MVD1_PANGI
ID MVD1_PANGI Reviewed; 417 AA.
AC D0EAP4;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 2.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Diphosphomevalonate decarboxylase 1 {ECO:0000305};
DE Short=Mevalonate diphosphate decarboxylase {ECO:0000303|Ref.1};
DE EC=4.1.1.33 {ECO:0000250|UniProtKB:O23722};
DE AltName: Full=Mevalonate pyrophosphate decarboxylase {ECO:0000303|PubMed:29509695};
GN Name=MVD1 {ECO:0000305};
GN Synonyms=MPD {ECO:0000303|PubMed:29509695}, MVD {ECO:0000303|Ref.1};
OS Panax ginseng (Korean ginseng).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Araliaceae; Panax.
OX NCBI_TaxID=4054;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Root hair;
RA Hou C., Zhao S.;
RT "Cloning and characterization of mevalonate diphosphate decarboxylase genes
RT in the important medicinal plant, Panax ginseng.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP REVIEW.
RX PubMed=29378087; DOI=10.1002/bab.1649;
RA Lu J., Li J., Wang S., Yao L., Liang W., Wang J., Gao W.;
RT "Advances in ginsenoside biosynthesis and metabolic regulation.";
RL Biotechnol. Appl. Biochem. 65:514-522(2018).
RN [3]
RP REVIEW, AND NOMENCLATURE.
RX PubMed=29509695; DOI=10.3390/molecules23030589;
RA Yang J.-L., Hu Z.-F., Zhang T.-T., Gu A.-D., Gong T., Zhu P.;
RT "Progress on the studies of the key enzymes of ginsenoside biosynthesis.";
RL Molecules 23:0-0(2018).
CC -!- FUNCTION: Performs the first committed step in the biosynthesis of
CC isoprene-containing compounds such as sterols and terpenoids (By
CC similarity). Component of the triterpene saponins (e.g. ginsenosides or
CC panaxosides) and phytosterols biosynthetic pathways (PubMed:29378087).
CC Catalyzes the conversion of mevalonate diphosphate to isopentenyl
CC diphosphate (IPP) (PubMed:29509695). {ECO:0000250|UniProtKB:O23722,
CC ECO:0000303|PubMed:29378087, ECO:0000303|PubMed:29509695}.
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:O23722};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 3/3. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O23722}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250|UniProtKB:O23722}.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; GQ455989; ACW83616.2; -; mRNA.
DR AlphaFoldDB; D0EAP4; -.
DR SMR; D0EAP4; -.
DR UniPathway; UPA00057; UER00100.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway.
DR GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
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; Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Nucleotide-binding; Peroxisome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..417
FT /note="Diphosphomevalonate decarboxylase 1"
FT /id="PRO_0000446949"
FT MOTIF 39..47
FT /note="Peroxisomal targeting signal PTS2"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 22..25
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 77
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 160..165
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 216
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
SQ SEQUENCE 417 AA; 46266 MW; EB183FD50027032B CRC64;
MAESWVIMVT AQTPINIAVI KYWGKRDETL ILPINDSIRV SLDPDHLCTT TTVSVRPSFE
QDRMWLNGKE ISLLGGRFQS CLREIRSRAR DLEDEKKGIV IKKMDWEKLH FHIASYNNFP
TAAGLASSAA GLACFVFALA KLLTLQEDNG QLSAIARRGS GSACRSLYGG FVKWIMGKEE
NGSDSIAVQL ADEKHWDDLV IVIAVVSARQ KETSSTTGMQ DSCKTSMLIQ HRAKEVVPKR
ILQMEDAIEK RDFPSFARLA CADSNQFHAV CLDTSPPIFY INDTSHKIIS CVEKWNRSVG
TPQVAYTFDA GPNAVLIARD RKIAALLLRR LLFHFPPHSN TDSNSYVIGD KSILQDVGVQ
DTKDIESLPP PPEIKDNIPA QKSNGDVSYF ICTRPGRGPV LLPDSRALLN PETGLPK
