FES_OCIBA
ID FES_OCIBA Reviewed; 598 AA.
AC Q5SBP2;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=(-)-endo-fenchol synthase, chloroplastic;
DE EC=4.2.3.10;
DE Flags: Precursor;
GN Name=FES;
OS Ocimum basilicum (Sweet basil).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Ociminae;
OC Ocimum.
OX NCBI_TaxID=39350;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15516500; DOI=10.1104/pp.104.051318;
RA Iijima Y., Davidovich-Rikanati R., Fridman E., Gang D.R., Bar E.,
RA Lewinsohn E., Pichersky E.;
RT "The biochemical and molecular basis for the divergent patterns in the
RT biosynthesis of terpenes and phenylpropenes in the peltate glands of three
RT cultivars of basil.";
RL Plant Physiol. 136:3724-3736(2004).
CC -!- FUNCTION: Monoterpene synthase that catalyzes the formation of fenchol
CC from geranyl diphosphate. {ECO:0000269|PubMed:15516500}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (1S,2S,4R)-endo-fenchol +
CC diphosphate; Xref=Rhea:RHEA:20565, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15405, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=4.2.3.10;
CC Evidence={ECO:0000269|PubMed:15516500};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
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; AY693648; AAV63790.1; -; mRNA.
DR AlphaFoldDB; Q5SBP2; -.
DR SMR; Q5SBP2; -.
DR KEGG; ag:AAV63790; -.
DR BioCyc; MetaCyc:MON-15443; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050437; F:(-)-endo-fenchol synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; 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 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 35..598
FT /note="(-)-endo-fenchol synthase, chloroplastic"
FT /id="PRO_0000399249"
FT MOTIF 351..355
FT /note="DDXXD motif"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 598 AA; 69865 MW; B3393F62A43B7264 CRC64;
MWSTISISMN VAILKKPLNF LHNSNNKASN PRCVSSTRRR PSCPLQLDVE PRRSGNYQPS
AWDFNYIQSL NNNHSKEERH LQGKAKLIEE VKMLLEQEMA AVQQLEFIED LKNLGLSYLF
QDEIKIILNS IYNHHKCFHN NHQQRTDENA DLYFVALGFR LFRQHGFKVS QEVFDCFKNE
EGSDFIPNLA EDTKGLLQLY EASYLVRQDE DTLEMARQFS TKILQKKVEE KMIEENLLSW
TCHSLELPLH WRVQRIEAKW FLDAYASKPD MNPIIFELAK LEFNIAQALQ QGELKDLSRW
WNDTGIAEKL PFARDRIVEA HYWAIGTLEP YQYRYQRSLI AKIIALTTVV DDVYDVYGTL
DEPQLFTDAI RRWDIESINQ LPHYLQLCYL AIYNFVSELA YDIFRDKGFN SLPYLHKSWL
DLVEAYFLEA KWFHSGYTPT LEEYLNNSKM TITCPAIVSE IYFAFANSID KTEVESVYKY
HDILYLSGML LRLPDDLGTT TFEMKRGDVA KAIQCYMKEH NASEEEAREH IRFLMREAWK
QMNTAAAANN CPFVNDFVVG AASLGRVANF VYVEGDGFGV QHSKIHQQMA ELLFYPYQ
