ID   PMVK_HUMAN              Reviewed;         192 AA.
AC   Q15126; Q5TZW9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 195.
DE   RecName: Full=Phosphomevalonate kinase;
DE            Short=PMKase;
DE            Short=hPMK;
DE            EC=2.7.4.2 {ECO:0000269|PubMed:16519518, ECO:0000269|PubMed:17902708, ECO:0000269|PubMed:8663599, ECO:0000269|PubMed:9392419};
GN   Name=PMVK; Synonyms=PMKI;
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, TISSUE SPECIFICITY, AND
RP   FUNCTION.
RC   TISSUE=Liver;
RX   PubMed=8663599; DOI=10.1074/jbc.271.29.17330;
RA   Chambliss K.L., Slaughter C.A., Schreiner R., Hoffmann G.F., Gibson K.M.;
RT   "Molecular cloning of human phosphomevalonate kinase and identification of
RT   a consensus peroxisomal targeting sequence.";
RL   J. Biol. Chem. 271:17330-17334(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-125.
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Skin, and Uterus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-192, AND INDUCTION.
RX   PubMed=10191291;
RA   Olivier L.M., Chambliss K.L., Gibson K.M., Krisans S.K.;
RT   "Characterization of phosphomevalonate kinase: chromosomal localization,
RT   regulation, and subcellular targeting.";
RL   J. Lipid Res. 40:672-679(1999).
RN   [5]
RP   CATALYTIC ACTIVITY, FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
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=14729858; DOI=10.1194/jlr.m300373-jlr200;
RA   Hogenboom S., Tuyp J.J., Espeel M., Koster J., Wanders R.J., Waterham H.R.;
RT   "Phosphomevalonate kinase is a cytosolic protein in humans.";
RL   J. Lipid Res. 45:697-705(2004).
RN   [7]
RP   FUNCTION, MUTAGENESIS OF LYS-17; ARG-18; LYS-19; LYS-22 AND ASP-23,
RP   BIOPHYSICOCHEMICAL PROPERTIES, ATP-BINDING, CATALYTIC ACTIVITY, AND
RP   SUBUNIT.
RX   PubMed=16519518; DOI=10.1021/bi052231u;
RA   Herdendorf T.J., Miziorko H.M.;
RT   "Phosphomevalonate kinase: functional investigation of the recombinant
RT   human enzyme.";
RL   Biochemistry 45:3235-3242(2006).
RN   [8]
RP   FUNCTION, MUTAGENESIS OF LYS-48; LYS-69; ARG-73; ARG-84; ARG-110; ARG-111
RP   AND ARG-141, ATP-BINDING, AND CATALYTIC ACTIVITY.
RX   PubMed=17902708; DOI=10.1021/bi701408t;
RA   Herdendorf T.J., Miziorko H.M.;
RT   "Functional evaluation of conserved basic residues in human
RT   phosphomevalonate kinase.";
RL   Biochemistry 46:11780-11788(2007).
RN   [9]
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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [11]
RP   IDENTIFICATION BY 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   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS), ATP-BINDING, AND SUBSTRATE BINDING.
RX   PubMed=18618710; DOI=10.1002/prot.22151;
RA   Chang Q., Yan X.-X., Gu S.-Y., Liu J.-F., Liang D.-C.;
RT   "Crystal structure of human phosphomevalonate kinase at 1.8 A resolution.";
RL   Proteins 73:254-258(2008).
RN   [14]
RP   INVOLVEMENT IN POROK1, AND VARIANT POROK1 GLU-69.
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   VARIANT POROK1 138-ARG--LEU-192 DEL, AND SUBCELLULAR LOCATION.
RX   PubMed=27052676; DOI=10.1038/srep24226;
RA   Wang J., Liu Y., Liu F., Huang C., Han S., Lv Y., Liu C.J., Zhang S.,
RA   Qin Y., Ling L., Gao M., Yu S., Li C., Huang M., Liao S., Hu X., Lu Z.,
RA   Liu X., Jiang T., Tang Z., Zhang H., Guo A.Y., Liu M.;
RT   "Loss-of-function mutation in PMVK causes autosomal dominant disseminated
RT   superficial porokeratosis.";
RL   Sci. Rep. 6:24226-24226(2016).
CC   -!- FUNCTION: Catalyzes the reversible ATP-dependent phosphorylation of
CC       mevalonate 5-phosphate to produce mevalonate diphosphate and ADP, a key
CC       step in the mevalonic acid mediated biosynthesis of isopentenyl
CC       diphosphate and other polyisoprenoid metabolites.
CC       {ECO:0000269|PubMed:16519518, ECO:0000269|PubMed:17902708,
CC       ECO:0000269|PubMed:8663599, ECO:0000269|PubMed:9392419}.
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:16519518, ECO:0000269|PubMed:17902708,
CC         ECO:0000269|PubMed:8663599, ECO:0000269|PubMed:9392419};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16342;
CC         Evidence={ECO:0000305|PubMed:16519518, ECO:0000305|PubMed:9392419};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16343;
CC         Evidence={ECO:0000305|PubMed:16519518};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=25 uM for (R)-5-phosphomevalonate {ECO:0000269|PubMed:16519518,
CC         ECO:0000269|PubMed:9392419};
CC         KM=0.26 mM for ATP {ECO:0000269|PubMed:16519518,
CC         ECO:0000269|PubMed:9392419};
CC         Vmax=46.4 umol/min/mg enzyme with (R)-5-phosphomevalonate as
CC         substrate {ECO:0000269|PubMed:16519518, ECO:0000269|PubMed:9392419};
CC         Vmax=52 umol/min/mg enzyme with ATP as substrate
CC         {ECO:0000269|PubMed:16519518, ECO:0000269|PubMed:9392419};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC       step 2/3. {ECO:0000305}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16519518}.
CC   -!- INTERACTION:
CC       Q15126; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-1055562, EBI-742054;
CC       Q15126; Q13360-2: ZNF177; NbExp=3; IntAct=EBI-1055562, EBI-12272076;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10191291,
CC       ECO:0000269|PubMed:27052676}.
CC   -!- TISSUE SPECIFICITY: Heart, liver, skeletal muscle, kidney, and
CC       pancreas. Lower level in brain, placenta and lung.
CC       {ECO:0000269|PubMed:8663599}.
CC   -!- INDUCTION: By sterol. {ECO:0000269|PubMed:10191291}.
CC   -!- DISEASE: Porokeratosis 1, multiple types (POROK1) [MIM:175800]: 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:26202976,
CC       ECO:0000269|PubMed:27052676}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- CAUTION: Was originally thought to be located in the peroxisome
CC       (PubMed:10191291). However, was later shown to be cytosolic
CC       (PubMed:14729858, PubMed:27052676). {ECO:0000269|PubMed:14729858,
CC       ECO:0000269|PubMed:27052676, ECO:0000305|PubMed:10191291}.
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DR   EMBL; L77213; AAC37593.1; -; mRNA.
DR   EMBL; BT019976; AAV38779.1; -; mRNA.
DR   EMBL; BC006089; AAH06089.1; -; mRNA.
DR   EMBL; BC007694; AAH07694.1; -; mRNA.
DR   EMBL; AF026069; AAC60791.1; -; Genomic_DNA.
DR   CCDS; CCDS1073.1; -.
DR   RefSeq; NP_006547.1; NM_006556.3.
DR   PDB; 3CH4; X-ray; 1.76 A; B=1-192.
DR   PDBsum; 3CH4; -.
DR   AlphaFoldDB; Q15126; -.
DR   SMR; Q15126; -.
DR   BioGRID; 115897; 104.
DR   IntAct; Q15126; 25.
DR   MINT; Q15126; -.
DR   STRING; 9606.ENSP00000357452; -.
DR   GuidetoPHARMACOLOGY; 641; -.
DR   SwissLipids; SLP:000001241; -.
DR   iPTMnet; Q15126; -.
DR   PhosphoSitePlus; Q15126; -.
DR   BioMuta; PMVK; -.
DR   DMDM; 3024422; -.
DR   REPRODUCTION-2DPAGE; IPI00220648; -.
DR   EPD; Q15126; -.
DR   jPOST; Q15126; -.
DR   MassIVE; Q15126; -.
DR   PaxDb; 9606-ENSP00000357452; -.
DR   PeptideAtlas; Q15126; -.
DR   ProteomicsDB; 60453; -.
DR   Pumba; Q15126; -.
DR   Antibodypedia; 34158; 286 antibodies from 28 providers.
DR   DNASU; 10654; -.
DR   Ensembl; ENST00000368467.4; ENSP00000357452.3; ENSG00000163344.6.
DR   GeneID; 10654; -.
DR   KEGG; hsa:10654; -.
DR   MANE-Select; ENST00000368467.4; ENSP00000357452.3; NM_006556.4; NP_006547.1.
DR   AGR; HGNC:9141; -.
DR   DisGeNET; 10654; -.
DR   GeneCards; PMVK; -.
DR   HGNC; HGNC:9141; PMVK.
DR   HPA; ENSG00000163344; Low tissue specificity.
DR   MalaCards; PMVK; -.
DR   MIM; 175800; phenotype.
DR   MIM; 607622; gene.
DR   neXtProt; NX_Q15126; -.
DR   OpenTargets; ENSG00000163344; -.
DR   Orphanet; 735; Porokeratosis of Mibelli.
DR   PharmGKB; PA33465; -.
DR   VEuPathDB; HostDB:ENSG00000163344; -.
DR   eggNOG; ENOG502QYPQ; Eukaryota.
DR   GeneTree; ENSGT00390000014801; -.
DR   HOGENOM; CLU_092097_0_0_1; -.
DR   InParanoid; Q15126; -.
DR   OMA; YGFFCRA; -.
DR   OrthoDB; 2877244at2759; -.
DR   PhylomeDB; Q15126; -.
DR   TreeFam; TF312935; -.
DR   BioCyc; MetaCyc:HS08830-MONOMER; -.
DR   BRENDA; 2.7.4.2; 2681.
DR   PathwayCommons; Q15126; -.
DR   Reactome; R-HSA-191273; Cholesterol biosynthesis.
DR   Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR   SABIO-RK; Q15126; -.
DR   SignaLink; Q15126; -.
DR   UniPathway; UPA00057; UER00099.
DR   BioGRID-ORCS; 10654; 316 hits in 1165 CRISPR screens.
DR   ChiTaRS; PMVK; human.
DR   EvolutionaryTrace; Q15126; -.
DR   GenomeRNAi; 10654; -.
DR   Pharos; Q15126; Tchem.
DR   PRO; PR:Q15126; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q15126; Protein.
DR   Bgee; ENSG00000163344; Expressed in apex of heart and 201 other cell types or tissues.
DR   ExpressionAtlas; Q15126; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0004631; F:phosphomevalonate kinase activity; IDA:UniProtKB.
DR   GO; GO:0006695; P:cholesterol biosynthetic process; IDA: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:0070723; P:response to cholesterol; IEP:UniProtKB.
DR   GO; GO:0016126; P:sterol biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005919; Pmev_kin_anim.
DR   NCBIfam; TIGR01223; Pmev_kin_anim; 1.
DR   PANTHER; PTHR13101; PHOSPHOMEVALONATE KINASE; 1.
DR   PANTHER; PTHR13101:SF1; PHOSPHOMEVALONATE KINASE; 1.
DR   Pfam; PF04275; P-mevalo_kinase; 1.
DR   PIRSF; PIRSF036639; PMK_anim; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   Genevisible; Q15126; HS.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cholesterol biosynthesis;
KW   Cholesterol metabolism; Cytoplasm; Disease variant; Kinase;
KW   Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW   Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW   Sterol biosynthesis; Sterol metabolism; Transferase.
FT   CHAIN           1..192
FT                   /note="Phosphomevalonate kinase"
FT                   /id="PRO_0000058472"
FT   BINDING         17..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|PubMed:16519518,
FT                   ECO:0000305|PubMed:18618710"
FT   BINDING         141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|PubMed:17902708,
FT                   ECO:0000305|PubMed:18618710"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:18618710"
FT   BINDING         171
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|PubMed:18618710"
FT   BINDING         176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|PubMed:18618710"
FT   BINDING         180
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000305|PubMed:18618710"
FT   VARIANT         69
FT                   /note="K -> E (in POROK1; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:26202976"
FT                   /id="VAR_075051"
FT   VARIANT         125
FT                   /note="V -> M (in dbSNP:rs16836525)"
FT                   /evidence="ECO:0000269|Ref.2"
FT                   /id="VAR_051283"
FT   VARIANT         138..192
FT                   /note="Missing (in POROK1; results in reduced expression
FT                   and solubility; disturbs subcellular localization with
FT                   punctate rather than diffuse cytoplasmic distribution)"
FT                   /evidence="ECO:0000269|PubMed:27052676"
FT                   /id="VAR_080138"
FT   MUTAGEN         17
FT                   /note="K->M: Approximately 8-fold decrease in Vmax for
FT                   MgATP and R-MVP. Approximately 5-fold increase in KM for
FT                   MgATP and R-MVP."
FT                   /evidence="ECO:0000269|PubMed:16519518"
FT   MUTAGEN         18
FT                   /note="R->Q: Approximately 85-fold decrease in Vmax for
FT                   MgATP and R-MVP. Approximately 5-fold increase in KM for
FT                   MgATP and R-MVP."
FT                   /evidence="ECO:0000269|PubMed:16519518"
FT   MUTAGEN         19
FT                   /note="K->M: Approximately 9-fold decrease in Vmax for
FT                   MgATP and R-MVP. Approximately 10-fold increase in KM for
FT                   MgATP and R-MVP."
FT                   /evidence="ECO:0000269|PubMed:16519518"
FT   MUTAGEN         22
FT                   /note="K->M: Approximately 100000-fold decrease in Vmax for
FT                   MgATP."
FT                   /evidence="ECO:0000269|PubMed:16519518"
FT   MUTAGEN         23
FT                   /note="D->N: Approximately 7-fold decrease in Vmax for
FT                   MgATP and R-MVP. Approximately 10-fold increase in KM for
FT                   MgATP and 5-fold increase in KM for R-MVP."
FT                   /evidence="ECO:0000269|PubMed:16519518"
FT   MUTAGEN         48
FT                   /note="K->M: Approximately 1400-fold decrease in Vmax for
FT                   MgATP and R-MVP. Approximately 3-fold increase in KM for
FT                   MgATP and R-MVP."
FT                   /evidence="ECO:0000269|PubMed:17902708"
FT   MUTAGEN         69
FT                   /note="K->M: Approximately 500-fold decrease in Vmax for
FT                   MgATP and R-MVP. Approximately 3-fold increase in KM for
FT                   MgATP and R-MVP."
FT                   /evidence="ECO:0000269|PubMed:17902708"
FT   MUTAGEN         73
FT                   /note="R->M: Approximately 3000-fold decrease in Vmax for
FT                   MgATP and R-MVP. No change in KM for MgATP and
FT                   approximately 3-fold increase in KM for R-MVP."
FT                   /evidence="ECO:0000269|PubMed:17902708"
FT   MUTAGEN         84
FT                   /note="R->M: Approximately 10-fold decrease in Vmax for
FT                   MgATP and R-MVP. Approximately 3-fold increase in KM for
FT                   MgATP and 50-fold increase in KM for R-MVP."
FT                   /evidence="ECO:0000269|PubMed:17902708"
FT   MUTAGEN         93
FT                   /note="R->M: Almost no change in KM and Vmax for MgATP and
FT                   R-MVP."
FT   MUTAGEN         110
FT                   /note="R->M: Approximately 20000-fold decrease in Vmax for
FT                   MgATP."
FT                   /evidence="ECO:0000269|PubMed:17902708"
FT   MUTAGEN         111
FT                   /note="R->M: Approximately 65-fold decrease in Vmax for
FT                   MgATP and R-MVP. Approximately 8-fold increase in KM for
FT                   MgATP and 60-fold increase in KM for R-MVP."
FT                   /evidence="ECO:0000269|PubMed:17902708"
FT   MUTAGEN         130
FT                   /note="R->M: Approximately 4-fold decrease in Vmax for
FT                   MgATP and R-MVP. Approximately 3-fold increase in KM for
FT                   MgATP and R-MVP."
FT   MUTAGEN         138
FT                   /note="R->M: Approximately 3-fold decrease in Vmax for
FT                   MgATP and R-MVP. Approximately 5-fold increase in KM for
FT                   MgATP and no change in KM for R-MVP."
FT   MUTAGEN         141
FT                   /note="R->M: Approximately 15-fold decrease in Vmax for
FT                   MgATP and R-MVP. Approximately 50-fold increase in KM for
FT                   MgATP and approximately 7-fold in KM for R-MVP."
FT                   /evidence="ECO:0000269|PubMed:17902708"
FT   STRAND          9..16
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   HELIX           22..33
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   STRAND          38..41
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   HELIX           44..53
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   HELIX           72..86
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   TURN            88..91
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   HELIX           92..95
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   STRAND          102..106
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   HELIX           112..122
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   HELIX           123..125
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   STRAND          126..133
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   HELIX           135..140
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   TURN            147..151
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   HELIX           153..156
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   TURN            157..160
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   STRAND          165..170
FT                   /evidence="ECO:0007829|PDB:3CH4"
FT   HELIX           174..189
FT                   /evidence="ECO:0007829|PDB:3CH4"
SQ   SEQUENCE   192 AA;  21995 MW;  D7E720D0DDCCA249 CRC64;
     MAPLGGAPRL VLLFSGKRKS GKDFVTEALQ SRLGADVCAV LRLSGPLKEQ YAQEHGLNFQ
     RLLDTSTYKE AFRKDMIRWG EEKRQADPGF FCRKIVEGIS QPIWLVSDTR RVSDIQWFRE
     AYGAVTQTVR VVALEQSRQQ RGWVFTPGVD DAESECGLDN FGDFDWVIEN HGVEQRLEEQ
     LENLIEFIRS RL
//