ID PMK_ARATH Reviewed; 505 AA. AC Q9C6T1; Q681V6; Q682Q9; DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 29-MAY-2024, entry version 161. DE RecName: Full=Phosphomevalonate kinase, peroxisomal {ECO:0000305}; DE EC=2.7.4.2 {ECO:0000269|PubMed:24327557}; DE AltName: Full=5-phosphomevalonate kinase {ECO:0000303|PubMed:21655959}; DE Short=AtPMK {ECO:0000303|PubMed:21655959}; GN Name=PMK {ECO:0000303|PubMed:21655959}; GN OrderedLocusNames=At1g31910 {ECO:0000312|Araport:AT1G31910}; GN ORFNames=F5M6.9 {ECO:0000312|EMBL:AAG50716.1}; 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] (ISOFORMS 1 AND 2). RC STRAIN=cv. Columbia; RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K., RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., RA Shinozaki K.; RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [4] 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). RN [5] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [6] RP 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). CC -!- CATALYTIC ACTIVITY: CC Reaction=(R)-5-phosphomevalonate + ATP = (R)-5-diphosphomevalonate + CC ADP; Xref=Rhea:RHEA:16341, ChEBI:CHEBI:30616, ChEBI:CHEBI:57557, CC ChEBI:CHEBI:58146, ChEBI:CHEBI:456216; EC=2.7.4.2; CC Evidence={ECO:0000269|PubMed:24327557}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=11.8 uM for (R)-5-phosphomevalonate {ECO:0000269|PubMed:24327557}; CC Note=kcat is 20.9 sec(-1) with (R)-5-phosphomevalonate. CC {ECO:0000269|PubMed:24327557}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: CC step 2/3. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:21655959}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9C6T1-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9C6T1-2; Sequence=VSP_058117, VSP_058118; CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase CC subfamily. {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; AC079041; AAG50716.1; -; Genomic_DNA. DR EMBL; CP002684; AEE31414.1; -; Genomic_DNA. DR EMBL; CP002684; AEE31415.1; -; Genomic_DNA. DR EMBL; AK175299; BAD43062.1; -; mRNA. DR EMBL; AK175308; BAD43071.1; -; mRNA. DR EMBL; AK175511; BAD43274.1; -; mRNA. DR EMBL; AK176723; BAD44486.1; -; mRNA. DR EMBL; AK176889; BAD44652.1; -; mRNA. DR EMBL; AK221797; BAD93949.1; -; mRNA. DR PIR; C86443; C86443. DR RefSeq; NP_001185124.1; NM_001198195.1. [Q9C6T1-2] DR RefSeq; NP_174473.1; NM_102927.3. [Q9C6T1-1] DR AlphaFoldDB; Q9C6T1; -. DR STRING; 3702.Q9C6T1; -. DR iPTMnet; Q9C6T1; -. DR PaxDb; 3702-AT1G31910-1; -. DR ProteomicsDB; 234854; -. [Q9C6T1-1] DR EnsemblPlants; AT1G31910.1; AT1G31910.1; AT1G31910. [Q9C6T1-1] DR EnsemblPlants; AT1G31910.2; AT1G31910.2; AT1G31910. [Q9C6T1-2] DR GeneID; 840081; -. DR Gramene; AT1G31910.1; AT1G31910.1; AT1G31910. [Q9C6T1-1] DR Gramene; AT1G31910.2; AT1G31910.2; AT1G31910. [Q9C6T1-2] DR KEGG; ath:AT1G31910; -. DR Araport; AT1G31910; -. DR TAIR; AT1G31910; -. DR eggNOG; KOG4519; Eukaryota. DR HOGENOM; CLU_022059_1_0_1; -. DR InParanoid; Q9C6T1; -. DR OMA; LVIHRTM; -. DR OrthoDB; 991613at2759; -. DR PhylomeDB; Q9C6T1; -. DR BioCyc; ARA:AT1G31910-MONOMER; -. DR UniPathway; UPA00057; UER00099. DR PRO; PR:Q9C6T1; -. DR Proteomes; UP000006548; Chromosome 1. DR ExpressionAtlas; Q9C6T1; baseline and differential. DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004631; F:phosphomevalonate kinase activity; IDA:UniProtKB. DR GO; GO:0006696; P:ergosterol biosynthetic process; IEA:TreeGrafter. DR GO; GO:0010142; P:farnesyl diphosphate biosynthetic process, mevalonate pathway; IEA:TreeGrafter. DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IDA:UniProtKB. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1. DR InterPro; IPR016005; Erg8. DR InterPro; IPR013750; GHMP_kinase_C_dom. DR InterPro; IPR036554; GHMP_kinase_C_sf. DR InterPro; IPR006204; GHMP_kinase_N_dom. DR InterPro; IPR035102; Phosphomevalonate_kinase. DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF. DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr. DR NCBIfam; TIGR01219; Pmev_kin_ERG8; 1. DR PANTHER; PTHR31814; -; 1. DR PANTHER; PTHR31814:SF2; PHOSPHOMEVALONATE KINASE; 1. DR Pfam; PF08544; GHMP_kinases_C; 1. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PIRSF; PIRSF017288; PMK_GHMP_euk; 1. DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; ATP-binding; Kinase; Lipid biosynthesis; KW Lipid metabolism; Nucleotide-binding; Peroxisome; Reference proteome; KW Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; KW Sterol metabolism; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22223895" FT CHAIN 2..505 FT /note="Phosphomevalonate kinase, peroxisomal" FT /id="PRO_0000435609" FT MOTIF 57..65 FT /note="Peroxisomal targeting signal PTS2" FT /evidence="ECO:0000305|PubMed:21655959" FT BINDING 177..187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22223895" FT VAR_SEQ 418..450 FT /note="IEPESQTQLLDSTMSAEGVLLAGVPGAGGFDAI -> NLNSIHDIRVPQIPH FT LEQIDFIIIDLEGPWNCR (in isoform 2)" FT /id="VSP_058117" FT VAR_SEQ 451..505 FT /note="Missing (in isoform 2)" FT /id="VSP_058118" FT CONFLICT 44 FT /note="E -> G (in Ref. 3; BAD43274)" FT /evidence="ECO:0000305" FT CONFLICT 54 FT /note="K -> N (in Ref. 3; BAD43274)" FT /evidence="ECO:0000305" SQ SEQUENCE 505 AA; 54409 MW; B1CBA6CA338B3D63 CRC64; MAVVASAPGK VLMTGGYLVL EKPNAGLVLS TNARFYAIVK PINEEVKPES WAWKWTDVKL TSPQLSRESM YKLSLNHLTL QSVSASDSRN PFVEHAIQYA IAAAHLATEK DKESLHKLLL QGLDITILGS NDFYSYRNQI ESAGLPLTPE SLGTLAPFAS ITFNAAESNG ANSKPEVAKT GLGSSAAMTT AVVAALLHYL GVVDLSDPCK EGKFGCSDLD VIHMIAQTSH CLAQGKVGSG FDVSCAVYGS QRYVRFSPEV LSFAQVAVTG LPLNEVIGTI LKGKWDNKRT EFSLPPLMNL FLGEPGSGGS STPSMVGAVK KWQMSDPEKA RENWQNLSDA NLELETKLND LSKLAKDHWD VYLRVIKSCS VLTSEKWVLH ATEPINEAII KELLEAREAM LRIRILMRQM GEAASVPIEP ESQTQLLDST MSAEGVLLAG VPGAGGFDAI FAITLGDSGT KLTQAWSSHN VLALLVREDP HGVCLESGDP RTTCITSGVS SIHLE //