FARS_ARTAN
ID FARS_ARTAN Reviewed; 577 AA.
AC Q9FXY7; A9LPA6; Q4VM12;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=(E)-beta-farnesene synthase;
DE Short=AaFS;
DE EC=4.2.3.47;
DE AltName: Full=Terpene synthase 10;
GN Name=CASC125;
OS Artemisia annua (Sweet wormwood).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Artemisiinae; Artemisia.
OX NCBI_TaxID=35608;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Flower, and Leaf;
RX PubMed=10996256; DOI=10.1016/s0168-9452(00)00322-8;
RA Van Geldre E., De Pauw I., Inze D., Van Montagu M., Van den Eeckhout E.;
RT "Cloning and molecular analysis of two new sesquiterpene cyclases from
RT Artemisia annua L.";
RL Plant Sci. 158:163-171(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=15896363; DOI=10.1016/j.phytochem.2005.03.027;
RA Picaud S., Brodelius M., Brodelius P.E.;
RT "Expression, purification and characterization of recombinant (E)-beta-
RT farnesene synthase from Artemisia annua.";
RL Phytochemistry 66:961-967(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mirzaee H., Hashemi Sohi H., Sharafi A.;
RT "Molecular cloning, characterization and transient expression of
RT sesquiterpene cyclase for increasing Artemisinin from Iranian Artemisia
RT annua.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Sesquiterpene cyclase catalyzing the production of beta-
CC farnesene from farnesyl diphosphate. Unable to use geranyl diphosphate
CC as substrate. {ECO:0000269|PubMed:15896363}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene +
CC diphosphate; Xref=Rhea:RHEA:27425, ChEBI:CHEBI:10418,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.47;
CC Evidence={ECO:0000269|PubMed:15896363};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15896363};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:15896363};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15896363};
CC -!- ACTIVITY REGULATION: Strongly inhibited by manganese at concentration
CC higher than 20 uM. {ECO:0000269|PubMed:15896363}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.1 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:15896363};
CC pH dependence:
CC Optimum pH is 6.5-7.5. {ECO:0000269|PubMed:15896363};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in flowers.
CC {ECO:0000269|PubMed:10996256}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX39387.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ271792; CAC12731.1; -; mRNA.
DR EMBL; AY835398; AAX39387.1; ALT_FRAME; mRNA.
DR EMBL; EU252034; ABX09997.1; -; mRNA.
DR AlphaFoldDB; Q9FXY7; -.
DR SMR; Q9FXY7; -.
DR PRIDE; Q9FXY7; -.
DR BioCyc; MetaCyc:MON-13549; -.
DR BRENDA; 4.2.3.47; 7150.
DR UniPathway; UPA00213; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Cobalt; Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..577
FT /note="(E)-beta-farnesene synthase"
FT /id="PRO_0000402128"
FT MOTIF 327..331
FT /note="DDXXD motif"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 327
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 331
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 482
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 61
FT /note="L -> F (in Ref. 3; ABX09997)"
FT /evidence="ECO:0000305"
FT CONFLICT 248..250
FT /note="NED -> DEV (in Ref. 2; AAX39387)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="D -> V (in Ref. 3; ABX09997)"
FT /evidence="ECO:0000305"
FT CONFLICT 361
FT /note="M -> I (in Ref. 3; ABX09997)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 577 AA; 66722 MW; EFEFE2BC0AF82116 CRC64;
MSTLPISSVS FSSSTSPLVV DDKVSTKPDV IRHTMNFNAS IWGDQFLTYD EPEDLVMKKQ
LVEELKEEVK KELITIKGSN EPMQHVKLIE LIDAVQRLGI AYHFEEEIEE ALQHIHVTYG
EQWVDKENLQ SISLWFRLLR QQGFNVSSGV FKDFMDEKGK FKESLCNDAQ GILALYEAAF
MRVEDETILD NALEFTKVHL DIIAKDPSCD SSLRTQIHQA LKQPLRRRLA RIEALHYMPI
YQQETSHNED LLKLAKLDFS VLQSMHKKEL SHICKWWKDL DLQNKLPYVR DRVVEGYFWI
LSIYYEPQHA RTRMFLMKTC MWLVVLDDTF DNYGTYEELE IFTQAVERWS ISCLDMLPEY
MKLIYQELVN LHVEMEESLG KGGKNISNSL CQGRWQKELG SQITLVETKM AKRGVHAQPL
EEYMSVSMVT GTYGLMIARS YVGRGDIVTE DTFKWVSSYP PIIKASCVIV RLMDDIVSHK
EEQERGHVAS SIECYSKESG ASEEEACEYI SRKVEDAWKV INRESLRPTA VPFPLLMPAI
NLARMCEVLY SVNDGFTHAE GDMKSYMKSF FVHPMVV
