MVD1_DEBHA
ID MVD1_DEBHA Reviewed; 388 AA.
AC Q6BY07;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Diphosphomevalonate decarboxylase {ECO:0000250|UniProtKB:P32377};
DE EC=4.1.1.33 {ECO:0000250|UniProtKB:P32377};
DE AltName: Full=Ergosterol biosynthesis protein 19 {ECO:0000250|UniProtKB:P32377};
DE AltName: Full=Mevalonate pyrophosphate decarboxylase {ECO:0000250|UniProtKB:P32377};
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=MVD1 {ECO:0000250|UniProtKB:P32377}; OrderedLocusNames=DEHA2A13398g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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 is carried out in the
CC vacuole and involves the formation of farnesyl diphosphate, which is
CC also an important intermediate in the biosynthesis of ubiquinone,
CC dolichol, heme and prenylated proteins (By similarity). 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 (By
CC similarity). The diphosphomevalonate decarboxylase MVD1/ERG19 then
CC produces isopentenyl diphosphate (By similarity). The isopentenyl-
CC diphosphate delta-isomerase IDI1 then catalyzes the 1,3-allylic
CC rearrangement of the homoallylic substrate isopentenyl (IPP) to its
CC highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP)
CC (By similarity). Finally the farnesyl diphosphate synthase ERG20
CC catalyzes the sequential condensation of isopentenyl pyrophosphate with
CC dimethylallyl pyrophosphate, and then with the resultant
CC geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (By
CC similarity). {ECO:0000250|UniProtKB:P32377}.
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:P32377};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23733;
CC Evidence={ECO:0000250|UniProtKB:P32377};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 3/3. {ECO:0000250|UniProtKB:P32377}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P32377}.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; CR382133; CAG84889.2; -; Genomic_DNA.
DR RefSeq; XP_456912.2; XM_456912.1.
DR AlphaFoldDB; Q6BY07; -.
DR SMR; Q6BY07; -.
DR STRING; 4959.XP_456912.2; -.
DR EnsemblFungi; CAG84889; CAG84889; DEHA2A13398g.
DR GeneID; 2899434; -.
DR KEGG; dha:DEHA2A13398g; -.
DR VEuPathDB; FungiDB:DEHA2A13398g; -.
DR eggNOG; KOG2833; Eukaryota.
DR HOGENOM; CLU_040369_4_2_1; -.
DR InParanoid; Q6BY07; -.
DR OMA; LTLHAMM; -.
DR OrthoDB; 1065019at2759; -.
DR UniPathway; UPA00057; UER00100.
DR Proteomes; UP000000599; Chromosome A.
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; 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 3: Inferred from homology;
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..388
FT /note="Diphosphomevalonate decarboxylase"
FT /id="PRO_0000310440"
FT REGION 367..388
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 74
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 153..158
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 209
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
SQ SEQUENCE 388 AA; 42538 MW; 759601F2FFEDDBB3 CRC64;
MTVYTSSATA PVNIATLKYW GKRDKSLNLP TNSSISVTLS QNDLRTLTSV AASEDFKEDK
LWLNGKLESL ESERTKACLA DLRTLRKELE SNDSSIPKLS QFGVHIVSEN NFPTAAGLAS
SAAGFAALVV SIAKLYELPQ NMSEISKIAR KGSGSACRSL FGGYVAWEMG QETNGEDSKA
VEVAPLSHWP NMKAAILVVS DDKKDTPSTS GMQTTVATSD LFQWRIKEVV PKRFDDMKDS
ILRKDFATFG DLTMKDSNSF HAVCLDSTPP IFYLNDTSKK IIKLIHELNK REGKIIAAYT
FDAGPNAVIY YEQENESKVL GVIYKYFSKV SGWEKLDTKT LDTTSDIQAD PELYKGVSKI
ILTEVGQGPQ GSSESLINDK GLPKAVAN
