVQ GETKLVDLDS KPFAKLSSMQ QTDSEVCAAF
LAWLSQLDRS PAASVAP
