IPK1_YEAST
ID IPK1_YEAST Reviewed; 281 AA.
AC Q06667; D6VSU4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
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; Synonyms=GSL1; OrderedLocusNames=YDR315C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=10390371; DOI=10.1126/science.285.5424.96;
RA York J.D., Odom A.R., Murphy R., Ives E.B., Wente S.R.;
RT "A phospholipase C-dependent inositol polyphosphate kinase pathway required
RT for efficient messenger RNA export.";
RL Science 285:96-100(1999).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASN-10 AND CYS-139, AND
RP 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).
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.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20314;
CC Evidence={ECO:0000305|PubMed:10960485};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=644 nM for IP5 {ECO:0000269|PubMed:10960485};
CC KM=62.8 uM for ATP {ECO:0000269|PubMed:10960485};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10390371}.
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; U28374; AAB64751.1; -; Genomic_DNA.
DR EMBL; AY557740; AAS56066.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12154.1; -; Genomic_DNA.
DR PIR; S61201; S61201.
DR RefSeq; NP_010601.3; NM_001180623.3.
DR AlphaFoldDB; Q06667; -.
DR SMR; Q06667; -.
DR BioGRID; 32368; 473.
DR DIP; DIP-1388N; -.
DR IntAct; Q06667; 4.
DR MINT; Q06667; -.
DR STRING; 4932.YDR315C; -.
DR PaxDb; Q06667; -.
DR PRIDE; Q06667; -.
DR EnsemblFungi; YDR315C_mRNA; YDR315C; YDR315C.
DR GeneID; 851910; -.
DR KEGG; sce:YDR315C; -.
DR SGD; S000002723; IPK1.
DR VEuPathDB; FungiDB:YDR315C; -.
DR eggNOG; ENOG502S05I; Eukaryota.
DR HOGENOM; CLU_046294_1_0_1; -.
DR InParanoid; Q06667; -.
DR OMA; NDYLRHK; -.
DR BioCyc; MetaCyc:YDR315C-MON; -.
DR BioCyc; YEAST:YDR315C-MON; -.
DR Reactome; R-SCE-1855167; Synthesis of pyrophosphates in the cytosol.
DR Reactome; R-SCE-1855191; Synthesis of IPs in the nucleus.
DR PRO; PR:Q06667; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06667; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0035299; F:inositol pentakisphosphate 2-kinase activity; IDA:SGD.
DR GO; GO:0032958; P:inositol phosphate biosynthetic process; IDA:SGD.
DR GO; GO:0052746; P:inositol phosphorylation; IBA:GO_Central.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IMP:SGD.
DR InterPro; IPR009286; Ins_P5_2-kin.
DR PANTHER; PTHR14456; PTHR14456; 2.
DR Pfam; PF06090; Ins_P5_2-kin; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..281
FT /note="Inositol-pentakisphosphate 2-kinase"
FT /id="PRO_0000110528"
FT MOTIF 123..127
FT /note="EXKPK motif"
FT MUTAGEN 10
FT /note="N->D: More than 95% loss of activity."
FT /evidence="ECO:0000269|PubMed:10960485"
FT MUTAGEN 139
FT /note="C->Y: More than 95% loss of activity."
FT /evidence="ECO:0000269|PubMed:10960485"
SQ SEQUENCE 281 AA; 32918 MW; 43CD1ACC4161DCD1 CRC64;
MQVIGRGGAN ILIDYGDPTW LWRCCIRWPD LLSSNNSYTI KNISYIKDYV EPLLHGLLCP
MYLIDVDIEA IRPILSDFIL NLDDKVVKVI KIKNLTNNTS NLILNNHFLK SYCSQNLQTV
ILELKPKWLY YDTDYCRNCT HNAFKGRGTK YCYNQLLMNP AHLELIFGEC NIFPVKFKDA
MHEYLRNDNN IFKILYDLQK KLTKNTTPIS DIKSINDVND EHLLLMTLRD VTCFIEWNSA
ENALHVNIID VDLKPKEKWT HWTKTYSQLT SSQKIYHTSN K
