ISY_ANTMA
ID ISY_ANTMA Reviewed; 387 AA.
AC A0A221J5P3;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=(S)-8-oxocitronellyl enol synthase {ECO:0000305};
DE EC=1.3.1.122 {ECO:0000269|PubMed:28701463};
DE AltName: Full=7-epi-iridoid synthase {ECO:0000305};
DE EC=1.3.1.123 {ECO:0000269|PubMed:28701463};
DE AltName: Full=Iridoid synthase {ECO:0000303|PubMed:28701463};
DE Short=AmISY {ECO:0000303|PubMed:28701463};
GN Name=ISY {ECO:0000303|PubMed:28701463};
OS Antirrhinum majus (Garden snapdragon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Plantaginaceae; Antirrhineae; Antirrhinum.
OX NCBI_TaxID=4151;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=28701463; DOI=10.1074/jbc.m117.800979;
RA Kries H., Kellner F., Kamileen M.O., O'Connor S.E.;
RT "Inverted stereocontrol of iridoid synthase in snapdragon.";
RL J. Biol. Chem. 292:14659-14667(2017).
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:28701463). Reduces 8-oxogeranial,
CC generating an unstable product that is subsequently cyclized into
CC several possible products, either non-enzymically or by dedicated
CC cyclases (PubMed:28701463). Iridoids comprise a large family of
CC distinctive bicyclic monoterpenes that possess a wide range of
CC pharmacological activities, including anticancer, anti-inflammatory,
CC antifungal and antibacterial activities (PubMed:28701463).
CC {ECO:0000269|PubMed:28701463}.
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:28701463};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:62594;
CC Evidence={ECO:0000269|PubMed:28701463};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-8-oxocitronellyl enol + NADP(+) = (6E)-8-oxogeranial +
CC H(+) + NADPH; Xref=Rhea:RHEA:61432, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:64239,
CC ChEBI:CHEBI:144487; EC=1.3.1.123;
CC Evidence={ECO:0000269|PubMed:28701463};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:61434;
CC Evidence={ECO:0000269|PubMed:28701463};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.1 uM for (6E)-8-oxogeranial {ECO:0000269|PubMed:28701463};
CC Note=kcat is 0.72 sec(-1) with (6E)-8-oxogeranial as substrate.
CC {ECO:0000269|PubMed:28701463};
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:28701463}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. Highly divergent. {ECO:0000305}.
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DR EMBL; MF281392; ASM61954.1; -; mRNA.
DR AlphaFoldDB; A0A221J5P3; -.
DR SMR; A0A221J5P3; -.
DR KEGG; ag:ASM61954; -.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IDA:UniProtKB.
DR GO; GO:0006721; P:terpenoid metabolic process; IDA:UniProtKB.
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..387
FT /note="(S)-8-oxocitronellyl enol synthase"
FT /id="PRO_0000452245"
FT ACT_SITE 144
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT ACT_SITE 177
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 36..38
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 64..65
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 82..83
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 106..107
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 140
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 177
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 177
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 211..213
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
SQ SEQUENCE 387 AA; 44183 MW; 148C5925BC26FEB7 CRC64;
MSWWYRRSIG ETEQKRIEIN GVSPTYQSVA LIVGVTGIAG SGLAETLSFS DTPGGPWKVY
GVARRPCPKW LAKLNVNYVQ CDIANTDETY SKVAPLTDIT HIFYVSWTGS EDVALNTLMF
KNILDSVIPN APNLKHVSLQ TGIKYYWGNM AEMDSTNQPH ECPFYENMPR LKQDNFYYNL
EDLVYDSAVR KNGLSWSIHR PALIFGFSPC SMMNTVSTLC VYAAICKHEN KPLVYTGTET
SWTCLWDAVD SDLLAEHFLW AATVPNAKNQ AFNINNGDVF KWKHMWKVLA KEFDIEAIGY
EGKEPVLLED LMKDKDSVWD EIVKKHDLVP TKLRDIAAFW LADVVFRNKE TLCSMNKNKE
FGFMGFRDTT KSFVSSINKM RDFKFIP
