MVD1_CANAL
ID MVD1_CANAL Reviewed; 362 AA.
AC A0A1D8PC43;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Diphosphomevalonate decarboxylase {ECO:0000305};
DE EC=4.1.1.33 {ECO:0000269|PubMed:12073030};
DE AltName: Full=Mevalonate pyrophosphate decarboxylase {ECO:0000305};
DE Short=MPD {ECO:0000305};
DE AltName: Full=Mevalonate-5-diphosphate decarboxylase {ECO:0000303|PubMed:12073030};
DE Short=MDD {ECO:0000305};
DE Short=MDDase {ECO:0000305};
GN Name=MVD {ECO:0000303|PubMed:12073030}; Synonyms=MVD1;
GN OrderedLocusNames=orf19.6105; ORFNames=CAALFM_C100070WA;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP INDUCTION, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=12073030; DOI=10.1007/s00438-002-0648-7;
RA Dassanayake R.S., Cao L., Samaranayake L.P., Berges T.;
RT "Characterization, heterologous expression and functional analysis of
RT mevalonate diphosphate decarboxylase gene (MVD) of Candida albicans.";
RL Mol. Genet. Genomics 267:281-290(2002).
RN [5]
RP FUNCTION.
RX PubMed=14653518; DOI=10.1080/1369378031000137233;
RA Song J.L., Lyons C.N., Holleman S., Oliver B.G., White T.C.;
RT "Antifungal activity of fluconazole in combination with lovastatin and
RT their effects on gene expression in the ergosterol and prenylation pathways
RT in Candida albicans.";
RL Med. Mycol. 41:417-425(2003).
RN [6]
RP INDUCTION.
RX PubMed=15917516; DOI=10.1128/aac.49.6.2226-2236.2005;
RA Liu T.T., Lee R.E., Barker K.S., Lee R.E., Wei L., Homayouni R.,
RA Rogers P.D.;
RT "Genome-wide expression profiling of the response to azole, polyene,
RT echinocandin, and pyrimidine antifungal agents in Candida albicans.";
RL Antimicrob. Agents Chemother. 49:2226-2236(2005).
RN [7]
RP INDUCTION.
RX PubMed=19527170; DOI=10.1086/599838;
RA Nett J.E., Lepak A.J., Marchillo K., Andes D.R.;
RT "Time course global gene expression analysis of an in vivo Candida
RT biofilm.";
RL J. Infect. Dis. 200:307-313(2009).
RN [8]
RP INDUCTION.
RX PubMed=22265407; DOI=10.1016/j.cell.2011.10.048;
RA Nobile C.J., Fox E.P., Nett J.E., Sorrells T.R., Mitrovich Q.M.,
RA Hernday A.D., Tuch B.B., Andes D.R., Johnson A.D.;
RT "A recently evolved transcriptional network controls biofilm development in
RT Candida albicans.";
RL Cell 148:126-138(2012).
CC -!- FUNCTION: Diphosphomevalonate decarboxylase; part of the second module
CC of ergosterol biosynthesis pathway that includes the middle steps of
CC the pathway (PubMed:12073030). MVD1 converts diphosphomevalonate into
CC isopentenyl diphosphate (PubMed:12073030). The second module is carried
CC out in the vacuole and involves the formation of farnesyl diphosphate,
CC which is also an important intermediate in the biosynthesis of
CC ubiquinone, dolichol, heme and prenylated proteins. Activity by the
CC mevalonate kinase ERG12 first converts mevalonate into 5-
CC phosphomevalonate. 5-phosphomevalonate is then further converted to 5-
CC diphosphomevalonate by the phosphomevalonate kinase ERG8. The
CC diphosphomevalonate decarboxylase MVD then produces isopentenyl
CC diphosphate. The isopentenyl-diphosphate delta-isomerase IDI1 then
CC catalyzes the 1,3-allylic rearrangement of the homoallylic substrate
CC isopentenyl (IPP) to its highly electrophilic allylic isomer,
CC dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate
CC synthase ERG20 catalyzes the sequential condensation of isopentenyl
CC pyrophosphate with dimethylallyl pyrophosphate, and then with the
CC resultant geranylpyrophosphate to the ultimate product farnesyl
CC pyrophosphate (Probable). {ECO:0000269|PubMed:12073030,
CC ECO:0000305|PubMed:14653518}.
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:0000269|PubMed:12073030};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23733;
CC Evidence={ECO:0000269|PubMed:12073030};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 3/3. {ECO:0000269|PubMed:12073030}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P32377}.
CC -!- INDUCTION: Expression is high in media supplemented with glucose,
CC moderate in acetate, galactose and low in maltose medium
CC (PubMed:12073030). Expression is higher in the yeast phase than in the
CC hyphal phase of growth as well as higher in the exponential than in the
CC stationary phase (PubMed:12073030). Expression is affected by
CC antifungals (PubMed:15917516). Expression is repressed during biofilm
CC formation (PubMed:19527170, PubMed:22265407).
CC {ECO:0000269|PubMed:12073030, ECO:0000269|PubMed:15917516,
CC ECO:0000269|PubMed:19527170, ECO:0000269|PubMed:22265407}.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; CP017623; AOW25709.1; -; Genomic_DNA.
DR RefSeq; XP_019330598.1; XM_019475053.1.
DR AlphaFoldDB; A0A1D8PC43; -.
DR SMR; A0A1D8PC43; -.
DR STRING; 237561.A0A1D8PC43; -.
DR GeneID; 3639306; -.
DR KEGG; cal:CAALFM_C100070WA; -.
DR CGD; CAL0000181620; MVD.
DR VEuPathDB; FungiDB:C1_00070W_A; -.
DR eggNOG; KOG2833; Eukaryota.
DR OMA; LTLHAMM; -.
DR OrthoDB; 1065019at2759; -.
DR UniPathway; UPA00057; UER00100.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; IGI:CGD.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IGI:CGD.
DR GO; GO:0016126; P:sterol biosynthetic process; IGI:CGD.
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 1: Evidence at protein level;
KW ATP-binding; Lipid biosynthesis; Lipid metabolism; Lyase;
KW Nucleotide-binding; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..362
FT /note="Diphosphomevalonate decarboxylase"
FT /id="PRO_0000454168"
FT BINDING 17..20
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 72
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 150..155
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 206
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
SQ SEQUENCE 362 AA; 39544 MW; C1E3FE2AC040C8D3 CRC64;
MYSASVTAPV NIATLKYWGK RDKSLNLPTN SSISVTLSQD DLRTLTTASA SESFEKDQLW
LNGKLESLDT PRTQACLADL RKLRASIEQS PDTPKLSQMK LHIVSENNFP TAAGLASSAA
GFAALVSAIA KLYELPQDMS ELSKIARKGS GSACRSLFGG FVAWEMGTLP DGQDSKAVEI
APLEHWPSLR AVILVVSDDK KDTPSTTGMQ STVATSDLFA HRIAEVVPQR FEAMKKAILD
KDFPKFAELT MKDSNSFHAV CLDSYPPIFY LNDTSKKIIK MVETINQQEV VAAYTFDAGP
NAVIYYDEAN QDKVLSLLYK HFGHVPGWKT HYTAETPVAG VSRIIQTSIG PGPQETSESL
TK
