MVD1_DICDI
ID MVD1_DICDI Reviewed; 391 AA.
AC Q54YQ9;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Diphosphomevalonate decarboxylase;
DE EC=4.1.1.33 {ECO:0000250|UniProtKB:P53602};
DE AltName: Full=Mevalonate (diphospho)decarboxylase;
DE Short=MDDase;
DE AltName: Full=Mevalonate pyrophosphate decarboxylase;
GN Name=mvd; ORFNames=DDB_G0278607;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Catalyzes the ATP dependent decarboxylation of (R)-5-
CC diphosphomevalonate to form isopentenyl diphosphate (IPP). Functions in
CC the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP),
CC a key precursor for the biosynthesis of isoprenoids and sterol
CC synthesis. {ECO:0000250|UniProtKB:P53602}.
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:P53602};
CC -!- PATHWAY: Steroid biosynthesis; cholesterol biosynthesis. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P53602}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53602}.
CC -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be located in the peroxisome.
CC However, was later shown to be cytosolic.
CC {ECO:0000250|UniProtKB:P53602}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AAFI02000023; EAL68476.1; -; Genomic_DNA.
DR RefSeq; XP_642143.1; XM_637051.1.
DR AlphaFoldDB; Q54YQ9; -.
DR SMR; Q54YQ9; -.
DR STRING; 44689.DDB0252847; -.
DR PaxDb; Q54YQ9; -.
DR EnsemblProtists; EAL68476; EAL68476; DDB_G0278607.
DR GeneID; 8621351; -.
DR KEGG; ddi:DDB_G0278607; -.
DR dictyBase; DDB_G0278607; mvd.
DR eggNOG; KOG2833; Eukaryota.
DR HOGENOM; CLU_040369_4_2_1; -.
DR InParanoid; Q54YQ9; -.
DR OMA; LTLHAMM; -.
DR PhylomeDB; Q54YQ9; -.
DR Reactome; R-DDI-191273; Cholesterol biosynthesis.
DR Reactome; R-DDI-446199; Synthesis of Dolichyl-phosphate.
DR UniPathway; UPA00063; -.
DR PRO; PR:Q54YQ9; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006695; P:cholesterol biosynthetic process; IEA:UniProtKB-UniPathway.
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; Cholesterol biosynthesis; Cholesterol metabolism; Cytoplasm;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Nucleotide-binding;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism.
FT CHAIN 1..391
FT /note="Diphosphomevalonate decarboxylase"
FT /id="PRO_0000328189"
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 142..147
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
FT BINDING 198
FT /ligand="(R)-5-diphosphomevalonate"
FT /ligand_id="ChEBI:CHEBI:57557"
FT /evidence="ECO:0000250|UniProtKB:O23722"
SQ SEQUENCE 391 AA; 43285 MW; 2F816038FC9CE51D CRC64;
MVLASVTCTA PVNIAVIKYW GKRDENIILP LNSSLSGTLH QDDLKTTTTI VASEDYTEDE
LYLNGKKEDI NAVRYQNVLK MIRSRATKLM DKKHCVHIAS INNFPTAAGL ASSASGYCCL
VFTLAQMYGV DGDISGIARL GSGSACRSMY GGFVKWEMGT KDDGSDSIAV QVQPESHWPD
MNIIVLVVND KKKETSSTDG MQKSAATSVM MKERCAVTVP NRMRDIEEAI NKKDFQTFGD
ITMKDSDDFH EVCATTTPPI YYLNDTSRYI MNLIHRYNKL SGSIKCAYTF DAGPNACIYL
PAESTTEVLS LFMKHFPGDD MQTYYRGPKE NIPSIENFVP SEKLASLYTP DTTFVNSLKY
ILHTKVGPGP QILSESESLI DNTTGLPKQL N
