ID C9SCF9_VERA1 Unreviewed; 412 AA.
AC C9SCF9;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 63.
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=VDBG_02883 {ECO:0000313|EMBL:EEY16774.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
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|ARBA:ARBA00029323};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23733;
CC Evidence={ECO:0000256|ARBA:ARBA00029323};
CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate:
CC step 3/3. {ECO:0000256|ARBA:ARBA00005055,
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 EMBL; DS985216; EEY16774.1; -; Genomic_DNA.
DR RefSeq; XP_003006744.1; XM_003006698.1.
DR AlphaFoldDB; C9SCF9; -.
DR STRING; 526221.C9SCF9; -.
DR GeneID; 9532886; -.
DR KEGG; val:VDBG_02883; -.
DR eggNOG; KOG2833; Eukaryota.
DR HOGENOM; CLU_040369_4_2_1; -.
DR OMA; LTLHAMM; -.
DR OrthoDB; 458712at2759; -.
DR UniPathway; UPA00057; UER00100.
DR Proteomes; UP000008698; Unassembled WGS sequence.
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:UP000008698};
KW Steroid biosynthesis {ECO:0000256|ARBA:ARBA00022955,
KW ECO:0000256|RuleBase:RU363086};
KW Steroid metabolism {ECO:0000256|ARBA:ARBA00023221,
KW ECO:0000256|RuleBase:RU363086};
KW Sterol biosynthesis {ECO:0000256|ARBA:ARBA00023011,
KW ECO:0000256|RuleBase:RU363086};
KW Sterol metabolism {ECO:0000256|ARBA:ARBA00023166,
KW ECO:0000256|RuleBase:RU363086}.
FT DOMAIN 131..188
FT /note="GHMP kinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00288"
FT DOMAIN 219..396
FT /note="Mvd1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18376"
SQ SEQUENCE 412 AA; 43762 MW; 640F0A66C5FBBEF6 CRC64;
MLHHGRQPSL PGPAPQLLLT LRSSSPARLS KFFSPRTCYQ IRYWGKRDAK LNLPTNSSLS
VTLAQSDLRT LTTASTSASY PEGDSLILNG EPSDITGART QACFRELRAR RAALEASDSS
LPKLAALPLR VVSENNFPTA AGLASSAAGF AALVRAIADL YQLPDTPDQL SLVARQGSGS
ACRSLFGGYV AWRMGSAADG SDSKADLVAE ASHWPDMRAL ILVVSAAKKG VSSSSGMQQT
VATSGLFQQR IQTVVPANMD LMEQAIRDRD FAKFAEVTMR DSNSFHSTCA DTYPPIFYMN
DVSRAAIRAV EAINAAAGRT VAAYTFDAGP NAVIYYQEAD EATVVGAFTA VLDGVGGFKE
RAQGLKSEAK LDEVLAGILK GGVSRVIMTG VGEGPIKSDE YLVGEDGEPV KR
//
