MVD1_SCHPO
ID MVD1_SCHPO Reviewed; 393 AA.
AC O13963;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
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:0000250|UniProtKB:P32377};
DE AltName: Full=Mevalonate-5-diphosphate decarboxylase {ECO:0000250|UniProtKB:P32377};
DE Short=MDDase {ECO:0000250|UniProtKB:P32377};
GN Name=mvd1; ORFNames=SPAC24C9.03;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 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 mvd1 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 fps1 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:0000250|UniProtKB:P32377, ECO:0000305}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11260.1; -; Genomic_DNA.
DR PIR; T38344; T38344.
DR RefSeq; NP_594027.1; NM_001019452.2.
DR AlphaFoldDB; O13963; -.
DR SMR; O13963; -.
DR STRING; 4896.SPAC24C9.03.1; -.
DR MaxQB; O13963; -.
DR PaxDb; O13963; -.
DR EnsemblFungi; SPAC24C9.03.1; SPAC24C9.03.1:pep; SPAC24C9.03.
DR GeneID; 2541430; -.
DR KEGG; spo:SPAC24C9.03; -.
DR PomBase; SPAC24C9.03; mvd1.
DR VEuPathDB; FungiDB:SPAC24C9.03; -.
DR eggNOG; KOG2833; Eukaryota.
DR HOGENOM; CLU_040369_4_2_1; -.
DR InParanoid; O13963; -.
DR OMA; LTLHAMM; -.
DR PhylomeDB; O13963; -.
DR Reactome; R-SPO-191273; Cholesterol biosynthesis.
DR Reactome; R-SPO-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00057; UER00100.
DR PRO; PR:O13963; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; ISS:PomBase.
DR GO; GO:0006696; P:ergosterol biosynthetic process; ISS:PomBase.
DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IBA:GO_Central.
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; Cytoplasm; Lipid biosynthesis; Lipid metabolism; Lyase;
KW Nucleotide-binding; Nucleus; Reference proteome; Steroid biosynthesis;
KW Steroid metabolism; Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..393
FT /note="Diphosphomevalonate decarboxylase"
FT /id="PRO_0000310441"
FT BINDING 21..24
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 77
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 156..161
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 212
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
SQ SEQUENCE 393 AA; 42755 MW; CEA055DFB98A55C0 CRC64;
MDKKVYQCTV SAPVNIAVIK YWGKRDVALN LPTNSSISVT LSQDDLRTVT TASCSEKFEN
DTLWLNGNAE EIFANKRLRV CVEELRKARL DLEEENDDLD KIGALKLHVV SENNFPTAAG
LASSAAGYAA FCEAIARLYD LPWTPTQLSR IARQGSGSAC RSLFGGYVAW EMGELHSGAD
SVAVQVEPVE NWPEIRVAVL VASAAKKGVS STAGMQATVA SSTLFQHRIQ NIVPQRIQEM
KTAIRERDFE TFAKLTMTDS NQFHACCLDT FPPIFYLNDT SRAVIRVVEN INATAGKTIA
AYTFDAGPNA VIYFLEENSE IVLNTLYAVT KNAEGWSKQY GSSPVTVDSA AANIVSSGIS
RVILTRVGNG PRVLTIDESL IDASGNPKFI GSH
