RLC1_CITLI
ID RLC1_CITLI Reviewed; 606 AA.
AC Q8L5K3;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=(R)-limonene synthase 1, chloroplastic {ECO:0000303|PubMed:12084056};
DE EC=4.2.3.20 {ECO:0000269|PubMed:12084056};
DE AltName: Full=(+)-limonene synthase 1 {ECO:0000303|PubMed:12084056};
DE Flags: Precursor;
OS Citrus limon (Lemon) (Citrus medica var. limon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2708;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. C62; TISSUE=Peelings;
RX PubMed=12084056; DOI=10.1046/j.1432-1033.2002.02985.x;
RA Lucker J., El Tamer M.K., Schwab W., Verstappen F.W.A.,
RA van der Plas L.H.W., Bouwmeester H.J., Verhoeven H.A.;
RT "Monoterpene biosynthesis in lemon (Citrus limon): cDNA isolation and
RT functional analysis of four monoterpene synthases.";
RL Eur. J. Biochem. 269:3160-3171(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (4R)-limonene + diphosphate;
CC Xref=Rhea:RHEA:10940, ChEBI:CHEBI:15382, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.20;
CC Evidence={ECO:0000269|PubMed:12084056};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AF514287; AAM53944.1; -; mRNA.
DR AlphaFoldDB; Q8L5K3; -.
DR SMR; Q8L5K3; -.
DR KEGG; ag:AAM53944; -.
DR BRENDA; 4.2.3.20; 1413.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0034002; F:(R)-limonene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..32
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 33..606
FT /note="(R)-limonene synthase 1, chloroplastic"
FT /evidence="ECO:0000255"
FT /id="PRO_0000186452"
FT MOTIF 342..346
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 342
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 342
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 342
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 346
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 346
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 346
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 484
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 487
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 487
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 503
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
SQ SEQUENCE 606 AA; 70348 MW; CF85278341DE8CF9 CRC64;
MSSCINPSTL VTSVNAFKCL PLATNKAAIR IMAKYKPVQC LISAKYDNLT VDRRSANYQP
SIWDHDFLQS LNSNYTDEAY KRRAEELRGK VKIAIKDVIE PLDQLELIDN LQRLGLAHRF
ETEIRNILNN IYNNNKDYNW RKENLYATSL EFRLLRQHGY PVSQEVFNGF KDDQGGFICD
DFKGILSLHE ASYYSLEGES IMEEAWQFTS KHLKEVMISK NMEEDVFVAE QAKRALELPL
HWKVPMLEAR WFIHIYERRE DKNHLLLELA KMEFNTLQAI YQEELKEISG WWKDTGLGEK
LSFARNRLVA SFLWSMGIAF EPQFAYCRRV LTISIALITV IDDIYDVYGT LDELEIFTDA
VERWDINYAL KHLPGYMKMC FLALYNFVNE FAYYVLKQQD FDLLLSIKNA WLGLIQAYLV
EAKWYHSKYT PKLEEYLENG LVSITGPLII TISYLSGTNP IIKKELEFLE SNPDIVHWSS
KIFRLQDDLG TSSDEIQRGD VPKSIQCYMH ETGASEEVAR QHIKDMMRQM WKKVNAYTAD
KDSPLTGTTT EFLLNLVRMS HFMYLHGDGH GVQNQETIDV GFTLLFQPIP LEDKHMAFTA
SPGTKG
