ISY2_NEPRA
ID ISY2_NEPRA Reviewed; 396 AA.
AC A0A221J5X6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 1.
DT 03-AUG-2022, entry version 13.
DE RecName: Full=(S)-8-oxocitronellyl enol synthase ISY2 {ECO:0000305};
DE EC=1.3.1.122 {ECO:0000269|PubMed:29091815};
DE AltName: Full=Iridoid synthase 2 {ECO:0000303|PubMed:29091815};
DE Short=NmISY2 {ECO:0000303|PubMed:29091815};
GN Name=ISY2 {ECO:0000303|PubMed:29091815};
OS Nepeta racemosa (Catmint) (Raceme catnip).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Nepetinae;
OC Nepeta.
OX NCBI_TaxID=54731;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITES, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=29091815; DOI=10.1016/j.phytochem.2017.10.004;
RA Sherden N.H., Lichman B., Caputi L., Zhao D., Kamileen M.O., Buell C.R.,
RA O'Connor S.E.;
RT "Identification of iridoid synthases from Nepeta species: Iridoid
RT cyclization does not determine nepetalactone stereochemistry.";
RL Phytochemistry 145:48-56(2018).
CC -!- FUNCTION: Iridoid synthase that catalyzes the first step in generation
CC of the iridoid ring scaffold using the linear monoterpene (6E)-8-
CC oxogeranial as substrate (PubMed:29091815). Iridoids comprise a large
CC family of distinctive bicyclic monoterpenes that possess a wide range
CC of pharmacological activities, including anticancer, anti-inflammatory,
CC antifungal and antibacterial activities (Probable). Catalyzes the
CC conversion of the linear monoterpene (6E)-8-oxogeranial to (S)-8-
CC oxocitronellyl enol, a precursor of nepetalactones, which are
CC metabolites that are both insect-repellent and have euphoric effect in
CC cats (PubMed:29091815). {ECO:0000269|PubMed:29091815, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-8-oxocitronellyl enol + NADP(+) = (6E)-8-oxogeranial +
CC H(+) + NADPH; Xref=Rhea:RHEA:62592, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64239,
CC ChEBI:CHEBI:144481; EC=1.3.1.122;
CC Evidence={ECO:0000269|PubMed:29091815};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:62594;
CC Evidence={ECO:0000269|PubMed:29091815};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-8-oxocitronellyl enol + NAD(+) = (6E)-8-oxogeranial + H(+)
CC + NADH; Xref=Rhea:RHEA:62596, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:64239, ChEBI:CHEBI:144481;
CC EC=1.3.1.122; Evidence={ECO:0000250|UniProtKB:K7WDL7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:62598;
CC Evidence={ECO:0000250|UniProtKB:K7WDL7};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.3 uM for (6E)-8-oxogeranial {ECO:0000269|PubMed:29091815};
CC KM=23.2 uM for NADPH {ECO:0000269|PubMed:29091815};
CC Note=kcat is 0.60 sec(-1) with 6E)-8-oxogeranial as substrate. kcat
CC is 0.84 sec(-1) with NADPH as proton donor.
CC {ECO:0000269|PubMed:29091815};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KY882236; ASM62112.1; -; mRNA.
DR AlphaFoldDB; A0A221J5X6; -.
DR SMR; A0A221J5X6; -.
DR BioCyc; MetaCyc:MON-20870; -.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NAD; NADP; Oxidoreductase.
FT CHAIN 1..396
FT /note="(S)-8-oxocitronellyl enol synthase ISY2"
FT /id="PRO_0000449835"
FT ACT_SITE 182
FT /evidence="ECO:0000305|PubMed:29091815"
FT BINDING 38..40
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 66..67
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 84..85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 108..109
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 146
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 182
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 209
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:Q9STX2"
FT BINDING 216..218
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
SQ SEQUENCE 396 AA; 44843 MW; 20755756C291A5FE CRC64;
MSLSWWRAGA AKKRMDDDES LLVKQQQQQC VALIVGVTGL VGNSLAEMLP LPDTPGGPWK
VYGVARRARP SWNEDQPMTY ISCDVSNTGE VEAKLSPLSD VTHIFYATWT SRSTEEENCE
ANGKMLKNVL DAMIPNCPNL KHICLQTGRF HYVASVVDWK INGSHDTPLT EDLPRLKTNN
FYYTQEDILL EEVKRKEGLT WSVHRPGTIF GFSPYSMMNL VGTLCVYAAI CKQEGAVLRF
PGCKGAWDGH SDCADADLIA EQQIWAALDP HAKNQAFNVS NGDLFKWKHL WKVLADQFGV
ECGDYEEGQQ LRLQDVMKDK GPVWDKIVAE NGLSNTKLED VGKWWFSDTI LWNECRLDSM
NKSKEHGFLG FRNSKNCFLY WIHKVKAYNL VPSTYT
