ID   MVD1_HUMAN              Reviewed;         400 AA.
AC   P53602; Q53Y65;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 189.
DE   RecName: Full=Diphosphomevalonate decarboxylase;
DE            EC=4.1.1.33 {ECO:0000269|PubMed:18823933, ECO:0000269|PubMed:8626466, ECO:0000269|PubMed:9392419};
DE   AltName: Full=Mevalonate (diphospho)decarboxylase;
DE            Short=MDDase;
DE   AltName: Full=Mevalonate pyrophosphate decarboxylase;
GN   Name=MVD; Synonyms=MPD {ECO:0000303|PubMed:14972328};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, SUBUNIT, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=8626466; DOI=10.1074/jbc.271.14.7895;
RA   Toth M.J., Huwyler L.;
RT   "Molecular cloning and expression of the cDNAs encoding human and yeast
RT   mevalonate pyrophosphate decarboxylase.";
RL   J. Biol. Chem. 271:7895-7898(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, AND FUNCTION.
RX   PubMed=9392419;
RA   Hinson D.D., Chambliss K.L., Toth M.J., Tanaka R.D., Gibson K.M.;
RT   "Post-translational regulation of mevalonate kinase by intermediates of the
RT   cholesterol and nonsterol isoprene biosynthetic pathways.";
RL   J. Lipid Res. 38:2216-2223(1997).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11108725;
RA   Olivier L.M., Kovacs W., Masuda K., Keller G.A., Krisans S.K.;
RT   "Identification of peroxisomal targeting signals in cholesterol
RT   biosynthetic enzymes. AA-CoA thiolase, hmg-coa synthase, MPPD, and FPP
RT   synthase.";
RL   J. Lipid Res. 41:1921-1935(2000).
RN   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14972328; DOI=10.1016/j.ymgme.2003.12.001;
RA   Hogenboom S., Tuyp J.J., Espeel M., Koster J., Wanders R.J., Waterham H.R.;
RT   "Human mevalonate pyrophosphate decarboxylase is localized in the
RT   cytosol.";
RL   Mol. Genet. Metab. 81:216-224(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
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=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [11]
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   INVOLVEMENT IN POROK7, AND VARIANTS POROK7 ARG-101; VAL-128; GLN-161;
RP   LEU-161; GLN-228; TRP-228; SER-249; SER-292; ILE-371 DEL AND ARG-376.
RX   PubMed=26202976; DOI=10.7554/elife.06322;
RA   Zhang Z., Li C., Wu F., Ma R., Luan J., Yang F., Liu W., Wang L., Zhang S.,
RA   Liu Y., Gu J., Hua W., Fan M., Peng H., Meng X., Song N., Bi X., Gu C.,
RA   Zhang Z., Huang Q., Chen L., Xiang L., Xu J., Zheng Z., Jiang Z.;
RT   "Genomic variations of the mevalonate pathway in porokeratosis.";
RL   Elife 4:E06322-E06322(2015).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), MUTAGENESIS OF ASN-17,
RP   CHARACTERIZATION OF VARIANT POROK7 GLN-161, FUNCTION, CATALYTIC ACTIVITY,
RP   AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18823933; DOI=10.1016/j.abb.2008.08.024;
RA   Voynova N.E., Fu Z., Battaile K.P., Herdendorf T.J., Kim J.J.,
RA   Miziorko H.M.;
RT   "Human mevalonate diphosphate decarboxylase: characterization,
RT   investigation of the mevalonate diphosphate binding site, and crystal
RT   structure.";
RL   Arch. Biochem. Biophys. 480:58-67(2008).
CC   -!- FUNCTION: Catalyzes the ATP dependent decarboxylation of (R)-5-
CC       diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in
CC       the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP),
CC       a key precursor for the biosynthesis of isoprenoids and sterol
CC       synthesis. {ECO:0000269|PubMed:18823933, ECO:0000269|PubMed:8626466,
CC       ECO:0000269|PubMed:9392419}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl
CC         diphosphate + phosphate; Xref=Rhea:RHEA:23732, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57557,
CC         ChEBI:CHEBI:128769, ChEBI:CHEBI:456216; EC=4.1.1.33;
CC         Evidence={ECO:0000269|PubMed:18823933, ECO:0000269|PubMed:8626466,
CC         ECO:0000269|PubMed:9392419};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7.4 uM for (R)-5-diphosphomevalonate {ECO:0000269|PubMed:9392419};
CC         KM=28.9 uM for (S,R)-5-diphosphomevalonate
CC         {ECO:0000269|PubMed:18823933};
CC         KM=0.69 mM for ATP {ECO:0000269|PubMed:18823933};
CC         KM=0.32 mM for ATP {ECO:0000269|PubMed:9392419};
CC   -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. {ECO:0000305}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8626466}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14972328}.
CC   -!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, lung, liver,
CC       brain, pancreas, kidney and placenta. {ECO:0000269|PubMed:8626466}.
CC   -!- DISEASE: Porokeratosis 7, multiple types (POROK7) [MIM:614714]: A form
CC       of porokeratosis, a disorder of faulty keratinization characterized by
CC       one or more atrophic patches surrounded by a distinctive hyperkeratotic
CC       ridgelike border called the cornoid lamella. The keratotic lesions can
CC       progress to overt cutaneous neoplasms, typically squamous cell
CC       carcinomas. Multiple clinical variants of porokeratosis are recognized,
CC       including porokeratosis of Mibelli, linear porokeratosis, disseminated
CC       superficial actinic porokeratosis, palmoplantar porokeratosis, and
CC       punctate porokeratosis. Different clinical presentations can be
CC       observed among members of the same family. Individuals expressing more
CC       than one variant have also been reported. {ECO:0000269|PubMed:18823933,
CC       ECO:0000269|PubMed:26202976}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to be located in the peroxisome
CC       (PubMed:11108725). However, was later shown to be cytosolic
CC       (PubMed:14972328). {ECO:0000269|PubMed:11108725,
CC       ECO:0000269|PubMed:14972328}.
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DR   EMBL; U49260; AAC50440.1; -; mRNA.
DR   EMBL; BT006930; AAP35576.1; -; mRNA.
DR   EMBL; CH471184; EAW66792.1; -; Genomic_DNA.
DR   EMBL; BC000011; AAH00011.1; -; mRNA.
DR   CCDS; CCDS10968.1; -.
DR   RefSeq; NP_002452.1; NM_002461.2.
DR   PDB; 3D4J; X-ray; 2.40 A; A/B=1-400.
DR   PDBsum; 3D4J; -.
DR   AlphaFoldDB; P53602; -.
DR   SMR; P53602; -.
DR   BioGRID; 110682; 57.
DR   IntAct; P53602; 10.
DR   STRING; 9606.ENSP00000301012; -.
DR   BindingDB; P53602; -.
DR   ChEMBL; CHEMBL4340; -.
DR   GuidetoPHARMACOLOGY; 642; -.
DR   SwissLipids; SLP:000001242; -.
DR   GlyGen; P53602; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P53602; -.
DR   PhosphoSitePlus; P53602; -.
DR   BioMuta; MVD; -.
DR   DMDM; 1706681; -.
DR   EPD; P53602; -.
DR   jPOST; P53602; -.
DR   MassIVE; P53602; -.
DR   MaxQB; P53602; -.
DR   PaxDb; 9606-ENSP00000301012; -.
DR   PeptideAtlas; P53602; -.
DR   ProteomicsDB; 56588; -.
DR   Pumba; P53602; -.
DR   Antibodypedia; 30739; 237 antibodies from 28 providers.
DR   DNASU; 4597; -.
DR   Ensembl; ENST00000301012.8; ENSP00000301012.3; ENSG00000167508.12.
DR   GeneID; 4597; -.
DR   KEGG; hsa:4597; -.
DR   MANE-Select; ENST00000301012.8; ENSP00000301012.3; NM_002461.3; NP_002452.1.
DR   UCSC; uc002flg.2; human.
DR   AGR; HGNC:7529; -.
DR   DisGeNET; 4597; -.
DR   GeneCards; MVD; -.
DR   HGNC; HGNC:7529; MVD.
DR   HPA; ENSG00000167508; Low tissue specificity.
DR   MalaCards; MVD; -.
DR   MIM; 603236; gene.
DR   MIM; 614714; phenotype.
DR   neXtProt; NX_P53602; -.
DR   OpenTargets; ENSG00000167508; -.
DR   Orphanet; 79152; Disseminated superficial actinic porokeratosis.
DR   PharmGKB; PA31330; -.
DR   VEuPathDB; HostDB:ENSG00000167508; -.
DR   eggNOG; KOG2833; Eukaryota.
DR   GeneTree; ENSGT00390000015359; -.
DR   HOGENOM; CLU_040369_4_4_1; -.
DR   InParanoid; P53602; -.
DR   OMA; LTLHAMM; -.
DR   OrthoDB; 458712at2759; -.
DR   PhylomeDB; P53602; -.
DR   TreeFam; TF105952; -.
DR   BioCyc; MetaCyc:ENSG00000167508-MONOMER; -.
DR   BRENDA; 4.1.1.33; 2681.
DR   PathwayCommons; P53602; -.
DR   Reactome; R-HSA-191273; Cholesterol biosynthesis.
DR   Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR   Reactome; R-HSA-446199; Synthesis of Dolichyl-phosphate.
DR   SABIO-RK; P53602; -.
DR   SignaLink; P53602; -.
DR   SIGNOR; P53602; -.
DR   UniPathway; UPA00063; -.
DR   BioGRID-ORCS; 4597; 508 hits in 1162 CRISPR screens.
DR   ChiTaRS; MVD; human.
DR   EvolutionaryTrace; P53602; -.
DR   GenomeRNAi; 4597; -.
DR   Pharos; P53602; Tchem.
DR   PRO; PR:P53602; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; P53602; Protein.
DR   Bgee; ENSG00000167508; Expressed in right hemisphere of cerebellum and 113 other cell types or tissues.
DR   ExpressionAtlas; P53602; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; IDA:UniProtKB.
DR   GO; GO:0030544; F:Hsp70 protein binding; IPI:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; NAS:UniProtKB.
DR   GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 1.
DR   InterPro; IPR036554; GHMP_kinase_C_sf.
DR   InterPro; IPR006204; GHMP_kinase_N_dom.
DR   InterPro; IPR005935; Mev_decarb.
DR   InterPro; IPR029765; Mev_diP_decarb.
DR   InterPro; IPR041431; Mvd1_C.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR01240; mevDPdecarb; 1.
DR   PANTHER; PTHR10977; DIPHOSPHOMEVALONATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR10977:SF3; DIPHOSPHOMEVALONATE DECARBOXYLASE; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   Pfam; PF18376; MDD_C; 1.
DR   PIRSF; PIRSF015950; Mev_P_decrbx; 1.
DR   SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   Genevisible; P53602; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Cholesterol biosynthesis;
KW   Cholesterol metabolism; Cytoplasm; Disease variant; Lipid biosynthesis;
KW   Lipid metabolism; Lyase; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW   Sterol biosynthesis; Sterol metabolism.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   CHAIN           2..400
FT                   /note="Diphosphomevalonate decarboxylase"
FT                   /id="PRO_0000087012"
FT   BINDING         23..26
FT                   /ligand="(R)-5-diphosphomevalonate"
FT                   /ligand_id="ChEBI:CHEBI:57557"
FT                   /evidence="ECO:0000250|UniProtKB:O23722"
FT   BINDING         78
FT                   /ligand="(R)-5-diphosphomevalonate"
FT                   /ligand_id="ChEBI:CHEBI:57557"
FT                   /evidence="ECO:0000250|UniProtKB:O23722"
FT   BINDING         156..161
FT                   /ligand="(R)-5-diphosphomevalonate"
FT                   /ligand_id="ChEBI:CHEBI:57557"
FT                   /evidence="ECO:0000250|UniProtKB:O23722"
FT   BINDING         212
FT                   /ligand="(R)-5-diphosphomevalonate"
FT                   /ligand_id="ChEBI:CHEBI:57557"
FT                   /evidence="ECO:0000250|UniProtKB:O23722"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:19413330,
FT                   ECO:0007744|PubMed:22223895"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   VARIANT         101
FT                   /note="P -> R (in POROK7; uncertain significance;
FT                   dbSNP:rs200033380)"
FT                   /evidence="ECO:0000269|PubMed:26202976"
FT                   /id="VAR_075052"
FT   VARIANT         128
FT                   /note="A -> V (in POROK7; uncertain significance;
FT                   dbSNP:rs776358937)"
FT                   /evidence="ECO:0000269|PubMed:26202976"
FT                   /id="VAR_075053"
FT   VARIANT         161
FT                   /note="R -> L (in POROK7; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:26202976"
FT                   /id="VAR_075054"
FT   VARIANT         161
FT                   /note="R -> Q (in POROK7; 1000-fold diminution in
FT                   diphosphomevalonate decarboxylase activity;
FT                   dbSNP:rs144010349)"
FT                   /evidence="ECO:0000269|PubMed:18823933,
FT                   ECO:0000269|PubMed:26202976"
FT                   /id="VAR_075055"
FT   VARIANT         228
FT                   /note="R -> Q (in POROK7; uncertain significance;
FT                   dbSNP:rs770939767)"
FT                   /evidence="ECO:0000269|PubMed:26202976"
FT                   /id="VAR_075056"
FT   VARIANT         228
FT                   /note="R -> W (in POROK7; uncertain significance;
FT                   dbSNP:rs776684503)"
FT                   /evidence="ECO:0000269|PubMed:26202976"
FT                   /id="VAR_075057"
FT   VARIANT         249
FT                   /note="F -> S (in POROK7; dbSNP:rs761991070)"
FT                   /evidence="ECO:0000269|PubMed:26202976"
FT                   /id="VAR_075058"
FT   VARIANT         278
FT                   /note="N -> H (in dbSNP:rs34519538)"
FT                   /id="VAR_051605"
FT   VARIANT         292
FT                   /note="N -> S (in POROK7; dbSNP:rs755948940)"
FT                   /evidence="ECO:0000269|PubMed:26202976"
FT                   /id="VAR_075059"
FT   VARIANT         371
FT                   /note="Missing (in POROK7; uncertain significance;
FT                   dbSNP:rs764836183)"
FT                   /evidence="ECO:0000269|PubMed:26202976"
FT                   /id="VAR_075060"
FT   VARIANT         376
FT                   /note="G -> R (in POROK7; uncertain significance;
FT                   dbSNP:rs546127665)"
FT                   /evidence="ECO:0000269|PubMed:26202976"
FT                   /id="VAR_075061"
FT   MUTAGEN         17
FT                   /note="N->A: 15-fold inflation in KM for mevalonate
FT                   diphosphate."
FT                   /evidence="ECO:0000269|PubMed:18823933"
FT   STRAND          10..14
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          17..21
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          26..28
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   TURN            29..32
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          33..36
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          38..43
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   TURN            45..47
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          50..56
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          64..67
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           77..88
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          110..118
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   TURN            120..122
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           126..139
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   TURN            140..143
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           149..155
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           157..163
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          164..170
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          178..180
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          183..187
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           189..191
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          195..202
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           211..221
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           223..231
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           233..245
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           249..268
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          270..272
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           279..295
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          300..303
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          306..308
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          310..315
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           316..318
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           319..329
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   TURN            337..339
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          340..343
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           352..358
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          366..375
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   HELIX           385..387
FT                   /evidence="ECO:0007829|PDB:3D4J"
FT   STRAND          392..394
FT                   /evidence="ECO:0007829|PDB:3D4J"
SQ   SEQUENCE   400 AA;  43405 MW;  3FD4741BCC4B68D8 CRC64;
     MASEKPLAAV TCTAPVNIAV IKYWGKRDEE LVLPINSSLS VTLHQDQLKT TTTAVISKDF
     TEDRIWLNGR EEDVGQPRLQ ACLREIRCLA RKRRNSRDGD PLPSSLSCKV HVASVNNFPT
     AAGLASSAAG YACLAYTLAR VYGVESDLSE VARRGSGSAC RSLYGGFVEW QMGEQADGKD
     SIARQVAPES HWPELRVLIL VVSAEKKLTG STVGMRASVE TSPLLRFRAE SVVPARMAEM
     ARCIRERDFP SFAQLTMKDS NQFHATCLDT FPPISYLNAI SWRIIHLVHR FNAHHGDTKV
     AYTFDAGPNA VIFTLDDTVA EFVAAVWHGF PPGSNGDTFL KGLQVRPAPL SAELQAALAM
     EPTPGGVKYI IVTQVGPGPQ ILDDPCAHLL GPDGLPKPAA
//