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Database: UniProt
Entry: Q15GI4
LinkDB: Q15GI4
Original site: Q15GI4 
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   07-APR-2021, entry version 56.
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; 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   SMR; Q15GI4; -.
DR   KEGG; ag:ABD17321; -.
DR   BioCyc; MetaCyc:MONOMER-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   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR008030; NmrA-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   NP_BIND         16..19
FT                   /note="NADP"
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   NP_BIND         38..44
FT                   /note="NADP"
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   NP_BIND         85..87
FT                   /note="NADP"
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   NP_BIND         110..112
FT                   /note="NADP"
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   NP_BIND         152..154
FT                   /note="NADP"
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   ACT_SITE        132
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000269|PubMed:17912370"
FT   BINDING         39
FT                   /note="NADP"
FT                   /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT   BINDING         114
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000305|PubMed:17912370,
FT                   ECO:0007744|PDB:2QZZ, ECO:0007744|PDB:2R2G"
FT   BINDING         132
FT                   /note="NADP"
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         258
FT                   /note="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:0007744|PDB:2R6J"
FT   TURN            14..16
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           20..29
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   STRAND          34..38
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           45..53
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   STRAND          57..60
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           66..73
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   STRAND          77..81
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           85..87
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   TURN            88..90
FT                   /evidence="ECO:0007744|PDB:2QW8"
FT   HELIX           91..101
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   STRAND          106..108
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   TURN            116..118
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           123..141
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   STRAND          146..150
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           155..163
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   STRAND          170..175
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   STRAND          181..185
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           187..197
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           201..203
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   STRAND          206..209
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           213..215
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   STRAND          216..218
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           219..230
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   STRAND          235..239
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           241..250
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   TURN            253..255
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           256..266
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   TURN            270..272
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           283..285
FT                   /evidence="ECO:0007744|PDB:2R6J"
FT   HELIX           295..304
FT                   /evidence="ECO:0007744|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
//
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