KIME_ARATH
ID KIME_ARATH Reviewed; 378 AA.
AC P46086; Q9STB1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Mevalonate kinase {ECO:0000305};
DE Short=MK;
DE EC=2.7.1.36 {ECO:0000250|UniProtKB:Q03426};
GN OrderedLocusNames=At5g27450; ORFNames=F21A20.160;
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 [MRNA].
RC STRAIN=cv. Landsberg erecta; TISSUE=Leaf;
RX PubMed=7958957; DOI=10.1016/0378-1119(94)90701-3;
RA Riou C., Tourte Y., Lacroute F., Karst F.;
RT "Isolation and characterization of a cDNA encoding Arabidopsis thaliana
RT mevalonate kinase by genetic complementation in yeast.";
RL Gene 148:293-297(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10794536; DOI=10.1023/a:1006325630792;
RA Lluch M.A., Masferrer A., Arro M., Boronat A., Ferrer A.;
RT "Molecular cloning and expression analysis of the mevalonate kinase gene
RT from Arabidopsis thaliana.";
RL Plant Mol. Biol. 42:365-376(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21655959; DOI=10.1007/s00425-011-1444-6;
RA Simkin A.J., Guirimand G., Papon N., Courdavault V., Thabet I., Ginis O.,
RA Bouzid S., Giglioli-Guivarc'h N., Clastre M.;
RT "Peroxisomal localisation of the final steps of the mevalonic acid pathway
RT in planta.";
RL Planta 234:903-914(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of mevalonate to mevalonate 5-
CC phosphate, a key step in isoprenoid and cholesterol biosynthesis.
CC {ECO:0000250|UniProtKB:Q03426}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+);
CC Xref=Rhea:RHEA:17065, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:36464, ChEBI:CHEBI:58146, ChEBI:CHEBI:456216;
CC EC=2.7.1.36; Evidence={ECO:0000250|UniProtKB:Q03426};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P17256};
CC -!- ACTIVITY REGULATION: Its activity is inhibited in vitro by geranyl
CC pyrophosphate (GPP) and farnesyl pyrophosphate (FPP) that bind
CC competitively at the ATP-binding site on the enzyme.
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 1/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21655959}.
CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD45421.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X77793; CAA54820.1; -; mRNA.
DR EMBL; AF141853; AAD31719.1; -; Genomic_DNA.
DR EMBL; L77688; AAD45421.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC007123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED93688.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93689.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93690.1; -; Genomic_DNA.
DR EMBL; AY084333; AAM60916.1; -; mRNA.
DR EMBL; AY093165; AAM13164.1; -; mRNA.
DR EMBL; BT002104; AAN72115.1; -; mRNA.
DR PIR; S42088; S42088.
DR RefSeq; NP_001190411.1; NM_001203482.1.
DR RefSeq; NP_198097.1; NM_122627.6.
DR RefSeq; NP_851084.1; NM_180753.4.
DR AlphaFoldDB; P46086; -.
DR SMR; P46086; -.
DR STRING; 3702.AT5G27450.2; -.
DR PaxDb; P46086; -.
DR PRIDE; P46086; -.
DR ProteomicsDB; 237085; -.
DR EnsemblPlants; AT5G27450.1; AT5G27450.1; AT5G27450.
DR EnsemblPlants; AT5G27450.2; AT5G27450.2; AT5G27450.
DR EnsemblPlants; AT5G27450.3; AT5G27450.3; AT5G27450.
DR GeneID; 832804; -.
DR Gramene; AT5G27450.1; AT5G27450.1; AT5G27450.
DR Gramene; AT5G27450.2; AT5G27450.2; AT5G27450.
DR Gramene; AT5G27450.3; AT5G27450.3; AT5G27450.
DR KEGG; ath:AT5G27450; -.
DR Araport; AT5G27450; -.
DR TAIR; locus:2146375; AT5G27450.
DR eggNOG; KOG1511; Eukaryota.
DR HOGENOM; CLU_017814_0_1_1; -.
DR InParanoid; P46086; -.
DR OMA; NTVCTYG; -.
DR OrthoDB; 1196330at2759; -.
DR PhylomeDB; P46086; -.
DR BioCyc; MetaCyc:AT5G27450-MON; -.
DR UniPathway; UPA00057; UER00098.
DR PRO; PR:P46086; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P46086; baseline and differential.
DR Genevisible; P46086; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0004496; F:mevalonate kinase activity; ISS:UniProtKB.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 1.
DR InterPro; IPR013750; GHMP_kinase_C_dom.
DR InterPro; IPR036554; GHMP_kinase_C_sf.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS.
DR InterPro; IPR006205; Mev_gal_kin.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR43290; PTHR43290; 1.
DR Pfam; PF08544; GHMP_kinases_C; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR00549; mevalon_kin; 1.
DR PROSITE; PS00627; GHMP_KINASES_ATP; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Lipid biosynthesis; Lipid metabolism;
KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome;
KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis;
KW Sterol metabolism; Transferase.
FT CHAIN 1..378
FT /note="Mevalonate kinase"
FT /id="PRO_0000156660"
FT ACT_SITE 204
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q03426"
FT BINDING 10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17256"
FT BINDING 138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17256"
FT BINDING 143..149
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17256"
FT BINDING 149
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P17256"
FT BINDING 193
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P17256"
SQ SEQUENCE 378 AA; 40644 MW; 87E7E5C78BE53C66 CRC64;
MEVKARAPGK IILAGEHAVV HGSTAVAAAI DLYTYVTLRF PLPSAENNDR LTLQLKDISL
EFSWSLARIK EAIPYDSSTL CRSTPASCSE ETLKSIAVLV EEQNLPKEKM WLSSGISTFL
WLYTRIIGFN PATVVINSEL PYGSGLGSSA ALCVALTAAL LASSISEKTR GNGWSSLDET
NLELLNKWAF EGEKIIHGKP SGIDNTVSAY GNMIKFCSGE ITRLQSNMPL RMLITNTRVG
RNTKALVSGV SQRAVRHPDA MKSVFNAVDS ISKELAAIIQ SKDETSVTEK EERIKELMEM
NQGLLLSMGV SHSSIEAVIL TTVKHKLVSK LTGAGGGGCV LTLLPTGTVV DKVVEELESS
GFQCFTALIG GNGAQICY
