MVD1_BOVIN
ID MVD1_BOVIN Reviewed; 400 AA.
AC Q0P570;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Diphosphomevalonate decarboxylase;
DE EC=4.1.1.33 {ECO:0000250|UniProtKB:P53602};
DE AltName: Full=Mevalonate (diphospho)decarboxylase;
DE Short=MDDase;
DE AltName: Full=Mevalonate pyrophosphate decarboxylase;
GN Name=MVD;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal muscle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:P53602}.
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:0000250|UniProtKB:P53602};
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P53602}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53602}.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be located in the peroxisome.
CC However, was later shown to be cytosolic.
CC {ECO:0000250|UniProtKB:P53602}.
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DR EMBL; BC120432; AAI20433.1; -; mRNA.
DR RefSeq; NP_001068892.1; NM_001075424.1.
DR AlphaFoldDB; Q0P570; -.
DR SMR; Q0P570; -.
DR STRING; 9913.ENSBTAP00000015994; -.
DR PaxDb; Q0P570; -.
DR PeptideAtlas; Q0P570; -.
DR PRIDE; Q0P570; -.
DR Ensembl; ENSBTAT00000015994; ENSBTAP00000015994; ENSBTAG00000012059.
DR GeneID; 509958; -.
DR KEGG; bta:509958; -.
DR CTD; 4597; -.
DR VEuPathDB; HostDB:ENSBTAG00000012059; -.
DR VGNC; VGNC:31767; MVD.
DR eggNOG; KOG2833; Eukaryota.
DR GeneTree; ENSGT00390000015359; -.
DR HOGENOM; CLU_040369_4_4_1; -.
DR InParanoid; Q0P570; -.
DR OMA; LTLHAMM; -.
DR OrthoDB; 1065019at2759; -.
DR TreeFam; TF105952; -.
DR Reactome; R-BTA-191273; Cholesterol biosynthesis.
DR Reactome; R-BTA-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00063; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000012059; Expressed in diaphragm and 106 other tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.30.70.890; -; 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_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR Pfam; PF00288; GHMP_kinases_N; 1.
DR Pfam; PF18376; MDD_C; 1.
DR PIRSF; PIRSF015950; Mev_P_decrbx; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55060; SSF55060; 1.
DR TIGRFAMs; TIGR01240; mevDPdecarb; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cholesterol biosynthesis; Cholesterol metabolism;
KW Cytoplasm; Lipid biosynthesis; Lipid metabolism; Lyase; Nucleotide-binding;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P53602"
FT CHAIN 2..400
FT /note="Diphosphomevalonate decarboxylase"
FT /id="PRO_0000310437"
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:0000250|UniProtKB:P53602"
SQ SEQUENCE 400 AA; 43732 MW; C659D6635C9EF49B CRC64;
MASEKPIVVV TCTAPVNIAV VKYWGKRDEE LILPINSSLS VTLHQDQLKT TTTAAISRDF
TEDRIWLNGR EEDMGHPRLQ ACLREIRRLA RKRRSDGHED PLPLSLSYKV HVASENNFPT
AAGLASSAAG YACLAYTLAR VYGVDSDLSE VARRGSGSAC RSLYGGFVEW QMGERPDGKD
SVACQVAPES HWPELRVLIL VVSAERKPMG STAGMQTSVE TSALLKFRAE ALVPPRMAEM
TRCIRERNFQ AFGQLTMKDS NQFHATCLDT FPPISYLSDT SRRIIQLVHR FNAHHGQTKV
AYTFDAGPNA VVFTLDDTVA EFVAAVRHSF PPESNGDKFL KGLPVEPVLL SDELKAVLGM
DPVPGSIRYI IATQVGPGPQ VLDDPGAHLL GPDGLPKPAA
