GAS2_HELAN
ID GAS2_HELAN Reviewed; 559 AA.
AC B0FGA9;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Germacrene A synthase 2 {ECO:0000303|PubMed:19580670};
DE EC=4.2.3.23 {ECO:0000269|PubMed:19580670};
DE AltName: Full=Terpene synthase 1B {ECO:0000303|PubMed:19580670};
DE Short=HaTPS1B {ECO:0000303|PubMed:19580670};
GN Name=GAS2 {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=0.74 uM for farnesyl diphosphate {ECO:0000269|PubMed:19580670};
CC pH dependence:
CC Optimum pH is 7.5. {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; EU327785; ABY49939.1; -; mRNA.
DR EMBL; EU443249; ACA33925.1; -; Genomic_DNA.
DR AlphaFoldDB; B0FGA9; -.
DR SMR; B0FGA9; -.
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: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.
FT CHAIN 1..559
FT /note="Germacrene A synthase 2"
FT /id="PRO_0000422214"
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; 64436 MW; 6B114D28996D182F CRC64;
MAAVGASATL LTNTKSAEEP VRPVANFPPS VWGDLFLSFS LDNSMMEEYA EAMEEPKGQV
RKLILDPTMD SNKKLSLIYT VHRLGLTYMF FKEIEGQLDR LFKEFNLEDY VEVDLYTIST
NFQAFRHLGY KLSCDVFNKF KNYDSNTFKE SITSDVRGML GLYESAQLRL KGEKILDEAS
AFTETKLKSL VKTLEGSLAQ QVKQSLKRPF HQGMPMVEAR LYFSNYQEEC SRHDSLLKLA
KLHFNYLQLQ QKEELRIVSQ WWKDMRFQET TPYIRDRVPE IYLWILGLYF EPRYSLARII
ATKITLFLVV LDDTYDAYAT IEEVRLLTDA INRWDIGAMS QIPEYIRPFY KILLDEYAEL
EKQLAKEGRA NSVIASKEAF QDIARGYLEE AEWTNSGYVA SFPEYMKNGL ITSAYNVISK
SALVGMGEIV SEDALAWYES HPQILQASEL ISRLQDDVMT YQFERERGQS ATGVDAYIKT
YGVSEKEAID ELKKMIENAW KEINEGCLKP REVSMDLLAP ILNLARMIDV VYRYDDGFTF
PGKTLKEYIT LLFVGSSPM
