GAS_TANPA
ID GAS_TANPA Reviewed; 559 AA.
AC F8UL80;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Germacrene A synthase {ECO:0000303|PubMed:21620424};
DE Short=TpGAS {ECO:0000303|PubMed:21620424};
DE EC=4.2.3.23 {ECO:0000269|PubMed:21620424};
GN Name=GAS {ECO:0000303|PubMed:21620424};
OS Tanacetum parthenium (Feverfew) (Matricaria parthenium).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Anthemidinae; Tanacetum.
OX NCBI_TaxID=127999;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=21620424; DOI=10.1016/j.phytochem.2011.04.021;
RA Majdi M., Liu Q., Karimzadeh G., Malboobi M.A., Beekwilder J., Cankar K.,
RA de Vos R., Todorovic S., Simonovic A., Bouwmeester H.;
RT "Biosynthesis and localization of parthenolide in glandular trichomes of
RT feverfew (Tanacetum parthenium L. Schulz Bip.).";
RL Phytochemistry 72:1739-1750(2011).
RN [2]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=24704560; DOI=10.1016/j.ymben.2014.03.005;
RA Liu Q., Manzano D., Tanic N., Pesic M., Bankovic J., Pateraki I.,
RA Ricard L., Ferrer A., de Vos R., van de Krol S., Bouwmeester H.;
RT "Elucidation and in planta reconstitution of the parthenolide biosynthetic
RT pathway.";
RL Metab. Eng. 23C:145-153(2014).
RN [3]
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:21620424). Germacrene A is a precursor of several sesquiterpene
CC lactones (PubMed:21620424). {ECO:0000269|PubMed:21620424}.
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:21620424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12517;
CC Evidence={ECO:0000269|PubMed:21620424};
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 -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:21620424}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q40577}.
CC -!- TISSUE SPECIFICITY: Expressed in glandular trichomes of all aerial
CC tissues, with highest levels in tissues accumulating parthenolide (e.g.
CC flowers and, to some extent, leaves). {ECO:0000269|PubMed:21620424,
CC ECO:0000269|PubMed:24704560}.
CC -!- DEVELOPMENTAL STAGE: During flowers development, mostly observed in
CC ovaries during the biosynthetically most active stages (e.g. stages 2,
CC 3 and 4, when petals are progressively opening).
CC {ECO:0000269|PubMed:21620424, ECO:0000269|PubMed:24704560}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JF819848; AEH41844.1; -; mRNA.
DR AlphaFoldDB; F8UL80; -.
DR SMR; F8UL80; -.
DR BioCyc; MetaCyc:MON-18664; -.
DR BRENDA; 4.2.3.23; 12835.
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"
FT /id="PRO_0000448394"
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; 64458 MW; 369E6F553E30A47A CRC64;
MAAVQATTGI QANTKTSAEP VRPLANFPPS VWGDRFLSFS LDKSEFERYA IAMEKPKEDV
RKLIVDSTMD SNEKLGLIYS VHRVGLTYMF LQEIESQLDK LFNEFSLQDY EEVDLYTISI
NFQVFRHLGY KLPCDVFKKF KDAISGTFKE SITSDVRGML GLYESAQLRI RGEKILDEAS
VFIEGKLKSV VNTLEGNLAQ QVKQSLRRPF HQGMPMVEAR LYFSNYEEEC SSHDSLFKLA
KLHFKYLELQ QKEELRIVTK WYKDMRFQET TPYIRDRVPE IYLWILGLYF EPRYSLARII
ATKITLFLVV LDDTYDAYAT IEEIRLLTDA MNKWDISAME QIPEYIRPFY KVLLDEYAEI
GKRMAKEGRA DTVIASKEAF QDIARGYLEE AEWTNSGYVA SFPEYMKNGL ITSAYNVISK
SALVGMGEIV SEDALAWYES HPKPLQASEL ISRLQDDVMT YQFERERGQS ATGVDAYIKT
YGVSEKKAID ELKIMIENAW KDINEGCLKP RQVSMDLLAP ILNLARMIDV VYRYDDGFTF
PGSTLKEYIN LLFVDSLPV
