STS2_HUMLU
ID STS2_HUMLU Reviewed; 563 AA.
AC B6SCF6;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Germacrene-A synthase {ECO:0000305};
DE EC=4.2.3.23 {ECO:0000269|PubMed:18775972};
DE AltName: Full=Sesquiterpene synthase STS2 {ECO:0000303|PubMed:18775972};
DE Short=HlSTS2 {ECO:0000303|PubMed:18775972};
OS Humulus lupulus (European hop).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Humulus.
OX NCBI_TaxID=3486 {ECO:0000312|EMBL:ACI32640.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=Lupulin gland;
RX PubMed=18775972; DOI=10.1104/pp.108.125187;
RA Wang G., Tian L., Aziz N., Broun P., Dai X., He J., King A., Zhao P.X.,
RA Dixon R.A.;
RT "Terpene biosynthesis in glandular trichomes of hop.";
RL Plant Physiol. 148:1254-1266(2008).
CC -!- FUNCTION: Sesquiterpene synthase that catalyzes the formation of
CC germacrene A. Can use farnesyl diphosphate as substrate, but not
CC geranyl diphosphate or geranylgeranyl diphosphate. Beta-elemene, the
CC initially measured product in the assay, is derived nonenzymatically
CC from germacrene A. {ECO:0000269|PubMed:18775972}.
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:18775972};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.49 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:18775972};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- TISSUE SPECIFICITY: Expressed in young leaves. Detected in trichomes
CC and cones. {ECO:0000269|PubMed:18775972}.
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. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; EU760351; ACI32640.1; -; mRNA.
DR AlphaFoldDB; B6SCF6; -.
DR SMR; B6SCF6; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0034005; F:germacrene-A synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; 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 Lyase; Magnesium; Metal-binding.
FT CHAIN 1..563
FT /note="Germacrene-A synthase"
FT /id="PRO_0000439239"
FT MOTIF 316..320
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
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 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 320
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 563 AA; 65951 MW; EE5A4144FAFC3494 CRC64;
MSTQIFASSS QNEKIHKILR PTKKLQPSVW GERFLHYNIS EQELRYKQQQ VEELKAVVKK
EIFGESAYDV SHQLKLINVV ERLGLSYHFE SEIENELESI YNKSVDQNYI LKDENLHDAS
LRFRLLRQHG FRVSSADIFE KFKDEDGNFK ECLVSDTIGL LSLYEASHLS CVGENILDEA
LDFTTTHLTE FLANKKEHDD PLSKEISQAL ERPLRKSLER LAARHFISIY ANETSHNKVL
LQLAKLDFNL LQSIHKKELS EISRWWKESD FVHKFPFARD RIVELYLWIL AVYYEPQYYL
ARNILTKTIA LASIADDIYD EYGTIEELEL LTEAVERWDI NFIDKLNPEY LQTFYKELLN
SYEEFEQALS KEETYRVHYA KERFKELLRS SLEVAWWLKE GRVPSFDEYL KISLINCGYH
MLIVSSLIGM KGSIVTKEVF EWLSIDRKIV RASVTICRLM DDIAEYKFEQ EKNEEPSAVE
CYMKQYGVSE EEAYDELNKR VVNAWKEINE ELLKPTGVAS PILVRALNFS KFMDLFYKNG
DGYTQVGKVT KHSVAALLIH PIP
