MVD1_ASPFU
ID MVD1_ASPFU Reviewed; 404 AA.
AC Q4WNV9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Diphosphomevalonate decarboxylase mvd1 {ECO:0000303|PubMed:16110826};
DE EC=4.1.1.33 {ECO:0000305|PubMed:16110826};
DE AltName: Full=Ergosterol biosynthesis protein mvd1 {ECO:0000303|PubMed:16110826};
DE AltName: Full=Mevalonate pyrophosphate decarboxylase {ECO:0000303|PubMed:16110826};
DE AltName: Full=Mevalonate-5-diphosphate decarboxylase {ECO:0000303|PubMed:16110826};
DE Short=MDDase {ECO:0000303|PubMed:16110826};
GN Name=mvd1 {ECO:0000303|PubMed:16110826}; ORFNames=AFUA_4G07130;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2]
RP IDENTIFICATION, AND FUNCTION.
RX PubMed=16110826; DOI=10.1080/13693780400029114;
RA Ferreira M.E., Colombo A.L., Paulsen I., Ren Q., Wortman J., Huang J.,
RA Goldman M.H., Goldman G.H.;
RT "The ergosterol biosynthesis pathway, transporter genes, and azole
RT resistance in Aspergillus fumigatus.";
RL Med. Mycol. 43:S313-S319(2005).
RN [3]
RP FUNCTION.
RX PubMed=22106303; DOI=10.1073/pnas.1106399108;
RA Yasmin S., Alcazar-Fuoli L., Gruendlinger M., Puempel T., Cairns T.,
RA Blatzer M., Lopez J.F., Grimalt J.O., Bignell E., Haas H.;
RT "Mevalonate governs interdependency of ergosterol and siderophore
RT biosyntheses in the fungal pathogen Aspergillus fumigatus.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E497-E504(2012).
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). Mvd1 converts diphosphomevalonate into
CC isopentenyl diphosphate (By similarity). 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 (AFUA_4G07780) first converts mevalonate into
CC 5-phosphomevalonate. 5-phosphomevalonate is then further converted to
CC 5-diphosphomevalonate by the phosphomevalonate kinase erg8
CC (AFUA_5G10680). The diphosphomevalonate decarboxylase mvd1
CC (AFUA_4G07130) then produces isopentenyl diphosphate. The isopentenyl-
CC diphosphate delta-isomerase idi1 (AFUA_6G11160) then catalyzes the 1,3-
CC allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to
CC its highly electrophilic allylic isomer, dimethylallyl diphosphate
CC (DMAPP). Finally the farnesyl diphosphate synthase erg20 (AFUA_5G02450)
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
CC (PubMed:16110826, PubMed:22106303) (Probable).
CC {ECO:0000250|UniProtKB:P32377, ECO:0000305|PubMed:16110826,
CC ECO:0000305|PubMed:22106303}.
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:0000305|PubMed:16110826};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23733;
CC Evidence={ECO:0000305|PubMed:16110826};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 3/3. {ECO:0000305|PubMed:16110826}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P32377}.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000005; EAL90075.1; -; Genomic_DNA.
DR RefSeq; XP_752113.1; XM_747020.1.
DR STRING; 746128.CADAFUBP00006247; -.
DR EnsemblFungi; EAL90075; EAL90075; AFUA_4G07130.
DR GeneID; 3509586; -.
DR KEGG; afm:AFUA_4G07130; -.
DR VEuPathDB; FungiDB:Afu4g07130; -.
DR eggNOG; KOG2833; Eukaryota.
DR HOGENOM; CLU_040369_4_2_1; -.
DR InParanoid; Q4WNV9; -.
DR OMA; LTLHAMM; -.
DR OrthoDB; 1065019at2759; -.
DR UniPathway; UPA00057; UER00100.
DR Proteomes; UP000002530; Chromosome 4.
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..404
FT /note="Diphosphomevalonate decarboxylase mvd1"
FT /id="PRO_0000454154"
FT BINDING 25..28
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 82
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 161..166
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 217
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
SQ SEQUENCE 404 AA; 43154 MW; 4A44AD02DB7F4739 CRC64;
MAATSDRTVY RATTTAPVNI AVIKYWGKRD ASLNLPTNSS LSVTLSQRSL RTLTTASCSA
IYPAADELIL NGKPQDIQTS KRTLACLSNL RSLRQALENA DPSLPKLSTL PLRIVSENNF
PTAAGLASSA AGFAALVRAV ADLYQLPQSP LELSRIARQG SGSACRSLMG GYVAWRAGER
EDGSDSLAEE VAPASHWPEM RAIILVVSAE KKDVPSTEGM QTTVATSSLF ATRAASVVPE
RMAAIETAIQ NKDFATFAEI TMRDSNSFHA TCLDSWPPIF YMNDVSRAAV RLVHDINRAV
GRTVCAYTFD AGPNAVIYYL EKDSEVVAGT IKAILGPNTE GFDGPFYDIL KNVTASVVPL
EKVDSRAVEI LKNGISRVIL TGVGEGPISV EDHLVSATGD ILAS
