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Human Metabolome Database Version 2.5

 

Showing metabocard for Mevalonic acid-5P (HMDB01343)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2009-05-05 20:58:41
Accession Number HMDB01343
Secondary Accession Numbers Not Available
Common Name Mevalonic acid-5P
Description 5-Phosphomevalonate is a metabolic intermediate in the mevalonate pathway, catalyzed by the enzyme mevalonate kinase from Mevalonate. (wikipedia)
Synonyms
  1. (R)-5-phosphomevalonate
  2. (R)-5-phosphomevalonic acid
  3. (R)-5-phosphomevaloonate
  4. (R)-5-phosphomevaloonic acid
  5. (R)-mevalonic acid 5-phosphate
  6. 5-phosphomevalonate
  7. mevalonate-5-p
  8. mevalonate-5-phosphate
  9. mevalonate-5P
  10. mevalonate-p
  11. p-mevalonate
Chemical IUPAC Name 3-hydroxy-3-methyl-5-phosphonooxy-pentanoic acid
Chemical Formula C6H13O7P
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Miscellaneous
Class
  • Acyl Phosphates
Sub Class
  • Short chain acyl phosphates
Family
  • Mammalian Metabolite
Species
  • tertiary alcohol
  • carboxylic acid
  • phosphoric acid ester
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 228.137
Monoisotopic Molecular Weight 228.039886
Isomeric SMILES C[C@@](O)(CCOP(O)(O)=O)CC(O)=O
Canonical SMILES CC(O)(CCOP(O)(O)=O)CC(O)=O
KEGG Compound ID C01107 Link Image
BioCyc ID CPD-499 Link Image
BiGG ID 36819 Link Image
Wikipedia Link 5-phosphomevalonate Link Image
NuGOwiki Link HMDB01343 Link Image
Metagene Link HMDB01343 Link Image
METLIN ID 6177 Link Image
PubChem Compound 439400 Link Image
PubChem Substance 8144823 Link Image
ChEBI ID 17436 Link Image
CAS Registry Number 73566-35-5
InChI Identifier InChI=1/C6H13O7P/c1-6(9,4-5(7)8)2-3-13-14(10,11)12/h9H,2-4H2,1H3,(H,7,8)(H2,10,11,12)/t6-/m1/s1
Synthesis Reference Not Available
Melting Point (Experimental) Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 19.9 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -3
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.18 [Predicted by ALOGPS]; -2.1 [Predicted by PubChem via XLOGP] Calculated using ALOGPS
Material Safety Data Sheet (MSDS) Not Available
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Not Available
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Not Available
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum Not Available
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm (Predicted from LogP)
  • peroxisome
Biofluid Location Not Available
Tissue Location
Tissue References
Heart
Kidney
Liver
Pancreas
Skeletal Muscle
Concentrations (Normal) Not Available
Concentrations (Abnormal) Not Available
Associated Disorders Not Available
OMIM ID Not Available
Pathways
Name SMPDB Link KEGG Link
Steroid Biosynthesis SMP00023 Link Image map00100 Link Image
General References
  1. Popjak G, Boehm G, Parker TS, Edmond J, Edwards PA, Fogelman AM: Determination of mevalonate in blood plasma in man and rat. Mevalonate "tolerance" tests in man. J Lipid Res. 1979 Aug;20(6):716-28. [PubMed Link Image]
  2. Campos N, Rodriguez-Concepcion M, Sauret-Gueto S, Gallego F, Lois LM, Boronat A: Escherichia coli engineered to synthesize isopentenyl diphosphate and dimethylallyl diphosphate from mevalonate: a novel system for the genetic analysis of the 2-C-methyl-d-erythritol 4-phosphate pathway for isoprenoid biosynthesis. Biochem J. 2001 Jan 1;353(Pt 1):59-67. [PubMed Link Image]
  3. Houten SM, Waterham HR: Nonorthologous gene displacement of phosphomevalonate kinase. Mol Genet Metab. 2001 Mar;72(3):273-6. [PubMed Link Image]
  4. Wikipedia Link Image
Metabolic Enzymes
  1. Phosphomevalonate kinase
  2. Mevalonate kinase
  3. cDNA, FLJ96772, Homo sapiens mevalonate kinase (mevalonic aciduria) (MVK), mRNA (Mevalonate kinase (Mevalonic aciduria), isoform CRA_c)
Enzyme 1 [top]
Enzyme 1 ID 6305
Enzyme 1 Name Phosphomevalonate kinase
Enzyme 1 Synonyms
  1. PMKase
Enzyme 1 Gene Name PMVK
Enzyme 1 Protein Sequence >Phosphomevalonate kinase
MAPLGGAPRLVLLFSGKRKSGKDFVTEALQSRLGADVCAVLRLSGPLKEQYAQEHGLNFQ
RLLDTSTYKEAFRKDMIRWGEEKRQADPGFFCRKIVEGISQPIWLVSDTRRVSDIQWFRE
AYGAVTQTVRVVALEQSRQQRGWVFTPGVDDAESECGLDNFGDFDWVIENHGVEQRLEEQ
LENLIEFIRSRL
Enzyme 1 Number of Residues 192
Enzyme 1 Molecular Weight 21995
Enzyme 1 Theoretical pI 5.41
Enzyme 1 GO Classification
Function
  • catalytic activity
  • kinase activity
  • phosphomevalonate kinase activity
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • alcohol metabolism
  • cellular metabolism
  • cholesterol biosynthesis
  • cholesterol metabolism
  • metabolism
  • physiological process
  • sterol metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function ATP + (R)-5-phosphomevalonate = ADP + (R)-5- diphosphomevalonate
Enzyme 1 Pathways
Enzyme 1 Reactions
  • ATP + (R)-5-phosphomevalonate = ADP + (R)-5-diphosphomevalonate
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-21
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 1294782 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q15126 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name PMVK_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >579 bp
ATGGCCCCGCTGGGAGGCGCCCCGCGGCTGGTACTGCTGTTCAGCGGCAAGAGGAAATCC
GGGAAGGACTTCGTGACCGAGGCGCTGCAGAGCAGACTTGGAGCTGATGTCTGTGCTGTC
CTCCGGCTCTCTGGTCCACTCAAGGAACAGTATGCTCAGGAGCATGGCTTGAACTTCCAG
AGACTCCTGGACACCAGCACCTACAAGGAGGCCTTTCGGAAGGACATGATCCGCTGGGGA
GAGGAGAAACGCCAGGCTGACCCAGGCTTCTTTTGCAGGAAGATTGTGGAGGGCATCTCC
CAGCCCATCTGGCTGGTGAGTGACACACGGAGAGTGTCTGACATCCAGTGGTTTCGGGAG
GCCTATGGGGCCGTGACGCAGACGGTCCGCGTTGTAGCGTTGGAGCAGAGCCGACAGCAG
CGGGGCTGGGTGTTCACGCCAGGGGTGGACGATGCTGAGTCAGAATGTGGCCTGGACAAC
TTCGGGGACTTTGACTGGGTCATCGAGAACCATGGAGTTGAACAGCGCCTGGAGGAGCAG
TTGGAGAACCTGATAGAATTTATCCGCTCCAGACTTTAG
Enzyme 1 GenBank Gene ID L77213 Link Image
Enzyme 1 GeneCard ID PMVK Link Image
Enzyme 1 GenAtlas ID PMVK Link Image
Enzyme 1 HGNC ID HGNC:9141 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 1p13-q23
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Chambliss KL, Slaughter CA, Schreiner R, Hoffmann GF, Gibson KM: Molecular cloning of human phosphomevalonate kinase and identification of a consensus peroxisomal targeting sequence. J Biol Chem. 1996 Jul 19;271(29):17330-4. [PubMed Link Image]
  2. Olivier LM, Chambliss KL, Gibson KM, Krisans SK: Characterization of phosphomevalonate kinase: chromosomal localization, regulation, and subcellular targeting. J Lipid Res. 1999 Apr;40(4):672-9. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6342
Enzyme 2 Name Mevalonate kinase
Enzyme 2 Synonyms
  1. MK
Enzyme 2 Gene Name MVK
Enzyme 2 Protein Sequence >Mevalonate kinase
MLSEVLLVSAPGKVILHGEHAVVHGKVALAVSLNLRTFLRLQPHSNGKVDLSLPNIGIKR
AWDVARLQSLDTSFLEQGDVTTPTSEQVEKLKEVAGLPDDCAVTERLAVLAFLYLYLSIC
RKQRALPSLDIVVWSELPPGAGLGSSAAYSVCLAAALLTVCEEIPNPLKDGDCVNRWTKE
DLELINKWAFQGERMIHGNPSGVDNAVSTWGGALRYHQGKISSLKRSPALQILLTNTKVP
RNTRALVAGVRNRLLKFPEIVAPLLTSIDAISLECERVLGEMGEAPAPEQYLVLEELIDM
NQHHLNALGVGHASLDQLCQVTRARGLHSKLTGAGGGGCGITLLKPGLEQPEVEATKQAL
TSCGFDCLETSIGAPGVSIHSATSLDSRVQQALDGL
Enzyme 2 Number of Residues 396
Enzyme 2 Molecular Weight 42451
Enzyme 2 Theoretical pI 6.43
Enzyme 2 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • mevalonate kinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular lipid metabolism
  • cellular metabolism
  • isoprenoid biosynthesis
  • isoprenoid metabolism
  • lipid metabolism
  • metabolism
  • phosphate metabolism
  • phosphorus metabolism
  • phosphorylation
  • physiological process
  • primary metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 2 General Function Lipid transport and metabolism
Enzyme 2 Specific Function May be a regulatory site in cholesterol biosynthetic pathway
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + (R)-mevalonate = ADP + (R)-5-phosphomevalonate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 187561 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID Q03426 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name KIME_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >1191 bp
ATGTTGTCAGAAGTCCTACTGGTGTCTGCTCCGGGGAAAGTCATCCTTCATGGAGAACAT
GCCGTGGTACATGGCAAGGTAGCACTGGCTGTATCCTTGAACTTGAGAACATTCCTCCGG
CTTCAACCCCACAGCAATGGGAAAGTGGACCTCAGCTTACCCAACATTGGTATCAAGCGG
GCCTGGGATGTGGCCAGGCTTCAGTCACTGGACACAAGCTTTCTGGAGCAAGGTGATGTC
ACAACACCCACCTCAGAGCAAGTGGAGAAGCTAAAGGAGGTTGCAGGCTTGCCTGACGAC
TGTGCTGTCACCGAGCGCCTGGCTGTGCTGGCCTTTCTTTACTTATACCTGTCCATCTGC
CGGAAGCAGAGGGCCCTGCCGAGCCTGGATATCGTAGTGTGGTCGGAGCTGCCCCCCGGG
GCGGGCTTGGGCTCCAGCGCCGCCTACTCGGTGTGTCTGGCAGCAGCCCTCCTGACTGTG
TGCGAGGAGATCCCAAACCCGCTGAAGGACGGGGATTGCGTCAACAGGTGGACCAAGGAG
GATTTGGAGCTAATTAACAAGTGGGCCTTCCAAGGGGAGAGAATGATTCACGGGAACCCC
TCCGGAGTGGACAATGCTGTCAGCACCTGGGGAGGAGCCCTCCGATACCATCAAGGGAAG
ATTTCATCCTTAAAGAGGTCGCCAGCTCTCCAGATCCTGCTGACCAACACCAAAGTCCCT
CGCAATACCAGGGCCCTTGTGGCTGGCGTCAGAAACAGGCTGCTCAAGTTCCCAGAGATC
GTGGCCCCCCTCCTGACCTCAATAGATGCCATCTCCCTGGAGTGTGAGCGCGTGCTGGGA
GAGATGGGGGAAGCCCCAGCCCCGGAGCAGTACCTCGTGCTGGAAGAGCTCATTGACATG
AACCAGCACCATCTGAATGCCCTCGGCGTGGGCCACGCCTCTCTGGACCAGCTCTGCCAG
GTGACCAGGGCCCGCGGACTTCACAGCAAGCTGACTGGCGCAGGCGGTGGTGGCTGTGGC
ATCACACTCCTCAAGCCAGGGCTGGAGCAGCCAGAAGTGGAGGCCACGAAGCAGGCCCTG
ACCAGCTGTGGCTTTGACTGCTTGGAAACCAGCATCGGTGCCCCCGGCGTCTCCATCCAC
TCAGCCACCTCCCTGGACAGCCGAGTCCAGCAAGCCCTGGATGGCCTCTGA
Enzyme 2 GenBank Gene ID M88468 Link Image
Enzyme 2 GeneCard ID MVK Link Image
Enzyme 2 GenAtlas ID MVK Link Image
Enzyme 2 HGNC ID HGNC:7530 Link Image
Enzyme 2 Chromosome Location 12
Enzyme 2 Locus 12q24
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References
  1. Schafer BL, Bishop RW, Kratunis VJ, Kalinowski SS, Mosley ST, Gibson KM, Tanaka RD: Molecular cloning of human mevalonate kinase and identification of a missense mutation in the genetic disease mevalonic aciduria. J Biol Chem. 1992 Jul 5;267(19):13229-38. [PubMed Link Image]
  2. Graef E, Caselmann WH, Wells J, Koshy R: Insertional activation of mevalonate kinase by hepatitis B virus DNA in a human hepatoma cell line. Oncogene. 1994 Jan;9(1):81-7. [PubMed Link Image]
  3. Houten SM, Koster J, Romeijn GJ, Frenkel J, Di Rocco M, Caruso U, Landrieu P, Kelley RI, Kuis W, Poll-The BT, Gibson KM, Wanders RJ, Waterham HR: Organization of the mevalonate kinase (MVK) gene and identification of novel mutations causing mevalonic aciduria and hyperimmunoglobulinaemia D and periodic fever syndrome. Eur J Hum Genet. 2001 Apr;9(4):253-9. [PubMed Link Image]
  4. Hinson DD, Ross RM, Krisans S, Shaw JL, Kozich V, Rolland MO, Divry P, Mancini J, Hoffmann GF, Gibson KM: Identification of a mutation cluster in mevalonate kinase deficiency, including a new mutation in a patient of Mennonite ancestry. Am J Hum Genet. 1999 Aug;65(2):327-35. [PubMed Link Image]
  5. Houten SM, Romeijn GJ, Koster J, Gray RG, Darbyshire P, Smit GP, de Klerk JB, Duran M, Gibson KM, Wanders RJ, Waterham HR: Identification and characterization of three novel missense mutations in mevalonate kinase cDNA causing mevalonic aciduria, a disorder of isoprene biosynthesis. Hum Mol Genet. 1999 Aug;8(8):1523-8. [PubMed Link Image]
  6. Houten SM, Kuis W, Duran M, de Koning TJ, van Royen-Kerkhof A, Romeijn GJ, Frenkel J, Dorland L, de Barse MM, Huijbers WA, Rijkers GT, Waterham HR, Wanders RJ, Poll-The BT: Mutations in MVK, encoding mevalonate kinase, cause hyperimmunoglobulinaemia D and periodic fever syndrome. Nat Genet. 1999 Jun;22(2):175-7. [PubMed Link Image]
  7. Drenth JP, Cuisset L, Grateau G, Vasseur C, van de Velde-Visser SD, de Jong JG, Beckmann JS, van der Meer JW, Delpech M: Mutations in the gene encoding mevalonate kinase cause hyper-IgD and periodic fever syndrome. International Hyper-IgD Study Group. Nat Genet. 1999 Jun;22(2):178-81. [PubMed Link Image]
  8. Cuisset L, Drenth JP, Simon A, Vincent MF, van der Velde Visser S, van der Meer JW, Grateau G, Delpech M: Molecular analysis of MVK mutations and enzymatic activity in hyper-IgD and periodic fever syndrome. Eur J Hum Genet. 2001 Apr;9(4):260-6. [PubMed Link Image]
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 16528
Enzyme 3 Name cDNA, FLJ96772, Homo sapiens mevalonate kinase (mevalonic aciduria) (MVK), mRNA (Mevalonate kinase (Mevalonic aciduria), isoform CRA_c)
Enzyme 3 Synonyms Not Available
Enzyme 3 Gene Name MVK
Enzyme 3 Protein Sequence >cDNA, FLJ96772, Homo sapiens mevalonate kinase (mevalonic aciduria) (MVK), mRNA (Mevalonate kinase (Mevalonic aciduria), isoform CRA_c)
MLSEVLLVSAPGKVILHGEHAVVHGKVALAVSLNLRTFLRLQPHSNGKVDLSLPNIGIKR
AWDVARLQSLDTSFLEQGDVTTPTSEQVEKLKEVAGLPDDCAVTERLAVLAFLYLYLSIC
RKQRALPSLDIVVWSELPPGAGLGSSAAYSVCLAAALLTVCEEIPNPLKDGDCVNRWTKE
DLELINKWAFQGERMIHGNPSGVDNAVSTWGGALRYHQGKISSLKRSPALQILLTNTKVP
RNTRALVAGVRNRLLKFPEIVAPLLTSIDAISLECERVLGEMGEAPAPEQYLVLEELIDM
NQHHLNALGVGHASLDQLCQVTRARGLHSKLTGAGGGGCGITLLKPGLEQPEVEATKQAL
TSCGFDCLETSIGAPGVSIHSATSLDSRVQQALDGL
Enzyme 3 Number of Residues 396
Enzyme 3 Molecular Weight 42451
Enzyme 3 Theoretical pI 6.43
Enzyme 3 GO Classification
Function
  • ATP binding
  • adenyl nucleotide binding
  • binding
  • catalytic activity
  • kinase activity
  • mevalonate kinase activity
  • nucleotide binding
  • phosphotransferase activity, alcohol group as acceptor
  • purine nucleotide binding
  • transferase activity
  • transferase activity, transferring phosphorus-containing groups
Process
  • cellular lipid metabolism
  • cellular metabolism
  • isoprenoid biosynthesis
  • isoprenoid metabolism
  • lipid metabolism
  • metabolism
  • phosphate metabolism
  • phosphorus metabolism
  • phosphorylation
  • physiological process
  • primary metabolism
Component
  • cell
  • cytoplasm
  • intracellular
Enzyme 3 General Function Lipid transport and metabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein Not Available
Enzyme 3 UniProtKB/Swiss-Prot ID B2RDU6 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name B2RDU6_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID AK315678 Link Image
Enzyme 3 GeneCard ID B2RDU6 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location 12
Enzyme 3 Locus 12q24
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References Not Available
Enzyme 3 Metabolite References Not Available