ID   MVD1_DANRE              Reviewed;         400 AA.
AC   Q5U403;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
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; Synonyms=mvda; ORFNames=zgc:100824;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2004) 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; BC085325; AAH85325.1; -; mRNA.
DR   RefSeq; NP_001007423.1; NM_001007422.1.
DR   AlphaFoldDB; Q5U403; -.
DR   SMR; Q5U403; -.
DR   STRING; 7955.ENSDARP00000098620; -.
DR   PaxDb; Q5U403; -.
DR   GeneID; 492781; -.
DR   KEGG; dre:492781; -.
DR   CTD; 492781; -.
DR   ZFIN; ZDB-GENE-041114-127; mvda.
DR   eggNOG; KOG2833; Eukaryota.
DR   InParanoid; Q5U403; -.
DR   OrthoDB; 1065019at2759; -.
DR   PhylomeDB; Q5U403; -.
DR   Reactome; R-DRE-191273; Cholesterol biosynthesis.
DR   Reactome; R-DRE-446199; Synthesis of Dolichyl-phosphate.
DR   UniPathway; UPA00063; -.
DR   PRO; PR:Q5U403; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
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; IBA:GO_Central.
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   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   ATP-binding; Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasm;
KW   Lipid biosynthesis; Lipid metabolism; Lyase; Nucleotide-binding;
KW   Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW   Sterol biosynthesis; Sterol metabolism.
FT   CHAIN           1..400
FT                   /note="Diphosphomevalonate decarboxylase"
FT                   /id="PRO_0000310438"
FT   BINDING         25..28
FT                   /ligand="(R)-5-diphosphomevalonate"
FT                   /ligand_id="ChEBI:CHEBI:57557"
FT                   /evidence="ECO:0000250|UniProtKB:O23722"
FT   BINDING         80
FT                   /ligand="(R)-5-diphosphomevalonate"
FT                   /ligand_id="ChEBI:CHEBI:57557"
FT                   /evidence="ECO:0000250|UniProtKB:O23722"
FT   BINDING         155..160
FT                   /ligand="(R)-5-diphosphomevalonate"
FT                   /ligand_id="ChEBI:CHEBI:57557"
FT                   /evidence="ECO:0000250|UniProtKB:O23722"
FT   BINDING         211
FT                   /ligand="(R)-5-diphosphomevalonate"
FT                   /ligand_id="ChEBI:CHEBI:57557"
FT                   /evidence="ECO:0000250|UniProtKB:O23722"
SQ   SEQUENCE   400 AA;  44599 MW;  1AC5DFDF8A9313FD CRC64;
     MSENILQDLE MVTCTAPVNI AVIKYWGKRD EDLILPVNAS LSVTLHQDHL RTTTTIACSR
     SFHKDCIWLN GKEQDISHPR LQSCLLEIRR LAQRRKNTGD PASDVSNKVH ICSVNNFPTA
     AGLASSAAGY ACLVYTLSQL FNVEGELSGV ARQGSGSACR SLYGGFVQWK LGEQSDGKDS
     IAEQVASELY WPELRVLILV VSAEQKSVGS TSGMHTSVET SHLLKYRADA VVPGRMEEMI
     RAIRLRDFPK FGELTMKDSN QFHAICLDTY PPIFYLNNIS HQIISLVHRY NQYYGETRVA
     YTFDAGPNAV IYSLQDYLPE FVEVVRHFFP PEVNEEEFFK GLPVCPADLS EEMIRDINMK
     PTPNGIRYMI STKAGPGPRV VEDPNLHLLG ADGLPKKSAV