EDSM_MAIZE
ID EDSM_MAIZE Reviewed; 557 AA.
AC A0A3L6G2C1;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Eudesmanediol synthase {ECO:0000305};
DE Short=ZmEDS {ECO:0000305};
DE EC=4.2.3.197 {ECO:0000250|UniProtKB:A0A1D6EFT8};
DE AltName: Full=(+)-germacrene D synthase {ECO:0000312|EMBL:PWZ40931.1};
DE AltName: Full=Terpene synthase 17 {ECO:0000305};
GN Name=EDS {ECO:0000305};
GN Synonyms=TPS17 {ECO:0000305}, TSGD1_1 {ECO:0000312|EMBL:PWZ40931.1};
GN ORFNames=Zm00014a_032508 {ECO:0000312|EMBL:PWZ40931.1};
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Missouri 17; TISSUE=Seedling;
RX PubMed=30061735; DOI=10.1038/s41588-018-0182-0;
RA Sun S., Zhou Y., Chen J., Shi J., Zhao H., Zhao H., Song W., Zhang M.,
RA Cui Y., Dong X., Liu H., Ma X., Jiao Y., Wang B., Wei X., Stein J.C.,
RA Glaubitz J.C., Lu F., Yu G., Liang C., Fengler K., Li B., Rafalski A.,
RA Schnable P.S., Ware D.H., Buckler E.S., Lai J.;
RT "Extensive intraspecific gene order and gene structural variations between
RT Mo17 and other maize genomes.";
RL Nat. Genet. 50:1289-1295(2018).
CC -!- FUNCTION: Component of the volatile terpenes biosynthesis pathways (By
CC similarity). Dihydroxylated sesquiterpenoid synthase that generates
CC dually hydroxylated products directly from (E,E)-farnesyl diphosphate,
CC primarily eudesmane-2,11-diol, along with two closely related
CC structural isomers (By similarity). {ECO:0000250|UniProtKB:A0A1D6EFT8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + 2 H2O = 7-epi-ent-eudesmane-
CC 5,11-diol + diphosphate; Xref=Rhea:RHEA:58164, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:142536, ChEBI:CHEBI:175763;
CC EC=4.2.3.197; Evidence={ECO:0000250|UniProtKB:A0A1D6EFT8};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58165;
CC Evidence={ECO:0000250|UniProtKB:A0A1D6EFT8};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000250|UniProtKB:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; NCVQ01000003; PWZ40931.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6G2C1; -.
DR SMR; A0A3L6G2C1; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Unplaced.
DR Proteomes; UP000251960; Chromosome 2.
DR ExpressionAtlas; A0A3L6G2C1; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Plant defense;
KW Reference proteome.
FT CHAIN 1..557
FT /note="Eudesmanediol synthase"
FT /id="PRO_0000447518"
FT MOTIF 310..314
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:B1B1U3"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 310
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 450
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT SITE 303
FT /note="Required for the use of hedycaryol as a transient
FT intermediate during the reprotonation of germacrene A"
FT /evidence="ECO:0000250|UniProtKB:A0A1D6EFT8"
SQ SEQUENCE 557 AA; 63237 MW; 692C90374F6FC7C7 CRC64;
MAPSNIVVQS SSTPPVAGGD EEFAPSVWGD FFVTYAPPVS QASEQRMSER AELLKAQVCQ
AFDAASMDVA GLVTYVDTLE RLGLDNHFRD LIGAALERIG AEELPEHGGG LHIVALRFRL
LRQHGIWVST DVFDAFREDA GGFCSSLCSD DPRGLLSLYN AAHMAVPGEV VLDDAIAFAR
GRLLDIISKG EVRSPVSEQI TRALDIPLPR FTRRLETMHY IAEYEHEEAH DGLLLELARL
NFVLVRALHL RELKDLSLWW RELYNTVKLP YARDRMVEIY FWTCGMLHEE EYSLARMFFA
KTFGMVSLMD DTFDVHATLD ECHKLKEAMQ RWDESEVSIL PEYLRLLYIK TLSNFKEFEE
ILEPNKKYRM AYTKEAYKLC SKNYLKEAIW SNQKYQPSFK EHEELSIMTS GLPMLTILTL
MGFGDEATPE AFEWVSSVPE MVRAGSQVTR FLNDLSSYKL GKNKKDMPGS VETYMVENGL
TGDEAAAAIA ALLENRWRIL NQTRMEIDHT LLPAVQVVVN MARANEIIYL HGRDAYTFGA
DLKDLVTTLF LKQVLPL
