EGS1_PETHY
ID EGS1_PETHY Reviewed; 308 AA.
AC B2WSN1;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Eugenol synthase 1 {ECO:0000303|PubMed:18208524};
DE Short=PhEGS1 {ECO:0000303|PubMed:18208524};
DE EC=1.1.1.318;
GN Name=EGS1 {ECO:0000303|PubMed:18208524};
OS Petunia hybrida (Petunia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX NCBI_TaxID=4102;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF GLN-86 AND LEU-89,
RP CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, 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).
RN [2]
RP INDUCTION BY EOBI.
RC STRAIN=cv. W115;
RX PubMed=23275577; DOI=10.1105/tpc.112.105247;
RA Spitzer-Rimon B., Farhi M., Albo B., Cna'ani A., Ben Zvi M.M., Masci T.,
RA Edelbaum O., Yu Y., Shklarman E., Ovadis M., Vainstein A.;
RT "The R2R3-MYB-like regulatory factor EOBI, acting downstream of EOBII,
RT regulates scent production by activating ODO1 and structural scent-related
RT genes in petunia.";
RL Plant Cell 24:5089-5105(2012).
CC -!- FUNCTION: Involved in the biosynthesis of the floral volatile eugenol
CC (PubMed:18208524). Catalyzes the synthesis of the phenylpropene eugenol
CC from coniferyl acetate (PubMed:18208524). Phenylpropenes are produced
CC by 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=245.3 uM for coniferyl acetate {ECO:0000269|PubMed:18208524};
CC Vmax=18.4 nmol/sec/mg enzyme with coniferyl acetate as substrate
CC {ECO:0000269|PubMed:18208524};
CC Note=kcat is 0.60 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: In flowers, mostly expressed in limbs, and, to a
CC lower extent, in tubes. {ECO:0000269|PubMed:18208524}.
CC -!- INDUCTION: Triggered by EOBI in flowers. {ECO:0000269|PubMed:23275577}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; EF467241; ABR24115.1; -; mRNA.
DR AlphaFoldDB; B2WSN1; -.
DR SMR; B2WSN1; -.
DR BioCyc; MetaCyc:MON-13833; -.
DR BRENDA; 1.1.1.318; 4700.
DR UniPathway; UPA00711; -.
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 NADP; Nucleotide-binding; Oxidoreductase; Phenylpropanoid metabolism.
FT CHAIN 1..308
FT /note="Eugenol synthase 1"
FT /id="PRO_0000451500"
FT ACT_SITE 133
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT BINDING 13..16
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 35..45
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT BINDING 36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 86..88
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT BINDING 111..113
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 133
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 153..155
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT SITE 86
FT /note="Confers substrate specificity"
FT /evidence="ECO:0000269|PubMed:18208524"
FT SITE 89
FT /note="Confers substrate specificity"
FT /evidence="ECO:0000269|PubMed:18208524"
FT SITE 265
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT MUTAGEN 86
FT /note="Q->V: Confers some isoeugenol synthase activity;
FT when associated with Y-89."
FT /evidence="ECO:0000269|PubMed:18208524"
FT MUTAGEN 89
FT /note="L->Y: Confers some isoeugenol synthase activity;
FT when associated with V-86."
FT /evidence="ECO:0000269|PubMed:18208524"
SQ SEQUENCE 308 AA; 33807 MW; 4DDF43361B9B60F4 CRC64;
MAEKSKILII GGTGYIGKFV VEASAKAGHP TFVLVRESTV SDPAKGKIVE SFNNSGVTIL
YGDLYDHESL VKAIKQVDVV ISTVGQMQLA DQTKIIAAIK EAGNIKRFFP SEFGMDVDKV
NAVEPAKSTF AIKVQIRRAI EAEGIPYTYV SSNCFAGYFL PTLVQPGATD PPRDKVIISG
DGNAKAVFNE EHDIGTYTIK AVDDPRTLNK TLYIKPPKNT LSFNELVAIW EKLIGKTLEK
IYIPEEQILK DIATSPIPIN IILAINHSTF VKGDQTNFVI EPSFGVEASE LYPDVKYTTV
EEYLSHFA
