IGS1_CLABR
ID IGS1_CLABR Reviewed; 318 AA.
AC B2WSM8;
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=Isoeugenol synthase 1 {ECO:0000303|PubMed:18208524};
DE Short=CbIGS1 {ECO:0000303|PubMed:18208524};
DE EC=1.1.1.319;
GN Name=IGS1 {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 SER-83; VAL-84; TYR-87
RP AND PRO-88, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, PATHWAY,
RP BIOPHYSICOCHEMICAL 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 isoeugenol from
CC coniferyl acetate (PubMed:18208524). Phenylpropenes are the primary
CC constituents of various essential plant oils (PubMed:18208524). They
CC are produced as antimicrobial and antianimal compounds, or as floral
CC attractants of pollinators (PubMed:18208524). Isoeugenol is a
CC characteristic aromatic constituent of spices and a floral volatile
CC compound (PubMed:18208524). {ECO:0000269|PubMed:18208524}.
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:18208524};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:24696;
CC Evidence={ECO:0000269|PubMed:18208524};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=211.5 uM for coniferyl acetate {ECO:0000269|PubMed:18208524};
CC Vmax=27.6 nmol/sec/mg enzyme with coniferyl acetate as substrate
CC {ECO:0000269|PubMed:18208524};
CC Note=kcat is 0.99 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; EF467238; ABR24112.1; -; mRNA.
DR AlphaFoldDB; B2WSM8; -.
DR SMR; B2WSM8; -.
DR BioCyc; MetaCyc:MON-13837; -.
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..318
FT /note="Isoeugenol synthase 1"
FT /id="PRO_0000451501"
FT ACT_SITE 131
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT BINDING 10..13
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 32..43
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT BINDING 33
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 84..86
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT BINDING 109..111
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 131
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 151..153
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:D0VWT0"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT SITE 84
FT /note="Confers substrate specificity"
FT /evidence="ECO:0000269|PubMed:18208524"
FT SITE 87
FT /note="Confers substrate specificity"
FT /evidence="ECO:0000269|PubMed:18208524"
FT SITE 263
FT /note="Required for activity"
FT /evidence="ECO:0000250|UniProtKB:Q15GI4"
FT MUTAGEN 83
FT /note="S->P: Confers some eugenol synthase activity; when
FT associated with F-84. High eugenol synthase activity; when
FT associated with F-84, I-87 and S-88."
FT /evidence="ECO:0000269|PubMed:18208524"
FT MUTAGEN 84
FT /note="V->F: Confers some eugenol synthase activity.
FT Confers some eugenol synthase activity; when associated
FT with P-83. Confers eugenol synthase activity; when
FT associated with I-87. High eugenol synthase activity; when
FT associated with S-83, I-87 and S-88."
FT /evidence="ECO:0000269|PubMed:18208524"
FT MUTAGEN 87
FT /note="Y->I: Confers some eugenol synthase activity.
FT Confers some eugenol synthase activity; when associated
FT with S-88. Confers eugenol synthase activity; when
FT associated with F-84. High eugenol synthase activity; when
FT associated with S-83, F-84 and S-88."
FT /evidence="ECO:0000269|PubMed:18208524"
FT MUTAGEN 88
FT /note="P->S: Confers eugenol synthase activity; when
FT associated with I-87. High eugenol synthase activity; when
FT associated with S-83, F-84 and I-87."
FT /evidence="ECO:0000269|PubMed:18208524"
SQ SEQUENCE 318 AA; 36069 MW; F53E4E85B47EE96F CRC64;
MEKIIIYGGT GYIGKFMVRA SLSFSHPTFI YARPLTPDST PSSVQLREEF RSMGVTIIEG
EMEEHEKMVS VLRQVDVVIS ALSVPMYPSQ LLIIDAIKAA GNIKRFLPSE FGSEEDRIKP
LPPFESVLEK KRIIRRAIEA AELPYTYVSA NCFGAYFVNY LLHPSPHPNR DDDIVIYGTG
ETKFVLNYEE DIAKYTIKVA CDPRCCNRIV IYRPPKNIIS QNELISLWEA KSGLSFKKVH
MPDEQLVRLS QELPQPQNIP VSILHSIFVK GDLMSYEMRK DDIEASNLYP ELEFTSIDGL
LDLFISGRAP PPTLAEFE
