CYC2_CAMAC
ID CYC2_CAMAC Reviewed; 390 AA.
AC A0A1C9CX66;
DT 23-MAY-2018, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=(S)-8-oxocitronellyl enol synthase CYC2 {ECO:0000305};
DE EC=1.3.1.122 {ECO:0000269|PubMed:27432874};
DE AltName: Full=Cyclase 2 {ECO:0000303|PubMed:27432874};
DE AltName: Full=Iridoid synthase {ECO:0000305};
DE Short=ISY {ECO:0000305};
GN Name=CYC2 {ECO:0000303|PubMed:27432874};
OS Camptotheca acuminata (Happy tree).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Cornales; Nyssaceae; Camptotheca.
OX NCBI_TaxID=16922;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27432874; DOI=10.1105/tpc.16.00193;
RA Sadre R., Magallanes-Lundback M., Pradhan S., Salim V., Mesberg A.,
RA Jones A.D., DellaPenna D.;
RT "Metabolite diversity in alkaloid biosynthesis: a multilane (diastereomer)
RT highway for camptothecin synthesis in Camptotheca acuminata.";
RL Plant Cell 28:1926-1944(2016).
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. 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. {ECO:0000250|UniProtKB:K7WDL7,
CC ECO:0000269|PubMed:27432874}.
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:0000250|UniProtKB:K7WDL7, ECO:0000269|PubMed:27432874};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:62594;
CC Evidence={ECO:0000250|UniProtKB:K7WDL7, ECO:0000269|PubMed:27432874};
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 ECO:0000269|PubMed:27432874};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:62598;
CC Evidence={ECO:0000250|UniProtKB:K7WDL7, ECO:0000269|PubMed:27432874};
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. Highly divergent. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to catalyze the entire reaction from
CC (6E)-8-oxogeranial to nepetalactol including a cyclase step, but new
CC results have shown that the cyclase is a different enzyme and this
CC enzyme exclusively catalyzes a reduction step.
CC {ECO:0000250|UniProtKB:K7WDL7}.
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DR EMBL; KU842379; AON76723.1; -; mRNA.
DR AlphaFoldDB; A0A1C9CX66; -.
DR SMR; A0A1C9CX66; -.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IDA:UniProtKB.
DR GO; GO:0043693; P:monoterpene biosynthetic process; IDA:UniProtKB.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW NADP; Oxidoreductase.
FT CHAIN 1..390
FT /note="(S)-8-oxocitronellyl enol synthase CYC2"
FT /id="PRO_0000444194"
FT ACT_SITE 147
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT ACT_SITE 179
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 35..37
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 63..64
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 81..82
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 105..106
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 143
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 179
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 179
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 213..215
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
SQ SEQUENCE 390 AA; 43785 MW; 293B7068B32E441E CRC64;
MSWWWAGAIG AARKKFEEDD APRDCQSVAL IIGVTGIVGN SLAEILPISD TPGGPWKVYG
VARRPRPAWN ADHPVEYIQC DISDASDTHT KLSPLTDVTH IFWVTWANRP TESECCELNG
TMLRNVLNAL IPKAANLHHI CLQTGHKHYI GPFEAFGKIK PHEPPFTEDM PRLNAPNFYY
TLEDMLVEAS EKKAGLNWSV HRPAVIFGFS PFSMMNIIGT LCVYAAICKH ENTPLKFPGT
KAAWNCYSVA SDADLIAEHQ IWAAVDPYAK NEAFNCSNGD LFKWKHLWKV LAEQFGVEYA
EFDESEKPTS LVERMKDKGP VWEEIVRENG LHTTKLEGVA TWWFADVILG GECLLDSMNK
SKEHGYLGFR NTKNSLISVI DKMKAHKIVP
