GAS1_HELAN
ID GAS1_HELAN Reviewed; 559 AA.
AC Q4U3F7;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Germacrene A synthase 1 {ECO:0000303|PubMed:19580670};
DE EC=4.2.3.23 {ECO:0000269|PubMed:19580670};
DE AltName: Full=Terpene synthase 1A {ECO:0000303|PubMed:19580670};
DE Short=HaTPS1A {ECO:0000303|PubMed:19580670};
GN Name=GAS1 {ECO:0000303|PubMed:19580670};
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Trichome gland;
RX PubMed=19580670; DOI=10.1186/1471-2229-9-86;
RA Goepfert J.C., Macnevin G., Ro D.-K., Spring O.;
RT "Identification, functional characterization and developmental regulation
RT of sesquiterpene synthases from sunflower capitate glandular trichomes.";
RL BMC Plant Biol. 9:86-86(2009).
RN [2]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Sesquiterpene synthase involved in germacrene A biosynthesis
CC (PubMed:19580670). Germacrene A is a precursor of several sesquiterpene
CC lactones (PubMed:19580670). {ECO:0000269|PubMed:19580670}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-(R)-germacrene A +
CC diphosphate; Xref=Rhea:RHEA:12516, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:41595, ChEBI:CHEBI:175763; EC=4.2.3.23;
CC Evidence={ECO:0000269|PubMed:19580670};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12517;
CC Evidence={ECO:0000269|PubMed:19580670};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.82 uM for farnesyl diphosphate {ECO:0000269|PubMed:19580670};
CC pH dependence:
CC Optimum pH is 7.7. {ECO:0000269|PubMed:19580670};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000250|UniProtKB:Q40577}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q40577}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in sunflower trichomes.
CC {ECO:0000269|PubMed:19580670}.
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|UniProtKB:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; DQ016667; AAY41421.2; -; mRNA.
DR EMBL; EU439590; ACA14463.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4U3F7; -.
DR SMR; Q4U3F7; -.
DR EnsemblPlants; mRNA:HanXRQr2_Chr06g0249511; mRNA:HanXRQr2_Chr06g0249511; HanXRQr2_Chr06g0249511.
DR Gramene; mRNA:HanXRQr2_Chr06g0249511; mRNA:HanXRQr2_Chr06g0249511; HanXRQr2_Chr06g0249511.
DR OMA; HYTIARI; -.
DR OrthoDB; 360509at2759; -.
DR BRENDA; 4.2.3.23; 2597.
DR UniPathway; UPA00213; -.
DR GO; GO:0034005; F:germacrene-A synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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 Lyase; Magnesium; Metal-binding; Oxidoreductase.
FT CHAIN 1..559
FT /note="Germacrene A synthase 1"
FT /id="PRO_0000422213"
FT MOTIF 312..316
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 559 AA; 64383 MW; E5EE38C1E26C5987 CRC64;
MAAVGASATP LTNTKSTAEP VRPVANFPPS VWGDLFLSFS LDKSIMEEYA EAMEEPKEQV
RRLILDPTMD SNKKLSLIYT VHRLGLTYMF LKEIEAQLDR LFKEFNLEDY VELDLYTISI
NFQAFRHLGY KLPCDVFNKF KNDDSTTFKE SITGDVRGML GLYESAQLRL KGENILDEAS
AFAETKLKSL VNTLEGSLAQ QVKQSLRRPF HQGMPMVEAR LYFSNYQEEC SAHDSILKLA
KLHFNYLQLQ QKEELRIVSQ WWKDMRFQET TPYIRDRVPE IYLWILGLYF EPRYSLARII
ATKITLFLVV LDDTYDAYAT IEEIRLLTDA INRWDISAMN QIPEYIRPFY KILLDEYAEL
EKQLAKEGRA NSVIASKEAF QDIARGYLEE AEWTNSGYVA SFPEYMKNGL ITSAYNVISK
SALVGMGEIV SEDALVWYES HPQILQASEL ISRLQDDVMT YQFERERGQS ATGVDSYIKT
YGVSEKVAID ELKKMIENAW KEINEGCLKP REVSMDLLAP ILNLARMIDV VYRYDDGFTF
PGKTLKEYIT LLFVGSSPM
