EGS1_CLABR
ID EGS1_CLABR Reviewed; 318 AA.
AC D0VWT0; B2WSM9;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 2.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Eugenol synthase 1 {ECO:0000303|PubMed:18208524};
DE Short=CbEGS1 {ECO:0000303|PubMed:18208524};
DE EC=1.1.1.318 {ECO:0000269|PubMed:18208524};
GN Name=EGS1 {ECO:0000303|PubMed:18208524};
OS Clarkia breweri (Fairy fans) (Eucharidium breweri).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Clarkia.
OX NCBI_TaxID=36903;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN
RP COMPLEX WITH NADP, FUNCTION, MUTAGENESIS OF PHE-84 AND ILE-87, CATALYTIC
RP ACTIVITY, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=18208524; DOI=10.1111/j.1365-313x.2008.03412.x;
RA Koeduka T., Louie G.V., Orlova I., Kish C.M., Ibdah M., Wilkerson C.G.,
RA Bowman M.E., Baiga T.J., Noel J.P., Dudareva N., Pichersky E.;
RT "The multiple phenylpropene synthases in both Clarkia breweri and Petunia
RT hybrida represent two distinct protein lineages.";
RL Plant J. 54:362-374(2008).
CC -!- FUNCTION: Catalyzes the synthesis of the phenylpropene eugenol from
CC coniferyl acetate (PubMed:18208524). Phenylpropenes are produced by
CC plants as defense compounds with antimicrobial and antianimal
CC properties, or as floral attractants of pollinators (PubMed:18208524).
CC {ECO:0000269|PubMed:18208524}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a carboxylate + eugenol + NADP(+) = a coniferyl ester + NADPH;
CC Xref=Rhea:RHEA:32655, ChEBI:CHEBI:4917, ChEBI:CHEBI:29067,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64292;
CC EC=1.1.1.318; Evidence={ECO:0000269|PubMed:18208524};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:32657;
CC Evidence={ECO:0000269|PubMed:18208524};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + eugenol + NADP(+) = (E)-coniferyl acetate + NADPH;
CC Xref=Rhea:RHEA:24690, ChEBI:CHEBI:4917, ChEBI:CHEBI:30089,
CC ChEBI:CHEBI:47905, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.318; Evidence={ECO:0000269|PubMed:18208524};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24692;
CC Evidence={ECO:0000269|PubMed:18208524};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=93.3 uM for coniferyl acetate {ECO:0000269|PubMed:18208524};
CC Vmax=7.3 nmol/sec/mg enzyme with coniferyl acetate as substrate
CC {ECO:0000269|PubMed:18208524};
CC Note=kcat is 0.26 sec(-1) with coniferyl acetate as substrate.
CC {ECO:0000269|PubMed:18208524};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000269|PubMed:18208524}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in petals, and, to a lower extent,
CC in sepals, stamens and pistils. {ECO:0000269|PubMed:18208524}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; EF467239; ABR24113.1; -; mRNA.
DR PDB; 3C1O; X-ray; 1.80 A; A=1-318.
DR PDBsum; 3C1O; -.
DR AlphaFoldDB; D0VWT0; -.
DR SMR; D0VWT0; -.
DR BioCyc; MetaCyc:MON-13842; -.
DR UniPathway; UPA00711; -.
DR EvolutionaryTrace; D0VWT0; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0009699; P:phenylpropanoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05259; PCBER_SDR_a; 1.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR008030; NmrA-like.
DR InterPro; IPR045312; PCBER-like.
DR Pfam; PF05368; NmrA; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NADP; Nucleotide-binding; Oxidoreductase;
KW Phenylpropanoid metabolism.
FT CHAIN 1..318
FT /note="Eugenol synthase 1"
FT /id="PRO_0000451498"
FT ACT_SITE 131
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT BINDING 10..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18208524,
FT ECO:0007744|PDB:3C1O"
FT BINDING 32..43
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT BINDING 33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18208524,
FT ECO:0007744|PDB:3C1O"
FT BINDING 47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18208524,
FT ECO:0007744|PDB:3C1O"
FT BINDING 83
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18208524,
FT ECO:0007744|PDB:3C1O"
FT BINDING 84..86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT BINDING 109..111
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18208524,
FT ECO:0007744|PDB:3C1O"
FT BINDING 131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18208524,
FT ECO:0007744|PDB:3C1O"
FT BINDING 151..153
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:18208524,
FT ECO:0007744|PDB:3C1O"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT SITE 84
FT /note="Confers substrate specificity"
FT /evidence="ECO:0000269|PubMed:18208524"
FT SITE 87
FT /note="Confers substrate specificity"
FT /evidence="ECO:0000269|PubMed:18208524"
FT SITE 263
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT MUTAGEN 84
FT /note="F->V: Confers some isoeugenol synthase activity;
FT when associated with Y-87."
FT /evidence="ECO:0000269|PubMed:18208524"
FT MUTAGEN 87
FT /note="I->Y: Confers some isoeugenol synthase activity;
FT when associated with V-84."
FT /evidence="ECO:0000269|PubMed:18208524"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:3C1O"
FT TURN 8..10
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 14..23
FT /evidence="ECO:0007829|PDB:3C1O"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:3C1O"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 65..72
FT /evidence="ECO:0007829|PDB:3C1O"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:3C1O"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 122..141
FT /evidence="ECO:0007829|PDB:3C1O"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:3C1O"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:3C1O"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 189..201
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:3C1O"
FT STRAND 208..211
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3C1O"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 221..232
FT /evidence="ECO:0007829|PDB:3C1O"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 243..252
FT /evidence="ECO:0007829|PDB:3C1O"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:3C1O"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:3C1O"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:3C1O"
SQ SEQUENCE 318 AA; 36019 MW; A908B6421061C8F3 CRC64;
MEKIIIYGGT GYIGKFMVRA SLSFSHPTFI YARPLTPDST PSSVQLREEF RSMGVTIIEG
EMEEHEKMVS VLKQVDIVIS ALPFPMISSQ IHIINAIKAA GNIKRFLPSD FGCEEDRIKP
LPPFESVLEK KRIIRRAIEA AALPYTYVSA NCFGAYFVNY LLHPSPHPNR NDDIVIYGTG
ETKFVLNYEE DIAKYTIKVA CDPRCCNRIV IYRPPKNIIS QNELISLWEA KSGLSFKKVH
MPDEQLVRLS QELPQPQNIP VSILHSIFVK GDLMSYEMRK DDIEASNLYP ELEFTSIDGL
LDLFISGRAP PPTLAEFE
