EGS1_OCIBA
ID EGS1_OCIBA Reviewed; 314 AA.
AC Q15GI4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Eugenol synthase 1 {ECO:0000303|PubMed:16782809, ECO:0000303|PubMed:18208524};
DE Short=ObEGS1 {ECO:0000303|PubMed:18208524};
DE EC=1.1.1.318 {ECO:0000269|PubMed:16782809, ECO:0000269|PubMed:17912370};
GN Name=EGS1 {ECO:0000303|PubMed:16782809, ECO:0000303|PubMed:18208524};
OS Ocimum basilicum (Sweet basil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Ociminae;
OC Ocimum.
OX NCBI_TaxID=39350;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=cv. SW; TISSUE=Trichome gland;
RX PubMed=16782809; DOI=10.1073/pnas.0603732103;
RA Koeduka T., Fridman E., Gang D.R., Vassao D.G., Jackson B.L., Kish C.M.,
RA Orlova I., Spassova S.M., Lewis N.G., Noel J.P., Baiga T.J., Dudareva N.,
RA Pichersky E.;
RT "Eugenol and isoeugenol, characteristic aromatic constituents of spices,
RT are biosynthesized via reduction of a coniferyl alcohol ester.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10128-10133(2006).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH NADP AND A
RP COMPETITIVE INHIBITOR, FUNCTION, MUTAGENESIS OF LYS-132; TYR-157; ILE-261
RP AND PHE-314, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVE SITE.
RX PubMed=17912370; DOI=10.1371/journal.pone.0000993;
RA Louie G.V., Baiga T.J., Bowman M.E., Koeduka T., Taylor J.H.,
RA Spassova S.M., Pichersky E., Noel J.P.;
RT "Structure and reaction mechanism of basil eugenol synthase.";
RL PLoS ONE 2:e993-e993(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH NADP, MUTAGENESIS OF
RP PHE-85 AND ILE-88, GENE FAMILY, AND 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:16782809, PubMed:17912370). Phenylpropenes
CC are produced by plants as defense compounds with antimicrobial and
CC antianimal properties, or as floral attractants of pollinators
CC (PubMed:16782809). Eugenol is a characteristic aromatic constituent of
CC spices (PubMed:16782809). {ECO:0000269|PubMed:16782809,
CC ECO:0000269|PubMed:17912370}.
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:16782809,
CC ECO:0000269|PubMed:17912370};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24692;
CC Evidence={ECO:0000269|PubMed:16782809, ECO:0000269|PubMed:17912370};
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:16782809,
CC ECO:0000269|PubMed:17912370};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:32657;
CC Evidence={ECO:0000269|PubMed:16782809, ECO:0000269|PubMed:17912370};
CC -!- ACTIVITY REGULATION: Inhibited by zinc and copper ions
CC (PubMed:16782809). Repressed by 4-bromo-cinnamyl acetate
CC (PubMed:16782809). Desactivated by the competitive inhibitor EMDF
CC ((7S,8S)-ethyl(7,8-methylene)-dihydroferulate) (PubMed:17912370).
CC {ECO:0000269|PubMed:16782809, ECO:0000269|PubMed:17912370}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5.1 mM for coniferyl acetate (at pH 6.5 and 28 degrees Celsius)
CC {ECO:0000269|PubMed:16782809};
CC KM=0.57 mM for coniferyl acetate (at pH 6.5 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:17912370};
CC KM=131 uM for NADPH (at pH 6.5 and 28 degrees Celsius)
CC {ECO:0000269|PubMed:16782809};
CC Vmax=19.9 nmol/sec/mg enzyme (at pH 6.5 and 28 degrees Celsius)
CC {ECO:0000269|PubMed:16782809};
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:16782809};
CC -!- PATHWAY: Aromatic compound metabolism; phenylpropanoid biosynthesis.
CC {ECO:0000269|PubMed:16782809}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17912370}.
CC -!- TISSUE SPECIFICITY: Trichome glands. {ECO:0000269|PubMed:16782809}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; DQ372812; ABD17321.1; -; mRNA.
DR PDB; 2QW8; X-ray; 1.60 A; A/B=1-314.
DR PDB; 2QX7; X-ray; 1.75 A; A/B=1-314.
DR PDB; 2QYS; X-ray; 1.80 A; A/B=1-314.
DR PDB; 2QZZ; X-ray; 1.60 A; A/B=1-314.
DR PDB; 2R2G; X-ray; 1.80 A; A/B=1-314.
DR PDB; 2R6J; X-ray; 1.50 A; A/B=1-314.
DR PDB; 3C3X; X-ray; 2.15 A; A/B=1-314.
DR PDBsum; 2QW8; -.
DR PDBsum; 2QX7; -.
DR PDBsum; 2QYS; -.
DR PDBsum; 2QZZ; -.
DR PDBsum; 2R2G; -.
DR PDBsum; 2R6J; -.
DR PDBsum; 3C3X; -.
DR AlphaFoldDB; Q15GI4; -.
DR SMR; Q15GI4; -.
DR KEGG; ag:ABD17321; -.
DR BioCyc; MetaCyc:MON-13834; -.
DR BRENDA; 1.1.1.318; 4385.
DR SABIO-RK; Q15GI4; -.
DR UniPathway; UPA00711; -.
DR EvolutionaryTrace; Q15GI4; -.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0042855; P:eugenol biosynthetic process; IDA:UniProtKB.
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..314
FT /note="Eugenol synthase 1"
FT /id="PRO_0000314576"
FT ACT_SITE 132
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000269|PubMed:17912370"
FT BINDING 16..19
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17912370,
FT ECO:0000269|PubMed:18208524, ECO:0007744|PDB:2QW8,
FT ECO:0007744|PDB:2QX7, ECO:0007744|PDB:2QZZ,
FT ECO:0007744|PDB:2R2G, ECO:0007744|PDB:2R6J,
FT ECO:0007744|PDB:3C3X"
FT BINDING 38..44
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17912370,
FT ECO:0000269|PubMed:18208524, ECO:0007744|PDB:2QW8,
FT ECO:0007744|PDB:2QX7, ECO:0007744|PDB:2QZZ,
FT ECO:0007744|PDB:2R2G, ECO:0007744|PDB:2R6J,
FT ECO:0007744|PDB:3C3X"
FT BINDING 39
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 85..87
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17912370,
FT ECO:0007744|PDB:2QW8, ECO:0007744|PDB:2QX7,
FT ECO:0007744|PDB:2QZZ, ECO:0007744|PDB:2R2G,
FT ECO:0007744|PDB:2R6J"
FT BINDING 110..112
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17912370,
FT ECO:0000269|PubMed:18208524, ECO:0007744|PDB:2QW8,
FT ECO:0007744|PDB:2QX7, ECO:0007744|PDB:2QZZ,
FT ECO:0007744|PDB:2R2G, ECO:0007744|PDB:2R6J,
FT ECO:0007744|PDB:3C3X"
FT BINDING 114
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:17912370,
FT ECO:0007744|PDB:2QZZ, ECO:0007744|PDB:2R2G"
FT BINDING 132
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17912370,
FT ECO:0007744|PDB:2QW8, ECO:0007744|PDB:2QX7,
FT ECO:0007744|PDB:2QZZ, ECO:0007744|PDB:2R6J"
FT BINDING 152..154
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:17912370,
FT ECO:0000269|PubMed:18208524, ECO:0007744|PDB:2QW8,
FT ECO:0007744|PDB:2QX7, ECO:0007744|PDB:2QZZ,
FT ECO:0007744|PDB:2R2G, ECO:0007744|PDB:2R6J,
FT ECO:0007744|PDB:3C3X"
FT BINDING 258
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:17912370,
FT ECO:0007744|PDB:2QZZ"
FT SITE 85
FT /note="Confers substrate specificity"
FT /evidence="ECO:0000269|PubMed:18208524"
FT SITE 88
FT /note="Confers substrate specificity"
FT /evidence="ECO:0000269|PubMed:18208524"
FT SITE 261
FT /note="Required for activity"
FT /evidence="ECO:0000269|PubMed:17912370"
FT MUTAGEN 85
FT /note="F->V: Confers some isoeugenol synthase activity;
FT when associated with Y-88."
FT /evidence="ECO:0000269|PubMed:18208524"
FT MUTAGEN 88
FT /note="I->Y: Confers some isoeugenol synthase activity;
FT when associated with V-85."
FT /evidence="ECO:0000269|PubMed:18208524"
FT MUTAGEN 132
FT /note="K->A,Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17912370"
FT MUTAGEN 132
FT /note="K->R: Reduced activity."
FT /evidence="ECO:0000269|PubMed:17912370"
FT MUTAGEN 157
FT /note="Y->A,F: Reduced activity."
FT /evidence="ECO:0000269|PubMed:17912370"
FT MUTAGEN 261
FT /note="I->H: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17912370"
FT MUTAGEN 314
FT /note="F->A: Reduced activity."
FT /evidence="ECO:0000269|PubMed:17912370"
FT MUTAGEN 314
FT /note="F->Y: Normal activity."
FT /evidence="ECO:0000269|PubMed:17912370"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:2R6J"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 20..29
FT /evidence="ECO:0007829|PDB:2R6J"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:2R6J"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 66..73
FT /evidence="ECO:0007829|PDB:2R6J"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2R6J"
FT TURN 88..90
FT /evidence="ECO:0007829|PDB:2QW8"
FT HELIX 91..101
FT /evidence="ECO:0007829|PDB:2R6J"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2R6J"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 123..141
FT /evidence="ECO:0007829|PDB:2R6J"
FT STRAND 146..150
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:2R6J"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:2R6J"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:2R6J"
FT STRAND 206..209
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:2R6J"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 219..230
FT /evidence="ECO:0007829|PDB:2R6J"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:2R6J"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 256..266
FT /evidence="ECO:0007829|PDB:2R6J"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:2R6J"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:2R6J"
SQ SEQUENCE 314 AA; 35607 MW; B221B0E8E733213B CRC64;
MEENGMKSKI LIFGGTGYIG NHMVKGSLKL GHPTYVFTRP NSSKTTLLDE FQSLGAIIVK
GELDEHEKLV ELMKKVDVVI SALAFPQILD QFKILEAIKV AGNIKRFLPS DFGVEEDRIN
ALPPFEALIE RKRMIRRAIE EANIPYTYVS ANCFASYFIN YLLRPYDPKD EITVYGTGEA
KFAMNYEQDI GLYTIKVATD PRALNRVVIY RPSTNIITQL ELISRWEKKI GKKFKKIHVP
EEEIVALTKE LPEPENIPIA ILHCLFIDGA TMSYDFKEND VEASTLYPEL KFTTIDELLD
IFVHDPPPPA SAAF
