MVD_GANLU
ID MVD_GANLU Reviewed; 400 AA.
AC G9BIY1;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 22-FEB-2012, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Diphosphomevalonate decarboxylase {ECO:0000250|UniProtKB:P32377};
DE EC=4.1.1.33 {ECO:0000250|UniProtKB:P32377};
DE AltName: Full=Mevalonate pyrophosphate decarboxylase {ECO:0000303|PubMed:22203490};
DE Short=MPD {ECO:0000250|UniProtKB:P32377};
DE AltName: Full=Mevalonate-5-diphosphate decarboxylase {ECO:0000250|UniProtKB:P32377};
DE Short=MDD {ECO:0000250|UniProtKB:P32377};
DE Short=MDDase {ECO:0000250|UniProtKB:P32377};
GN Name=MVD {ECO:0000303|PubMed:22203490};
OS Ganoderma lucidum (Ling zhi medicinal fungus) (Bracket fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Ganoderma.
OX NCBI_TaxID=5315;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], DEVELOPMENTAL STAGE, INDUCTION,
RP AND FUNCTION.
RC STRAIN=HG;
RX PubMed=22203490; DOI=10.1007/s11033-011-1431-9;
RA Shi L., Qin L., Xu Y., Ren A., Fang X., Mu D., Tan Q., Zhao M.;
RT "Molecular cloning, characterization, and function analysis of a mevalonate
RT pyrophosphate decarboxylase gene from Ganoderma lucidum.";
RL Mol. Biol. Rep. 39:6149-6159(2012).
RN [2]
RP FUNCTION.
RX PubMed=18540102; DOI=10.1271/bbb.80067;
RA Ding Y.X., Ou-Yang X., Shang C.H., Ren A., Shi L., Li Y.X., Zhao M.W.;
RT "Molecular cloning, characterization, and differential expression of a
RT farnesyl-diphosphate synthase gene from the basidiomycetous fungus
RT Ganoderma lucidum.";
RL Biosci. Biotechnol. Biochem. 72:1571-1579(2008).
RN [3]
RP FUNCTION.
RX PubMed=29476632; DOI=10.1002/bit.26583;
RA Wang W.F., Xiao H., Zhong J.J.;
RT "Biosynthesis of a ganoderic acid in Saccharomyces cerevisiae by expressing
RT a cytochrome P450 gene from Ganoderma lucidum.";
RL Biotechnol. Bioeng. 115:1842-1854(2018).
CC -!- FUNCTION: Diphosphomevalonate decarboxylase; part of the second module
CC of ergosterol biosynthesis pathway that includes the middle steps of
CC the pathway (By similarity). The second module involves the formation
CC of farnesyl diphosphate, which is also an important intermediate in the
CC biosynthesis of ubiquinone, dolichol, heme and prenylated proteins (By
CC similarity). This module also plays a key role in the biosynthesis of
CC triterpenes such as ganoderic acids (GA), a group of highly oxygenated
CC lanostane-type triterpenoids which are well recognized as a main group
CC of unique bioactive compounds in the medicinal mushroom Ganoderma
CC lucidum (PubMed:22203490, PubMed:29476632). Activity by the mevalonate
CC kinase first converts mevalonate into 5-phosphomevalonate (By
CC similarity). 5-phosphomevalonate is then further converted to 5-
CC diphosphomevalonate by the phosphomevalonate kinase (By similarity).
CC The diphosphomevalonate decarboxylase MVD then produces isopentenyl
CC diphosphate (PubMed:22203490). The isopentenyl-diphosphate delta-
CC isomerase then catalyzes the 1,3-allylic rearrangement of the
CC homoallylic substrate isopentenyl (IPP) to its highly electrophilic
CC allylic isomer, dimethylallyl diphosphate (DMAPP) (By similarity).
CC Finally the farnesyl diphosphate synthase FPS catalyzes the sequential
CC condensation of isopentenyl pyrophosphate with dimethylallyl
CC pyrophosphate, and then with the resultant geranylpyrophosphate to the
CC ultimate product farnesyl pyrophosphate (PubMed:18540102).
CC {ECO:0000250|UniProtKB:P32377, ECO:0000269|PubMed:18540102,
CC ECO:0000269|PubMed:22203490, ECO:0000269|PubMed:29476632}.
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:0000255|RuleBase:RU363086};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 3/3. {ECO:0000255|RuleBase:RU363086}.
CC -!- DEVELOPMENTAL STAGE: Expression levels are relatively low in the
CC mycelium. 53.9-fold higher expression level in the primordia than in
CC the 20-day old mycelia. {ECO:0000269|PubMed:22203490}.
CC -!- INDUCTION: By methyl jasmonate (MeJA). {ECO:0000269|PubMed:22203490}.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000255|RuleBase:RU363086, ECO:0000305}.
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DR EMBL; HQ596494; AEB00646.1; -; Genomic_DNA.
DR EMBL; HQ596495; AEB00647.1; -; mRNA.
DR AlphaFoldDB; G9BIY1; -.
DR SMR; G9BIY1; -.
DR BRENDA; 4.1.1.33; 2399.
DR UniPathway; UPA00057; UER00100.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; ISS:UniProtKB.
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; Lipid biosynthesis; Lipid metabolism; Lyase;
KW Nucleotide-binding; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..400
FT /note="Diphosphomevalonate decarboxylase"
FT /id="PRO_0000439249"
FT REGION 381..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 19..22
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 75
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 154..159
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 210
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
SQ SEQUENCE 400 AA; 43302 MW; CDDA36C26940EF2F CRC64;
MSVYQATASA PVNIACIKYW GKRDTKLILP TNSSLSVTLD QDHLRSTTTA RADPSFQKDR
LWLNGTEDEI KDGGRLATCI KEMKALRKQL EDKDASLPKI SSYSVHISSR NNFPTAAGLA
SSASGFAALV ASLAALYKLP TSQSDLSRIA RQGSGSACRS LFGGFVAWQM GELPDGSDSL
AVEIAPREHW PDIHALICVV NDEKKGTSST AGMQRTVETS PLLQHRIKHV VPARMAAISA
AIRTRDFDAF ARITMQDSNQ FHAVALDTEP PIFYMNDVSR AIIALIVEYN RVAVEKTGKL
KAAYTYDAGP NAVIYTPKEH IKEIVELIVK YFPQAENFKD PFGLFGAAGV QGKVVDGFNE
AVSKPFGVGA VKGLIHTRVG DGPRTLGPEE ALLSPDGLPK
