CYC1_CAMAC
ID CYC1_CAMAC Reviewed; 389 AA.
AC A0A1C9CX56;
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 CYC1 {ECO:0000305};
DE EC=1.3.1.122 {ECO:0000269|PubMed:27432874};
DE AltName: Full=Cyclase 1 {ECO:0000303|PubMed:27432874};
DE AltName: Full=Iridoid synthase {ECO:0000305};
DE Short=ISY {ECO:0000305};
GN Name=CYC1 {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: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: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; KU842378; AON76722.1; -; mRNA.
DR AlphaFoldDB; A0A1C9CX56; -.
DR SMR; A0A1C9CX56; -.
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..389
FT /note="(S)-8-oxocitronellyl enol synthase CYC1"
FT /id="PRO_0000444193"
FT ACT_SITE 142
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT ACT_SITE 174
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 34..36
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 62..63
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 80..81
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 104..105
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 138
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 174
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 201
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 208..210
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:K7WDL7"
SQ SEQUENCE 389 AA; 43905 MW; C2EA0C03983FA415 CRC64;
MSWWWARSLG AQKEFKENGA LTSYQSVGLI IGVTGIVGNS LAEILPLPDT PGGPWKVYGV
ARRPRPAWNT DHPIEYIQCD VASTEDTLAK LSPLTNITHI FYVAWTGSED CEVNETMFHN
VLKAVIPNAP NLRHICIQTG IKHYTGPLDP DGGIQPHDSP FTEDLPRLNA PNFYHNLEDI
LIEEAAKKKG LTWSVHRPAL VFGFSPYSMM NIIGALSVYA VICKHENKPL IYHGAPDNSR
DSWNVYADAA DADLIAEHQI WAAVDSNAKN EVFNCSNGDV FKWKQMWKIL AEQFEVELVG
YEDGQKRMSL QERMKGKGPV WDEIVRKHKL LPTKLEDVAQ WWFADIVSQS QNLVNGVNKS
KENGFLGFRD SKKSFVYWIK KMRAAKIIP
