Full text data of MVD
MVD
(MPD)
[Confidence: low (only semi-automatic identification from reviews)]
Diphosphomevalonate decarboxylase; 4.1.1.33 (Mevalonate (diphospho)decarboxylase; MDDase; Mevalonate pyrophosphate decarboxylase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Diphosphomevalonate decarboxylase; 4.1.1.33 (Mevalonate (diphospho)decarboxylase; MDDase; Mevalonate pyrophosphate decarboxylase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P53602
ID MVD1_HUMAN Reviewed; 400 AA.
AC P53602; Q53Y65;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Diphosphomevalonate decarboxylase;
DE EC=4.1.1.33;
DE AltName: Full=Mevalonate (diphospho)decarboxylase;
DE Short=MDDase;
DE AltName: Full=Mevalonate pyrophosphate decarboxylase;
GN Name=MVD; Synonyms=MPD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT yeast 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
RT 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP 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
RT of the cholesterol and nonsterol isoprene biosynthetic pathways.";
RL J. Lipid Res. 38:2216-2223(1997).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASS
RP SPECTROMETRY.
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
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.,
RA Buerckstuemmer T., 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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND MUTAGENESIS OF ASN-17 AND
RP ARG-161.
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: Performs the first committed step in the biosynthesis of
CC isoprenes.
CC -!- CATALYTIC ACTIVITY: ATP + (R)-5-diphosphomevalonate = ADP +
CC phosphate + isopentenyl diphosphate + CO(2).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.4 uM for (R)-5-diphosphomevalonate;
CC KM=0.32 mM for ATP;
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC -!- SUBUNIT: Homodimer.
CC -!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, lung,
CC liver, brain, pancreas, kidney and placenta.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_002452.1; NM_002461.1.
DR UniGene; Hs.252457; -.
DR PDB; 3D4J; X-ray; 2.40 A; A/B=1-400.
DR PDBsum; 3D4J; -.
DR ProteinModelPortal; P53602; -.
DR SMR; P53602; 8-396.
DR IntAct; P53602; 3.
DR MINT; MINT-5004338; -.
DR STRING; 9606.ENSP00000301012; -.
DR BindingDB; P53602; -.
DR ChEMBL; CHEMBL4340; -.
DR GuidetoPHARMACOLOGY; 642; -.
DR PhosphoSite; P53602; -.
DR DMDM; 1706681; -.
DR PaxDb; P53602; -.
DR PRIDE; P53602; -.
DR DNASU; 4597; -.
DR Ensembl; ENST00000301012; ENSP00000301012; ENSG00000167508.
DR GeneID; 4597; -.
DR KEGG; hsa:4597; -.
DR UCSC; uc002flf.1; human.
DR CTD; 4597; -.
DR GeneCards; GC16M088718; -.
DR HGNC; HGNC:7529; MVD.
DR HPA; HPA041404; -.
DR HPA; HPA048250; -.
DR MIM; 603236; gene.
DR neXtProt; NX_P53602; -.
DR PharmGKB; PA31330; -.
DR eggNOG; COG3407; -.
DR HOVERGEN; HBG051503; -.
DR InParanoid; P53602; -.
DR KO; K01597; -.
DR OMA; GIECYYT; -.
DR OrthoDB; EOG7K0ZCW; -.
DR PhylomeDB; P53602; -.
DR BioCyc; MetaCyc:ENSG00000167508-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_17015; Metabolism of proteins.
DR SABIO-RK; P53602; -.
DR UniPathway; UPA00063; -.
DR ChiTaRS; MVD; human.
DR EvolutionaryTrace; P53602; -.
DR GenomeRNAi; 4597; -.
DR NextBio; 17676; -.
DR PRO; PR:P53602; -.
DR ArrayExpress; P53602; -.
DR Bgee; P53602; -.
DR CleanEx; HS_MVD; -.
DR Genevestigator; P53602; -.
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:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006695; P:cholesterol biosynthetic process; NAS:UniProtKB.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR005935; Mev_diP_decarb.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10977; PTHR10977; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF015950; Mev_P_decrbx; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01240; mevDPdecarb; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cholesterol biosynthesis;
KW Cholesterol metabolism; Complete proteome; Lipid biosynthesis;
KW Lipid metabolism; Lyase; Nucleotide-binding; Phosphoprotein;
KW Polymorphism; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 400 Diphosphomevalonate decarboxylase.
FT /FTId=PRO_0000087012.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 96 96 Phosphoserine.
FT VARIANT 278 278 N -> H (in dbSNP:rs34519538).
FT /FTId=VAR_051605.
FT MUTAGEN 17 17 N->A: 15-fold inflation in K(m) for
FT mevalonate diphosphate.
FT MUTAGEN 161 161 R->Q: 1000-fold diminution in specific
FT activity.
FT STRAND 10 14
FT STRAND 17 21
FT STRAND 26 28
FT TURN 29 32
FT STRAND 33 36
FT STRAND 38 43
FT TURN 45 47
FT STRAND 50 56
FT STRAND 64 67
FT HELIX 77 88
FT STRAND 110 118
FT TURN 120 122
FT HELIX 126 139
FT TURN 140 143
FT HELIX 149 155
FT HELIX 157 163
FT STRAND 164 170
FT STRAND 178 180
FT STRAND 183 187
FT HELIX 189 191
FT STRAND 195 202
FT HELIX 211 221
FT HELIX 223 231
FT HELIX 233 245
FT HELIX 249 268
FT STRAND 270 272
FT HELIX 279 295
FT STRAND 300 303
FT STRAND 306 308
FT STRAND 310 315
FT HELIX 316 318
FT HELIX 319 329
FT TURN 337 339
FT STRAND 340 343
FT HELIX 352 358
FT STRAND 366 375
FT HELIX 385 387
FT STRAND 392 394
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
//
ID MVD1_HUMAN Reviewed; 400 AA.
AC P53602; Q53Y65;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-1996, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Diphosphomevalonate decarboxylase;
DE EC=4.1.1.33;
DE AltName: Full=Mevalonate (diphospho)decarboxylase;
DE Short=MDDase;
DE AltName: Full=Mevalonate pyrophosphate decarboxylase;
GN Name=MVD; Synonyms=MPD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT yeast 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
RT 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP 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
RT of the cholesterol and nonsterol isoprene biosynthetic pathways.";
RL J. Lipid Res. 38:2216-2223(1997).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96, AND MASS
RP SPECTROMETRY.
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
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.,
RA Buerckstuemmer T., 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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), AND MUTAGENESIS OF ASN-17 AND
RP ARG-161.
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: Performs the first committed step in the biosynthesis of
CC isoprenes.
CC -!- CATALYTIC ACTIVITY: ATP + (R)-5-diphosphomevalonate = ADP +
CC phosphate + isopentenyl diphosphate + CO(2).
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.4 uM for (R)-5-diphosphomevalonate;
CC KM=0.32 mM for ATP;
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.
CC -!- SUBUNIT: Homodimer.
CC -!- TISSUE SPECIFICITY: Expressed in heart, skeletal muscle, lung,
CC liver, brain, pancreas, kidney and placenta.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase
CC family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_002452.1; NM_002461.1.
DR UniGene; Hs.252457; -.
DR PDB; 3D4J; X-ray; 2.40 A; A/B=1-400.
DR PDBsum; 3D4J; -.
DR ProteinModelPortal; P53602; -.
DR SMR; P53602; 8-396.
DR IntAct; P53602; 3.
DR MINT; MINT-5004338; -.
DR STRING; 9606.ENSP00000301012; -.
DR BindingDB; P53602; -.
DR ChEMBL; CHEMBL4340; -.
DR GuidetoPHARMACOLOGY; 642; -.
DR PhosphoSite; P53602; -.
DR DMDM; 1706681; -.
DR PaxDb; P53602; -.
DR PRIDE; P53602; -.
DR DNASU; 4597; -.
DR Ensembl; ENST00000301012; ENSP00000301012; ENSG00000167508.
DR GeneID; 4597; -.
DR KEGG; hsa:4597; -.
DR UCSC; uc002flf.1; human.
DR CTD; 4597; -.
DR GeneCards; GC16M088718; -.
DR HGNC; HGNC:7529; MVD.
DR HPA; HPA041404; -.
DR HPA; HPA048250; -.
DR MIM; 603236; gene.
DR neXtProt; NX_P53602; -.
DR PharmGKB; PA31330; -.
DR eggNOG; COG3407; -.
DR HOVERGEN; HBG051503; -.
DR InParanoid; P53602; -.
DR KO; K01597; -.
DR OMA; GIECYYT; -.
DR OrthoDB; EOG7K0ZCW; -.
DR PhylomeDB; P53602; -.
DR BioCyc; MetaCyc:ENSG00000167508-MONOMER; -.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_17015; Metabolism of proteins.
DR SABIO-RK; P53602; -.
DR UniPathway; UPA00063; -.
DR ChiTaRS; MVD; human.
DR EvolutionaryTrace; P53602; -.
DR GenomeRNAi; 4597; -.
DR NextBio; 17676; -.
DR PRO; PR:P53602; -.
DR ArrayExpress; P53602; -.
DR Bgee; P53602; -.
DR CleanEx; HS_MVD; -.
DR Genevestigator; P53602; -.
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:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006695; P:cholesterol biosynthetic process; NAS:UniProtKB.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR006204; GHMP_kinase_N_dom.
DR InterPro; IPR005935; Mev_diP_decarb.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR PANTHER; PTHR10977; PTHR10977; 1.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR PIRSF; PIRSF015950; Mev_P_decrbx; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR01240; mevDPdecarb; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cholesterol biosynthesis;
KW Cholesterol metabolism; Complete proteome; Lipid biosynthesis;
KW Lipid metabolism; Lyase; Nucleotide-binding; Phosphoprotein;
KW Polymorphism; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 400 Diphosphomevalonate decarboxylase.
FT /FTId=PRO_0000087012.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 96 96 Phosphoserine.
FT VARIANT 278 278 N -> H (in dbSNP:rs34519538).
FT /FTId=VAR_051605.
FT MUTAGEN 17 17 N->A: 15-fold inflation in K(m) for
FT mevalonate diphosphate.
FT MUTAGEN 161 161 R->Q: 1000-fold diminution in specific
FT activity.
FT STRAND 10 14
FT STRAND 17 21
FT STRAND 26 28
FT TURN 29 32
FT STRAND 33 36
FT STRAND 38 43
FT TURN 45 47
FT STRAND 50 56
FT STRAND 64 67
FT HELIX 77 88
FT STRAND 110 118
FT TURN 120 122
FT HELIX 126 139
FT TURN 140 143
FT HELIX 149 155
FT HELIX 157 163
FT STRAND 164 170
FT STRAND 178 180
FT STRAND 183 187
FT HELIX 189 191
FT STRAND 195 202
FT HELIX 211 221
FT HELIX 223 231
FT HELIX 233 245
FT HELIX 249 268
FT STRAND 270 272
FT HELIX 279 295
FT STRAND 300 303
FT STRAND 306 308
FT STRAND 310 315
FT HELIX 316 318
FT HELIX 319 329
FT TURN 337 339
FT STRAND 340 343
FT HELIX 352 358
FT STRAND 366 375
FT HELIX 385 387
FT STRAND 392 394
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
//
MIM
603236
*RECORD*
*FIELD* NO
603236
*FIELD* TI
*603236 MEVALONATE PYROPHOSPHATE DECARBOXYLASE; MVD
;;MPD
*FIELD* TX
DESCRIPTION
read moreThe enzyme mevalonate pyrophosphate decarboxylase (MVD; EC 4.1.1.33)
catalyzes the conversion of mevalonate pyrophosphate into isopentenyl
pyrophosphate. This unusual enzyme decarboxylates and dehydrates its
substrate while hydrolyzing ATP. As a unique enzyme in one of the early
steps in cholesterol biosynthesis, MVD may be a useful target for drugs
aimed at lowering serum cholesterol levels (summary by Toth and Huwyler,
1996).
CLONING
Toth and Huwyler (1996) cloned the human MVD gene from a liver cDNA
library. The cDNA encoded a 400-amino acid polypeptide. Northern blot
analysis revealed a 2-kb mRNA present at similar levels in various human
tissues. Expression studies indicated that the recombinant human enzyme
is active as a 43-kD homodimer.
MAPPING
Gross (2012) mapped the MVD gene to chromosome 16q24.3 based on an
alignment of the MVD sequence (GenBank GENBANK BC000011) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 6/19/2012.
2. Toth, M. J.; Huwyler, L.: Molecular cloning and expression of
the cDNAs encoding human and yeast mevalonate pyrophosphate decarboxylase. J.
Biol. Chem. 271: 7895-7898, 1996.
*FIELD* CN
Matthew B. Gross - updated: 06/19/2012
*FIELD* CD
Jennifer P. Macke: 10/29/1998
*FIELD* ED
mgross: 06/19/2012
carol: 6/18/2012
carol: 6/15/2012
alopez: 10/29/1998
*RECORD*
*FIELD* NO
603236
*FIELD* TI
*603236 MEVALONATE PYROPHOSPHATE DECARBOXYLASE; MVD
;;MPD
*FIELD* TX
DESCRIPTION
read moreThe enzyme mevalonate pyrophosphate decarboxylase (MVD; EC 4.1.1.33)
catalyzes the conversion of mevalonate pyrophosphate into isopentenyl
pyrophosphate. This unusual enzyme decarboxylates and dehydrates its
substrate while hydrolyzing ATP. As a unique enzyme in one of the early
steps in cholesterol biosynthesis, MVD may be a useful target for drugs
aimed at lowering serum cholesterol levels (summary by Toth and Huwyler,
1996).
CLONING
Toth and Huwyler (1996) cloned the human MVD gene from a liver cDNA
library. The cDNA encoded a 400-amino acid polypeptide. Northern blot
analysis revealed a 2-kb mRNA present at similar levels in various human
tissues. Expression studies indicated that the recombinant human enzyme
is active as a 43-kD homodimer.
MAPPING
Gross (2012) mapped the MVD gene to chromosome 16q24.3 based on an
alignment of the MVD sequence (GenBank GENBANK BC000011) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Gross, M. B.: Personal Communication. Baltimore, Md. 6/19/2012.
2. Toth, M. J.; Huwyler, L.: Molecular cloning and expression of
the cDNAs encoding human and yeast mevalonate pyrophosphate decarboxylase. J.
Biol. Chem. 271: 7895-7898, 1996.
*FIELD* CN
Matthew B. Gross - updated: 06/19/2012
*FIELD* CD
Jennifer P. Macke: 10/29/1998
*FIELD* ED
mgross: 06/19/2012
carol: 6/18/2012
carol: 6/15/2012
alopez: 10/29/1998