EDSB_MAIZE
ID EDSB_MAIZE Reviewed; 557 AA.
AC A0A1D6EFT8; B6SYF3; B8A340;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Eudesmanediol synthase {ECO:0000303|PubMed:29570233};
DE Short=ZmEDS {ECO:0000303|PubMed:29570233};
DE EC=4.2.3.197 {ECO:0000269|PubMed:29570233};
DE AltName: Full=Terpene synthase 17 {ECO:0000303|PubMed:30187155};
DE AltName: Full=Terpene synthase 7 {ECO:0000312|EMBL:ACG29886.1};
GN Name=EDS {ECO:0000303|PubMed:29570233};
GN Synonyms=TPS17 {ECO:0000303|PubMed:30187155};
GN ORFNames=GRMZM2G010356 {ECO:0000303|PubMed:30187155},
GN ZEAMMB73_Zm00001d004509 {ECO:0000312|EMBL:ONM19045.1};
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. B73; TISSUE=Seedling;
RX PubMed=19965430; DOI=10.1126/science.1178534;
RA Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT "The B73 maize genome: complexity, diversity, and dynamics.";
RL Science 326:1112-1115(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT "Insights into corn genes derived from large-scale cDNA sequencing.";
RL Plant Mol. Biol. 69:179-194(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. B73;
RX PubMed=19936069; DOI=10.1371/journal.pgen.1000740;
RA Soderlund C., Descour A., Kudrna D., Bomhoff M., Boyd L., Currie J.,
RA Angelova A., Collura K., Wissotski M., Ashley E., Morrow D., Fernandes J.,
RA Walbot V., Yu Y.;
RT "Sequencing, mapping, and analysis of 27,455 maize full-length cDNAs.";
RL PLoS Genet. 5:E1000740-E1000740(2009).
RN [4]
RP FUNCTION, MUTAGENESIS OF PHE-303 AND TYR-529, CATALYTIC ACTIVITY, PATHWAY,
RP TISSUE SPECIFICITY, AND INDUCTION BY PATHOGEN INFECTION.
RC STRAIN=cv. Missouri 17;
RX PubMed=29570233; DOI=10.1111/tpj.13901;
RA Liang J., Liu J., Brown R., Jia M., Zhou K., Peters R.J., Wang Q.;
RT "Direct production of dihydroxylated sesquiterpenoids by a maize terpene
RT synthase.";
RL Plant J. 94:847-856(2018).
RN [5]
RP REVIEW.
RX PubMed=30187155; DOI=10.1007/s00425-018-2999-2;
RA Block A.K., Vaughan M.M., Schmelz E.A., Christensen S.A.;
RT "Biosynthesis and function of terpenoid defense compounds in maize (Zea
RT mays).";
RL Planta 249:21-30(2019).
CC -!- FUNCTION: Component of the volatile terpenes biosynthesis pathways
CC (PubMed:30187155). Dihydroxylated sesquiterpenoid synthase that
CC generates dually hydroxylated products directly from (E,E)-farnesyl
CC diphosphate, primarily eudesmane-2,11-diol, along with two closely
CC related structural isomers (PubMed:29570233).
CC {ECO:0000269|PubMed:29570233, ECO:0000303|PubMed:30187155}.
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:0000269|PubMed:29570233};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58165;
CC Evidence={ECO:0000269|PubMed:29570233};
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|PubMed:30187155}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in roots.
CC {ECO:0000269|PubMed:29570233}.
CC -!- INDUCTION: Induced by fungal pathogen infection (e.g.
CC F.verticillioide). {ECO:0000269|PubMed:29570233}.
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}.
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; CM007648; ONM19045.1; -; Genomic_DNA.
DR EMBL; EU957768; ACG29886.1; -; mRNA.
DR EMBL; BT055982; ACL54589.1; -; mRNA.
DR RefSeq; NP_001148146.1; NM_001154674.1.
DR AlphaFoldDB; A0A1D6EFT8; -.
DR SMR; A0A1D6EFT8; -.
DR STRING; 4577.GRMZM2G010356_P01; -.
DR EnsemblPlants; Zm00001eb089360_T001; Zm00001eb089360_P001; Zm00001eb089360.
DR GeneID; 100281754; -.
DR Gramene; Zm00001eb089360_T001; Zm00001eb089360_P001; Zm00001eb089360.
DR KEGG; zma:100281754; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR OMA; NSLHITT; -.
DR OrthoDB; 360509at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000007305; Chromosome 2.
DR ExpressionAtlas; A0A1D6EFT8; 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; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IEP:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046246; P:terpene biosynthetic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Plant defense;
KW Reference proteome.
FT CHAIN 1..557
FT /note="Eudesmanediol synthase"
FT /id="PRO_0000447517"
FT MOTIF 310..314
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
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 453
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
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:0000269|PubMed:29570233"
FT MUTAGEN 303
FT /note="F->A: Predominant production of hedycaryol."
FT /evidence="ECO:0000269|PubMed:29570233"
FT MUTAGEN 529
FT /note="Y->F: Increased accumulation of hedycaryol, but
FT presence of sesquiterpenoid diols."
FT /evidence="ECO:0000269|PubMed:29570233"
FT CONFLICT 37
FT /note="T -> P (in Ref. 2; ACG29886)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="I -> V (in Ref. 2; ACG29886)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="E -> D (in Ref. 2; ACG29886)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="R -> W (in Ref. 3; ACL54589)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="L -> V (in Ref. 2; ACG29886)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 63294 MW; 71909724979C8C57 CRC64;
MAPSNIVVQS SSTPPVAGGD EEFAPSVWGD FFVTYATPVS QASEQRMSER AELLKAQVRQ
AFDAASMDVA GLITYVDTLE 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 LLPAAQVVLN MARANEIIYL HGRDAYTFGA
DLKDLVTTLF LKQVLPL
