IPK1_SCHPO
ID IPK1_SCHPO Reviewed; 640 AA.
AC Q9USK0; P78889;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Inositol-pentakisphosphate 2-kinase;
DE EC=2.7.1.158 {ECO:0000269|PubMed:10960485};
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=SPCC4B3.10c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 358-640.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10960485; DOI=10.1074/jbc.m007586200;
RA Ives E.B., Nichols J., Wente S.R., York J.D.;
RT "Biochemical and functional characterization of inositol 1,3,4,5, 6-
RT pentakisphosphate 2-kinases.";
RL J. Biol. Chem. 275:36575-36583(2000).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-372, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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 ECO:0000269|PubMed:10960485}.
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 Evidence={ECO:0000269|PubMed:10960485};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.644 uM for 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
CC {ECO:0000269|PubMed:10960485};
CC KM=62.8 uM for ATP {ECO:0000269|PubMed:10960485};
CC Vmax=0.02 umol/min/mg enzyme with 1D-myo-inositol 1,3,4,5,6-
CC pentakisphosphate as substrate (at pH 7.5 and 37 degrees Celsius)
CC {ECO:0000269|PubMed:10960485};
CC pH dependence:
CC Optimum pH is 6.7-7.5 (at 30 degrees Celsius).
CC {ECO:0000269|PubMed:10960485};
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; CU329672; CAB60684.1; -; Genomic_DNA.
DR EMBL; D89240; BAA13901.1; -; mRNA.
DR PIR; T43146; T43146.
DR PIR; T50438; T50438.
DR RefSeq; NP_588080.1; NM_001023072.2.
DR AlphaFoldDB; Q9USK0; -.
DR SMR; Q9USK0; -.
DR BioGRID; 275371; 2.
DR STRING; 4896.SPCC4B3.10c.1; -.
DR iPTMnet; Q9USK0; -.
DR MaxQB; Q9USK0; -.
DR PaxDb; Q9USK0; -.
DR PRIDE; Q9USK0; -.
DR EnsemblFungi; SPCC4B3.10c.1; SPCC4B3.10c.1:pep; SPCC4B3.10c.
DR GeneID; 2538790; -.
DR KEGG; spo:SPCC4B3.10c; -.
DR PomBase; SPCC4B3.10c; ipk1.
DR VEuPathDB; FungiDB:SPCC4B3.10c; -.
DR eggNOG; ENOG502S7VH; Eukaryota.
DR HOGENOM; CLU_437524_0_0_1; -.
DR OMA; WVVCRTC; -.
DR BRENDA; 2.7.1.158; 5613.
DR Reactome; R-SPO-1855167; Synthesis of pyrophosphates in the cytosol.
DR Reactome; R-SPO-1855191; Synthesis of IPs in the nucleus.
DR PRO; PR:Q9USK0; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; ISS:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035299; F:inositol pentakisphosphate 2-kinase activity; IDA:PomBase.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IDA:PomBase.
DR GO; GO:0052746; P:inositol phosphorylation; IBA:GO_Central.
DR Gene3D; 1.20.1270.60; -; 1.
DR Gene3D; 3.30.200.110; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
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.
DR SUPFAM; SSF103657; SSF103657; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..640
FT /note="Inositol-pentakisphosphate 2-kinase"
FT /id="PRO_0000110526"
FT REGION 304..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 491..495
FT /note="EXKPK motif"
FT MOD_RES 372
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 640 AA; 72766 MW; F7231A833967CC36 CRC64;
MPLKNYTKTT SKKEPKQLDI AASDQQIEQW SDQIHKLDKA IRSTIDNSRL FYDAWRCMVC
IAPSVTASWI SLYRQLPPEK QPAASVGTLV DWNKALERQR REVLLALQNF HVIVIAPCKE
VKGYVKKAVE MIKRRDKKVK ELEKIQKELL VVYELPDPET KKSKIKALQS QLVRVNGELD
DLQKHLTLSF PTLIAKSRVF FGQLMKHFYC LQLQMFRKMH NIVRPWDCFQ DDIPQTWLVE
FSSVCQAAES ISLIAVNNNR PPVELPKSGD VLSNREWEAG KIDAMNSLIA QNLHTSASQV
SLSPMASTAS SSVTNSPVDT HTPSTPIMSR PPSMKALSSG VESQDESVAS SNFQVPIISN
PLFKSPAPYS PTSVISNHSS TGKSLVISEW AYLASGSANV VFEYVGKNPY FQDKVIRLRR
RGQVFTTEQV YEYYQNVIYP LFAGMESFLI EVFLQPVTRD FLLAAQNASG IYLNLNEQYC
LVMKDLKDGI EMKPKWLTQS PAAPPDWVVC RTCALSRMRG RPVGFCPLQL DFNNWPKFLC
CLQGFVSPDI AMRLFQSGIL RKLRDLQEQY SRTDVALAMT LRDVTLYIGK DHITLLDLDP
KDMNTKMSKW ERDERNLIEG GWYYGRGMKS TDKACRSSIK
