AFSY1_CUCME
ID AFSY1_CUCME Reviewed; 560 AA.
AC B2KSJ6;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Alpha-farnesene synthase;
DE Short=CmTpsDul;
DE EC=4.2.3.46;
OS Cucumis melo (Muskmelon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX NCBI_TaxID=3656;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=cv. Dulce;
RX PubMed=18264780; DOI=10.1007/s11103-008-9296-6;
RA Portnoy V., Benyamini Y., Bar E., Harel-Beja R., Gepstein S.,
RA Giovannoni J.J., Schaffer A.A., Burger J., Tadmor Y., Lewinsohn E.,
RA Katzir N.;
RT "The molecular and biochemical basis for varietal variation in
RT sesquiterpene content in melon (Cucumis melo L.) rinds.";
RL Plant Mol. Biol. 66:647-661(2008).
CC -!- FUNCTION: Sesquiterpene synthase producing exclusively alpha-farnesene.
CC Associated with the production of sesquiterpenes responsible for the
CC aroma of the fruit. {ECO:0000269|PubMed:18264780}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (3E,6E)-alpha-farnesene +
CC diphosphate; Xref=Rhea:RHEA:27421, ChEBI:CHEBI:10280,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.46;
CC Evidence={ECO:0000269|PubMed:18264780};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the rind tissues of ripe fruits.
CC {ECO:0000269|PubMed:18264780}.
CC -!- DEVELOPMENTAL STAGE: Expressed during ripening.
CC {ECO:0000269|PubMed:18264780}.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; EU158099; ABX83201.1; -; mRNA.
DR RefSeq; NP_001284384.1; NM_001297455.1.
DR AlphaFoldDB; B2KSJ6; -.
DR SMR; B2KSJ6; -.
DR GeneID; 103493391; -.
DR KEGG; cmo:103493391; -.
DR eggNOG; ENOG502QUCN; Eukaryota.
DR OrthoDB; 360509at2759; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000089565; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0052578; F:alpha-farnesene synthase activity; IEA:RHEA.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0045338; P:farnesyl diphosphate metabolic process; IDA:UniProtKB.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
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 Cytoplasm; Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..560
FT /note="Alpha-farnesene synthase"
FT /id="PRO_0000419799"
FT MOTIF 308..312
FT /note="DDXXD motif"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 560 AA; 65190 MW; 66FE9436CE3327D9 CRC64;
MSSNISAIPN SLEVIRRSAQ FQASVWGDYF LSYHSLSPEK GNKVMEKQTE ELKEEIKREL
NSTTKDEEPE KLRLIDSIQR LGVCYHFEYE INKILEQLHH ITITSKNNGD DHPYNMTLRF
RLLRQQGYNI SSKSFERFRG KWESSYDKNV EELLSLYEAS QLRMRGEEAL DEAFRFATAQ
LEAIVQDPTT DPTVVGEVCQ ALKWPMYKNL PRLQASHYIG LYSEKPWRNE SLPNFAKMDF
SKLQKLHQKE IAYISKWWDD YGFAEKLSFA RNRIVEGYFF ALGIFFEPQL STARLIMTKI
IAIGSVLDDI YDVYGTFEEL KLLTLALERW DKSETKKLPK YMKMYYEALL DVFEEIEQEM
SQKETTPYCI HQMKEATKEL GRVFLVEAKW CKEGYTPTVE EYLDIALISF GHKLLMVTAL
LGMGSTIATQ QIVQWITSMP NILKASAIIC RLMNDIVSHK FEQERGHVAS AIECYMEQNY
MSEHDVLIIL GKQIDEFWKD MVENYCVVIT EEEVPRGVLM RVLNLTRLFN VIYKDGDGYT
QSHGSTKTHI KSLLVDSLPL
