MVD1_ASHGO
ID MVD1_ASHGO Reviewed; 397 AA.
AC Q751D8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 03-AUG-2022, entry version 112.
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=AGL232C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54259.2; -; Genomic_DNA.
DR RefSeq; NP_986435.2; NM_211497.2.
DR AlphaFoldDB; Q751D8; -.
DR SMR; Q751D8; -.
DR STRING; 33169.AAS54259; -.
DR EnsemblFungi; AAS54259; AAS54259; AGOS_AGL232C.
DR GeneID; 4622728; -.
DR KEGG; ago:AGOS_AGL232C; -.
DR eggNOG; KOG2833; Eukaryota.
DR HOGENOM; CLU_040369_4_2_1; -.
DR InParanoid; Q751D8; -.
DR OMA; LTLHAMM; -.
DR UniPathway; UPA00057; UER00100.
DR Proteomes; UP000000591; Chromosome VII.
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; IBA:GO_Central.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
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..397
FT /note="Diphosphomevalonate decarboxylase"
FT /id="PRO_0000310439"
FT REGION 378..397
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 397 AA; 43535 MW; 869FCAA53C7C4FFC CRC64;
MSIYVASTTA PVNIATLKYW GKRDSMLNLP TNSSISVTLS QEDLRTLTSA ATGPELAEDR
LWLNGKPESL GNARTQQCLA DLRALRRALE TEEPDLPRMS EWKLHIVSEN NFPTAAGLAS
SAAGFAALVV AVAKLYGLPQ DYSEISKIAR KGSGSACRSL YGGYVAWEMG AEADGSDSRA
VQIADVEHWP EMRAAILVVS ADRKDTPSTS GMQQTVHTSD LFKERVATVV PRRYGEMAAA
IRARDFATFA RLTMQDSNSF HATCLDSFPP IFYMNDTSRR IVKLCHLINE FYNETIVAYT
FDAGPNAVLY YLAENEARLC GFLSAVFGAN DGWETTFSTE QRATFAAQFD ECVRGKLATD
LDDELHRGVA RLIFTKVGPG PQDTKSSLID PETGLPR
