ID A0A1J7H2A4_LUPAN Unreviewed; 420 AA.
AC A0A1J7H2A4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
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};
GN ORFNames=TanjilG_14338 {ECO:0000313|EMBL:OIW07000.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIW07000.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIW07000.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIW07000.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
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}.
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; CM007368; OIW07000.1; -; Genomic_DNA.
DR RefSeq; XP_019452383.1; XM_019596838.1.
DR AlphaFoldDB; A0A1J7H2A4; -.
DR STRING; 3871.A0A1J7H2A4; -.
DR EnsemblPlants; OIW07000; OIW07000; TanjilG_14338.
DR GeneID; 109354374; -.
DR Gramene; OIW07000; OIW07000; TanjilG_14338.
DR KEGG; lang:109354374; -.
DR OMA; LTLHAMM; -.
DR OrthoDB; 458712at2759; -.
DR Proteomes; UP000188354; Chromosome LG08.
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; 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_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; 1.
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:UP000188354};
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 115..173
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 204..403
FT /note="Mvd1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18376"
SQ SEQUENCE 420 AA; 46309 MW; 9D436E01C4B7FE17 CRC64;
MANESQKWVL MVTAQTPTNI AVIKYWGKRD ETLILPVNDS ISVTLDPNHL CTTTTVAVSP
TFQQDRMWLN GKEISLSGGR FQSCLREIRG RACDVEDKKK GIKITKEDWG KLHLHIASYN
NFPTAAGLAS SAAGFACLVY ALGKLMNVKE DESQLSAIAR QGSGSACRSL YGGFVKWIMG
KEDNGSDSLA VQLADEKHWD DLVIVIAVVS SRQKETSSTS GMCETVETSL LLQHRAKEVV
PKRILQMEEV IRNRDFASFS RLTCADSNQF HAVCLDTSPP IFYMNDTSHR IISIVEKWNR
SEEDPQVAYT FDAGPNAVLI ARNRKAAALL IQRLLYYFPP SSDDLDSYII GDKSIAKDAG
INGIADVEAL LPPPEVKDNI PSQKYTGDVS YFICTRPGRG PVLLSDESQA LLNGENGLPK
//
