EGS2_CLABR
ID EGS2_CLABR Reviewed; 309 AA.
AC B2WSN0;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Eugenol synthase 2 {ECO:0000303|PubMed:18208524};
DE Short=CbEGS2 {ECO:0000303|PubMed:18208524};
DE EC=1.1.1.318 {ECO:0000269|PubMed:18208524};
GN Name=EGS2 {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], FUNCTION, MUTAGENESIS OF PHE-86 AND ILE-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).
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=310.5 uM for coniferyl acetate {ECO:0000269|PubMed:18208524};
CC Vmax=6.9 nmol/sec/mg enzyme with coniferyl acetate as substrate
CC {ECO:0000269|PubMed:18208524};
CC Note=kcat is 0.25 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; EF467240; ABR24114.1; -; mRNA.
DR AlphaFoldDB; B2WSN0; -.
DR SMR; B2WSN0; -.
DR BioCyc; MetaCyc:MON-13843; -.
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..309
FT /note="Eugenol synthase 2"
FT /id="PRO_0000451499"
FT ACT_SITE 134
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 134
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 154..156
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 266
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT MUTAGEN 86
FT /note="F->V: Confers some isoeugenol synthase activity;
FT when associated with Y-89."
FT /evidence="ECO:0000269|PubMed:18208524"
FT MUTAGEN 89
FT /note="I->Y: Confers some isoeugenol synthase activity;
FT when associated with V-86."
FT /evidence="ECO:0000269|PubMed:18208524"
SQ SEQUENCE 309 AA; 34234 MW; B43AD57ED9F331F9 CRC64;
MGSKSKILII GGTGYIGKFI VEASVKEGHP TFALVRETTV SDPVKGKLVE KFQNLGVSLL
YGDLYDHDSL VKAIKQVDVV ISTVGFMQIA DQTKIIAAIK EAGNVKRFFP SEFGNDVDHV
NAVEPAKSVA FAVKANIRRA VEAEGIPYTY VASNCFNGYF LPTLVQPGAT TPPRDKVIIP
GDGNPKAIFN KEEDIGTYTI KAVDDPRTLN KILYLRPSNN IYSFNELVAL WEKKIGKTLE
KIYVPEEQIL KDIQEAPIPI NIFLGINHSV FVKGDHTNFE IEPSFGVEAS ELYPEVKYTT
VEEYLDQFV
