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   07-SEP-2016, entry version 121.
DE   RecName: Full=Phosphomevalonate kinase {ECO:0000305};
DE            EC=2.7.4.2 {ECO:0000305};
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|TAIR:AT1G31910};
GN   ORFNames=F5M6.9 {ECO:0000312|EMBL:AAG50716.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Hayashizaki Y., 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.,
RA   Ginis O., Bouzid S., Giglioli-Guivarc'h N., Clastre M.;
RT   "Peroxisomal localisation of the final steps of the mevalonic acid
RT   pathway 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
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.,
RA   Meinnel T., 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).
CC   -!- CATALYTIC ACTIVITY: ATP + (R)-5-phosphomevalonate = ADP + (R)-5-
CC       diphosphomevalonate. {ECO:0000305}.
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate
CC       biosynthesis via mevalonate pathway; isopentenyl diphosphate from
CC       (R)-mevalonate: step 2/3. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome.
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         Note=No experimental confirmation available. {ECO:0000305};
CC   -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase
CC       subfamily. {ECO:0000305}.
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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_102927.2. [Q9C6T1-1]
DR   UniGene; At.17280; -.
DR   STRING; 3702.AT1G31910.1; -.
DR   iPTMnet; Q9C6T1; -.
DR   EnsemblPlants; AT1G31910.1; AT1G31910.1; AT1G31910. [Q9C6T1-1]
DR   EnsemblPlants; AT1G31910.2; AT1G31910.2; AT1G31910. [Q9C6T1-2]
DR   GeneID; 840081; -.
DR   KEGG; ath:AT1G31910; -.
DR   TAIR; AT1G31910; -.
DR   eggNOG; KOG4519; Eukaryota.
DR   eggNOG; COG3890; LUCA.
DR   KO; K00938; -.
DR   OMA; GENCKPE; -.
DR   OrthoDB; EOG09360943; -.
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; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004631; F:phosphomevalonate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 2.
DR   Gene3D; 3.30.70.890; -; 2.
DR   InterPro; IPR016005; Erg8.
DR   InterPro; IPR013750; GHMP_kinase_C_dom.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR   InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR   Pfam; PF08544; GHMP_kinases_C; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   PIRSF; PIRSF017288; PMK_GHMP_euk; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   TIGRFAMs; TIGR01219; Pmev_kin_ERG8; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; ATP-binding; Complete proteome;
KW   Kinase; Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW   Peroxisome; Reference proteome; Steroid biosynthesis;
KW   Steroid metabolism; Sterol biosynthesis; Sterol metabolism;
KW   Transferase.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22223895}.
FT   CHAIN         2    505       Phosphomevalonate kinase.
FT                                /FTId=PRO_0000435609.
FT   NP_BIND     177    187       ATP. {ECO:0000255}.
FT   MOTIF        57     65       Peroxisomal targeting signal PTS2.
FT                                {ECO:0000305|PubMed:21655959}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:22223895}.
FT   VAR_SEQ     418    450       IEPESQTQLLDSTMSAEGVLLAGVPGAGGFDAI -> NLNS
FT                                IHDIRVPQIPHLEQIDFIIIDLEGPWNCR (in isoform
FT                                2).
FT                                /FTId=VSP_058117.
FT   VAR_SEQ     451    505       Missing (in isoform 2).
FT                                /FTId=VSP_058118.
FT   CONFLICT     44     44       E -> G (in Ref. 3; BAD43274).
FT                                {ECO:0000305}.
FT   CONFLICT     54     54       K -> N (in Ref. 3; BAD43274).
FT                                {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
//