IGS1_PETHY
ID IGS1_PETHY Reviewed; 323 AA.
AC Q15GI3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Isoeugenol synthase 1 {ECO:0000303|PubMed:16782809, ECO:0000303|PubMed:18208524};
DE Short=PhIGS1 {ECO:0000303|PubMed:18208524};
DE EC=1.1.1.319 {ECO:0000269|PubMed:16782809, ECO:0000269|PubMed:17241449};
GN Name=IGS1 {ECO:0000303|PubMed:16782809, 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, TISSUE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RC STRAIN=cv. Mitchell; TISSUE=Flower;
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 FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17241449; DOI=10.1111/j.1365-313x.2006.02954.x;
RA Dexter R., Qualley A., Kish C.M., Ma C.J., Koeduka T., Nagegowda D.A.,
RA Dudareva N., Pichersky E., Clark D.;
RT "Characterization of a petunia acetyltransferase involved in the
RT biosynthesis of the floral volatile isoeugenol.";
RL Plant J. 49:265-275(2007).
RN [3]
RP MUTAGENESIS OF VAL-88 AND TYR-91, BIOPHYSICOCHEMICAL PROPERTIES, GENE
RP 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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19222805; DOI=10.1111/j.1365-313x.2009.03834.x;
RA Koeduka T., Orlova I., Baiga T.J., Noel J.P., Dudareva N., Pichersky E.;
RT "The lack of floral synthesis and emission of isoeugenol in Petunia
RT axillaris subsp. parodii is due to a mutation in the isoeugenol synthase
RT gene.";
RL Plant J. 58:961-969(2009).
RN [5]
RP INDUCTION BY EOBII, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Violet 26;
RX PubMed=20543029; DOI=10.1105/tpc.109.067280;
RA Spitzer-Rimon B., Marhevka E., Barkai O., Marton I., Edelbaum O., Masci T.,
RA Prathapani N.K., Shklarman E., Ovadis M., Vainstein A.;
RT "EOBII, a gene encoding a flower-specific regulator of phenylpropanoid
RT volatiles' biosynthesis in petunia.";
RL Plant Cell 22:1961-1976(2010).
RN [6]
RP TISSUE SPECIFICITY.
RC STRAIN=cv. Mitchell, and cv. R27;
RX PubMed=22345641; DOI=10.1093/jxb/ers034;
RA Van Moerkercke A., Galvan-Ampudia C.S., Verdonk J.C., Haring M.A.,
RA Schuurink R.C.;
RT "Regulators of floral fragrance production and their target genes in
RT petunia are not exclusively active in the epidermal cells of petals.";
RL J. Exp. Bot. 63:3157-3171(2012).
RN [7]
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).
RN [8]
RP REPRESSION BY LHY.
RX PubMed=26124104; DOI=10.1073/pnas.1422875112;
RA Fenske M.P., Hewett Hazelton K.D., Hempton A.K., Shim J.S., Yamamoto B.M.,
RA Riffell J.A., Imaizumi T.;
RT "Circadian clock gene LATE ELONGATED HYPOCOTYL directly regulates the
RT timing of floral scent emission in Petunia.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:9775-9780(2015).
CC -!- FUNCTION: Involved in the biosynthesis of the floral volatile
CC isoeugenol (PubMed:16782809, PubMed:17241449, PubMed:19222805).
CC Catalyzes the synthesis of the phenylpropene isoeugenol from coniferyl
CC acetate (PubMed:16782809, PubMed:17241449, PubMed:19222805).
CC Phenylpropenes are the primary constituents of various essential plant
CC oils (PubMed:16782809). They are produced as antimicrobial and
CC antianimal compounds, or as floral attractants of pollinators
CC (PubMed:16782809). Isoeugenol is a characteristic aromatic constituent
CC of spices and a floral volatile compound (PubMed:16782809).
CC {ECO:0000269|PubMed:16782809, ECO:0000269|PubMed:17241449,
CC ECO:0000269|PubMed:19222805}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + NADP(+) + trans-isoeugenol = (E)-coniferyl acetate +
CC NADPH; Xref=Rhea:RHEA:24694, ChEBI:CHEBI:30089, ChEBI:CHEBI:47905,
CC ChEBI:CHEBI:50545, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.319; Evidence={ECO:0000269|PubMed:16782809,
CC ECO:0000269|PubMed:17241449};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24696;
CC Evidence={ECO:0000269|PubMed:16782809, ECO:0000269|PubMed:17241449};
CC -!- ACTIVITY REGULATION: Inhibited by zinc and copper ions
CC (PubMed:16782809). Repressed by 4-bromo-cinnamyl acetate
CC (PubMed:16782809). {ECO:0000269|PubMed:16782809}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for coniferyl acetate (at pH 6.5 and 28 degrees Celsius)
CC {ECO:0000269|PubMed:16782809};
CC KM=226.1 uM for coniferyl acetate {ECO:0000269|PubMed:18208524};
CC KM=73 uM for NADPH (at pH 6.5 and 28 degrees Celsius)
CC {ECO:0000269|PubMed:16782809};
CC Vmax=7.1 nmol/sec/mg enzyme (at pH 6.5 and 28 degrees Celsius)
CC {ECO:0000269|PubMed:16782809};
CC Vmax=35.7 nmol/sec/mg enzyme with coniferyl acetate as substrate
CC {ECO:0000269|PubMed:18208524};
CC Note=kcat is 1.3 sec(-1) with coniferyl acetate as substrate.
CC {ECO:0000269|PubMed:18208524};
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 -!- TISSUE SPECIFICITY: Expressed in flowers, especially in corolla and
CC tubes of petals, probably in both epidermal and mesophyll cell layers.
CC {ECO:0000269|PubMed:16782809, ECO:0000269|PubMed:20543029,
CC ECO:0000269|PubMed:22345641}.
CC -!- DEVELOPMENTAL STAGE: In corollas, accumulates progressively during
CC flower development, from buds to anthesis.
CC {ECO:0000269|PubMed:20543029}.
CC -!- INDUCTION: Up-regulated by EOBII (PubMed:20543029). Triggered by EOBI
CC in flowers via the regulation of its promoter (PubMed:23275577).
CC Circadian-regulation with peak levels occurring at the end of the light
CC period in flowers; this expression is monitored by LHY binding and
CC repression to cis-regulatory evening elements in its promoter
CC (PubMed:26124104). {ECO:0000269|PubMed:20543029,
CC ECO:0000269|PubMed:23275577, ECO:0000269|PubMed:26124104}.
CC -!- DISRUPTION PHENOTYPE: Accumulation of eugenol but reduced isoeugenol
CC levels in flowers. {ECO:0000269|PubMed:19222805}.
CC -!- SIMILARITY: Belongs to the NmrA-type oxidoreductase family.
CC {ECO:0000305}.
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DR EMBL; DQ372813; ABD17322.1; -; mRNA.
DR AlphaFoldDB; Q15GI3; -.
DR SMR; Q15GI3; -.
DR KEGG; ag:ABD17322; -.
DR BioCyc; MetaCyc:MON-13832; -.
DR BRENDA; 1.1.1.319; 4700.
DR SABIO-RK; Q15GI3; -.
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:0007623; P:circadian rhythm; IEP:UniProtKB.
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..323
FT /note="Isoeugenol synthase 1"
FT /id="PRO_0000314577"
FT ACT_SITE 135
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT BINDING 14..17
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 36..47
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT BINDING 88..90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT BINDING 113..115
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 135
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 155..157
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT SITE 88
FT /note="Confers substrate specificity"
FT /evidence="ECO:0000269|PubMed:18208524"
FT SITE 91
FT /note="Confers substrate specificity"
FT /evidence="ECO:0000269|PubMed:18208524"
FT SITE 264
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT MUTAGEN 88
FT /note="V->F: Confers some eugenol synthase activity; when
FT associated with I-91."
FT /evidence="ECO:0000269|PubMed:18208524"
FT MUTAGEN 91
FT /note="Y->I: Confers some eugenol synthase activity; when
FT associated with F-88."
FT /evidence="ECO:0000269|PubMed:18208524"
SQ SEQUENCE 323 AA; 35992 MW; F52CC6127D9C33C1 CRC64;
MTTGKGKILI LGATGYLGKY MVKASISLGH PTYAYVMPLK KNSDDSKLQL LKEFESLGVT
IFYGELSEHD KLVAVFKEVD IVISTLAVPQ YLEQLKVIEA IKEAGNIKRF VPSEFGNEVD
RVRALPRFQA VLDNKKKIRR ATEAAGIPFT FVSANSLTAY FVDYLLHPRQ KSEQVTIYGS
GDAKAVLNYE EDVAAYTIKA ADDPRAANRV LIIKPPKNIV SQLDLVSSWE KTTGSTLKMT
HISEQEIIKL SESINFPENI HASILHNIFI AGAQLSFELT QDHDLEASEL YPNYNYTSVD
EYLKICLVNP PKPKLATYAQ PST
