STPS1_SALMI
ID STPS1_SALMI Reviewed; 546 AA.
AC A0A1W6GW32;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2017, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=(-)-5-epieremophilene synthase STPS1;
DE EC=4.2.3.199 {ECO:0000269|PubMed:28487717};
DE AltName: Full=Sesquiterpene synthase 1 {ECO:0000303|PubMed:28487717};
DE Short=SmSTPS1 {ECO:0000303|PubMed:28487717};
GN Name=STPS1 {ECO:0000303|PubMed:28487717};
OS Salvia miltiorrhiza (Chinese sage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salviinae;
OC Salvia; Salvia incertae sedis.
OX NCBI_TaxID=226208;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=28487717; DOI=10.3389/fpls.2017.00627;
RA Fang X., Li C.Y., Yang Y., Cui M.Y., Chen X.Y., Yang L.;
RT "Identification of a novel (-)-5-epieremophilene synthase from Salvia
RT miltiorrhiza via transcriptome mining.";
RL Front. Plant Sci. 8:627-627(2017).
CC -!- FUNCTION: Sesquiterpene synthase that catalyzes the conversion of
CC farnesyl diphosphate to (-)-5-epi-eremophilene.
CC {ECO:0000269|PubMed:28487717}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-5-epi-eremophilene +
CC diphosphate; Xref=Rhea:RHEA:58168, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:142537, ChEBI:CHEBI:175763; EC=4.2.3.199;
CC Evidence={ECO:0000269|PubMed:28487717};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58169;
CC Evidence={ECO:0000269|PubMed:28487717};
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=25.35 uM for farnesyl diphosphate {ECO:0000269|PubMed:28487717};
CC Note=kcat is 2.09 sec(-1) with farnesyl diphosphate as substrate.
CC {ECO:0000269|PubMed:28487717};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q40577}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves and at lower levels in
CC flowers. {ECO:0000269|PubMed:28487717}.
CC -!- INDUCTION: Induced by ethylene. {ECO:0000269|PubMed:28487717}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; KY432512; ARM19967.1; -; mRNA.
DR AlphaFoldDB; A0A1W6GW32; -.
DR SMR; A0A1W6GW32; -.
DR KEGG; ag:ARM19967; -.
DR BRENDA; 4.2.3.199; 9850.
DR UniPathway; UPA00213; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0016106; P:sesquiterpenoid 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..546
FT /note="(-)-5-epieremophilene synthase STPS1"
FT /id="PRO_0000447712"
FT MOTIF 299..303
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 442
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 446
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 450
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 546 AA; 63487 MW; 2FB865AA3DD48409 CRC64;
MATTQAQIQR PIANFSPSLW GDQFIKNDPG AKAAEKHCKA VEELKKEVMN MITAAGSNLV
EAMNLIDTLE RLGISYHFEK EIDQKLKHFF NLNKDYSDES YDLYTVSLHF RLFRQHGHRI
SSDIFGRWID ESGKFKEGLK TDGKGLLSLY EASYLRTRGE TILDDALEFA TATLNSIAPH
LESPLSKQVV HALIQPLHYG NPRIEAHNFI SIYEENQDKN EFLLRFAKLD YNLLQMLHKE
ELNEVSRWWK ELDLVSKLPY ARDRVVECFF WAMGVYHEPQ YSRARIMLTK TITMTSIIDD
TYDAYGVIEE LDIFTEAIER WNMEEMKKLP EYIQPFYKAL LELYEQFEEE LAEEGRSYAA
HYAIESLKEL VRSYHVEAKW FIQGYLPPFE EYLKNALITC TYCYHTTTSL LGVESAVEED
FEWLANKPKM LVAGLLICRV IDDIATYEVE KERGQSATGI ESYMRDNNAT IEEAVAKFFE
IATDAWKDIN EECLMPSPYS RDVLMRILNL ERIIDVTYKG NEDGYTQPEK VLKPHIIALF
VDPIKM
