ID   A0A0E0CDR8_9ORYZ        Unreviewed;       392 AA.
AC   A0A0E0CDR8;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Diphosphomevalonate decarboxylase {ECO:0000256|ARBA:ARBA00012296, ECO:0000256|PIRNR:PIRNR015950};
DE            EC=4.1.1.33 {ECO:0000256|ARBA:ARBA00012296, ECO:0000256|PIRNR:PIRNR015950};
OS   Oryza meridionalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI02G00230.3};
RN   [1] {ECO:0000313|EnsemblPlants:OMERI02G00230.3}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI02G00230.3};
RA   Wing R.A., Panaud O., Henry R.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:OMERI02G00230.3}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
CC   -!- FUNCTION: Performs the first committed step in the biosynthesis of
CC       isoprene-containing compounds such as sterols and terpenoids.
CC       {ECO:0000256|RuleBase:RU363086}.
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:0000256|PIRNR:PIRNR015950,
CC         ECO:0000256|RuleBase:RU363086};
CC   -!- SIMILARITY: Belongs to the diphosphomevalonate decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00008831, ECO:0000256|PIRNR:PIRNR015950,
CC       ECO:0000256|RuleBase:RU363086}.
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DR   AlphaFoldDB; A0A0E0CDR8; -.
DR   EnsemblPlants; OMERI02G00230.3; OMERI02G00230.3; OMERI02G00230.
DR   Gramene; OMERI02G00230.3; OMERI02G00230.3; OMERI02G00230.
DR   eggNOG; KOG2833; Eukaryota.
DR   HOGENOM; CLU_040369_4_1_1; -.
DR   Proteomes; UP000008021; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004163; F:diphosphomevalonate decarboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniRule.
DR   GO; GO:0016126; P:sterol biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.30.70.890; GHMP kinase, C-terminal domain; 2.
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_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR01240; mevDPdecarb; 1.
DR   PANTHER; PTHR10977; DIPHOSPHOMEVALONATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR10977:SF3; DIPHOSPHOMEVALONATE DECARBOXYLASE; 1.
DR   Pfam; PF00288; GHMP_kinases_N; 1.
DR   Pfam; PF18376; MDD_C; 1.
DR   PIRSF; PIRSF015950; Mev_P_decrbx; 2.
DR   SUPFAM; SSF55060; GHMP Kinase, C-terminal domain; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR015950};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516,
KW   ECO:0000256|RuleBase:RU363086};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098,
KW   ECO:0000256|PIRNR:PIRNR015950};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|PIRNR:PIRNR015950};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR015950};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW   Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955,
KW   ECO:0000256|RuleBase:RU363086};
KW   Steroid metabolism {ECO:0000256|RuleBase:RU363086};
KW   Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011,
KW   ECO:0000256|RuleBase:RU363086};
KW   Sterol metabolism {ECO:0000256|RuleBase:RU363086}.
FT   DOMAIN          116..174
FT                   /note="GHMP kinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00288"
FT   DOMAIN          205..264
FT                   /note="Mvd1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18376"
SQ   SEQUENCE   392 AA;  42696 MW;  7516869A2890EFA1 CRC64;
     MAAAEEGQWV LMATGRSPTN IAVIKYWGKR DEALILPVND SISVTLDPDH LSATTTVAVS
     PSFPSDRMWL NGKEISLSGG RFQSCLREIR KRAQDVEDEK KGIRIKKEDW GKLHVHIASY
     NNFPTAAGLA SSAAGLACFV FTLGKLMNVK EDHGELSSIA RQGSGSACRS IYGGFVKWCM
     GKNNDGSDSI AVQLADEAHW NDLVIIIAVV SSKQKETSST SGMRDSVETS PLLQYRAQTV
     VPERVLKMEE AIKSRNFESF ARIISLVEKW NQSEGTPRVA YTFDAGPNAV LIAPNRKNAT
     ILLQKLLYYF PPQDNDLSSY MVGDKSILSD AGLKSIEDVE ALPAPAETKM PSQKFKGDVS
     YFICSRLGAG PKVVTDESLA LIDSVTGLPK GV
//