IPK_ARATH
ID IPK_ARATH Reviewed; 332 AA.
AC Q8H1F7; Q8VZ62; Q9LQY8;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Isopentenyl phosphate kinase {ECO:0000303|PubMed:24327557};
DE Short=AtIPK {ECO:0000303|PubMed:26216978};
DE Short=IPK {ECO:0000303|PubMed:24327557};
DE EC=2.7.4.26 {ECO:0000269|PubMed:24327557, ECO:0000269|PubMed:26216978};
GN Name=IPK {ECO:0000303|PubMed:24327557, ECO:0000303|PubMed:26216978};
GN OrderedLocusNames=At1g26640 {ECO:0000312|Araport:AT1G26640};
GN ORFNames=T24P13.2 {ECO:0000312|EMBL:AAF87047.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=24327557; DOI=10.7554/elife.00672;
RA Dellas N., Thomas S.T., Manning G., Noel J.P.;
RT "Discovery of a metabolic alternative to the classical mevalonate
RT pathway.";
RL Elife 2:E00672-E00672(2013).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=26216978; DOI=10.1073/pnas.1504798112;
RA Henry L.K., Gutensohn M., Thomas S.T., Noel J.P., Dudareva N.;
RT "Orthologs of the archaeal isopentenyl phosphate kinase regulate terpenoid
RT production in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:10050-10055(2015).
CC -!- FUNCTION: Catalyzes the formation of isopentenyl diphosphate (IPP), the
CC universal five-carbon isoprenoid building block of all natural
CC isoprenoids (PubMed:24327557, PubMed:26216978). Acts in parallel with
CC the mevalonate (MVA) pathway and plays an important role in regulating
CC the formation of both MVA and methylerythritol phosphate (MEP) pathway-
CC derived terpenoid compounds by controlling the ratio of isopentenyl
CC phosphate (IP) and dimethylallyl phosphate (DMAP) to isopentenyl
CC diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Controls the
CC levels of IP and DMAP that are competitive inhibitors of the farnesyl
CC diphosphate synthase. Regulates the production of farnesyl diphosphate-
CC derived terpenoids in the cytosol, and geranyl diphosphate-derived
CC compounds in plastids (PubMed:26216978). {ECO:0000269|PubMed:24327557,
CC ECO:0000269|PubMed:26216978}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + isopentenyl phosphate = ADP + isopentenyl diphosphate;
CC Xref=Rhea:RHEA:33963, ChEBI:CHEBI:30616, ChEBI:CHEBI:65078,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:456216; EC=2.7.4.26;
CC Evidence={ECO:0000269|PubMed:24327557, ECO:0000269|PubMed:26216978};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.79 uM for isopentenyl phosphate {ECO:0000269|PubMed:24327557};
CC KM=32 uM for isopentenyl phosphate {ECO:0000269|PubMed:26216978};
CC KM=33 uM for dimethylallyl diphosphate {ECO:0000269|PubMed:26216978};
CC KM=220 uM for geranyl phosphate {ECO:0000269|PubMed:26216978};
CC Note=kcat is 1.9 sec(-1) with isopentenyl phosphate
CC (PubMed:24327557). kcat is 3.7 sec(-1) with isopentenyl phosphate
CC (PubMed:26216978). kcat is 2.7 sec(-1) with dimethylallyl diphosphate
CC (PubMed:26216978). kcat is 0.0039 sec(-1) with geranyl phosphate
CC (PubMed:26216978). {ECO:0000269|PubMed:24327557,
CC ECO:0000269|PubMed:26216978};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:26216978}.
CC -!- SIMILARITY: Belongs to the isopentenyl phosphate kinase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF87047.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006535; AAF87047.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE30713.1; -; Genomic_DNA.
DR EMBL; AY065221; AAL38697.1; -; mRNA.
DR EMBL; AY150412; AAN12957.1; -; mRNA.
DR PIR; E86393; E86393.
DR RefSeq; NP_173986.2; NM_102426.6.
DR AlphaFoldDB; Q8H1F7; -.
DR SMR; Q8H1F7; -.
DR STRING; 3702.AT1G26640.1; -.
DR iPTMnet; Q8H1F7; -.
DR PaxDb; Q8H1F7; -.
DR PRIDE; Q8H1F7; -.
DR ProteomicsDB; 248474; -.
DR DNASU; 839204; -.
DR EnsemblPlants; AT1G26640.1; AT1G26640.1; AT1G26640.
DR GeneID; 839204; -.
DR Gramene; AT1G26640.1; AT1G26640.1; AT1G26640.
DR KEGG; ath:AT1G26640; -.
DR Araport; AT1G26640; -.
DR TAIR; locus:2200580; AT1G26640.
DR eggNOG; ENOG502QQ1X; Eukaryota.
DR HOGENOM; CLU_070213_0_0_1; -.
DR InParanoid; Q8H1F7; -.
DR OMA; SIRCIVK; -.
DR OrthoDB; 1271584at2759; -.
DR PhylomeDB; Q8H1F7; -.
DR BRENDA; 2.7.4.26; 399.
DR PRO; PR:Q8H1F7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8H1F7; baseline and differential.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0102043; F:isopentenyl phosphate kinase activity; IDA:UniProtKB.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IDA:UniProtKB.
DR CDD; cd04241; AAK_FomA-like; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR024192; Fosfomycin_R_FomA-type.
DR PANTHER; PTHR43654:SF1; PTHR43654:SF1; 1.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF016496; Kin_FomA; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Isoprene biosynthesis; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..332
FT /note="Isopentenyl phosphate kinase"
FT /id="PRO_0000444195"
FT BINDING 18..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT BINDING 202
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT BINDING 223
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT BINDING 228..233
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT BINDING 279
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT BINDING 283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT SITE 27
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 240
FT /note="V -> L (in Ref. 3; AAL38697)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 332 AA; 35676 MW; 4DC6579EDD15E7C7 CRC64;
MELNISESRS RSIRCIVKLG GAAITCKNEL EKIHDENLEV VACQLRQAML EGSAPSKVIG
MDWSKRPGSS EISCDVDDIG DQKSSEFSKF VVVHGAGSFG HFQASRSGVH KGGLEKPIVK
AGFVATRISV TNLNLEIVRA LAREGIPTIG MSPFSCGWST SKRDVASADL ATVAKTIDSG
FVPVLHGDAV LDNILGCTIL SGDVIIRHLA DHLKPEYVVF LTDVLGVYDR PPSPSEPDAV
LLKEIAVGED GSWKVVNPLL EHTDKKVDYS VAAHDTTGGM ETKISEAAMI AKLGVDVYIV
KAATTHSQRA LNGDLRDSVP EDWLGTIIRF SK
