BCPSF_ORIVU
ID BCPSF_ORIVU Reviewed; 554 AA.
AC E2E2N4;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=(E)-beta-caryophyllene synthase {ECO:0000305|PubMed:20419468};
DE EC=4.2.3.57 {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
DE AltName: Full=Alpha-humulene synthase {ECO:0000305|PubMed:20419468};
DE EC=4.2.3.104 {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
DE AltName: Full=Terpene synthase 6 {ECO:0000303|PubMed:20419468};
DE Short=OvTPS6 {ECO:0000303|PubMed:20419468};
GN Name=TPS6 {ECO:0000303|PubMed:20419468};
OS Origanum vulgare (Wild marjoram).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Origanum.
OX NCBI_TaxID=39352;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC STRAIN=cv. f02-04; TISSUE=Trichome gland;
RX PubMed=20419468; DOI=10.1007/s11103-010-9636-1;
RA Crocoll C., Asbach J., Novak J., Gershenzon J., Degenhardt J.;
RT "Terpene synthases of oregano (Origanum vulgare L.) and their roles in the
RT pathway and regulation of terpene biosynthesis.";
RL Plant Mol. Biol. 73:587-603(2010).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RA Crocoll C.;
RT "Biosynthesis of the phenolic monoterpenes, thymol and carvacrol, by
RT terpene synthases and cytochrome P450s in oregano and thyme.";
RL Thesis (2011), Friedrich Schiller University of Jena, Germany.
RN [3]
RP INDUCTION BY DROUGHT.
RX PubMed=27915173; DOI=10.1016/j.plaphy.2016.11.023;
RA Morshedloo M.R., Craker L.E., Salami A., Nazeri V., Sang H., Maggi F.;
RT "Effect of prolonged water stress on essential oil content, compositions
RT and gene expression patterns of mono- and sesquiterpene synthesis in two
RT oregano (Origanum vulgare L.) subspecies.";
RL Plant Physiol. Biochem. 111:119-128(2017).
RN [4]
RP TISSUE SPECIFICITY.
RX DOI=10.1016/j.indcrop.2018.07.006;
RA Jan S., Mir J.I., Shafi W., Faktoo S.Z., Singh D.B., Wijaya L.,
RA Alyemeni M.N., Ahmad P.;
RT "Divergence in tissue-specific expression patterns of genes associated with
RT the terpenoid biosynthesis in two oregano species Origanum vulgare L., and
RT Origanum majorana.";
RL Ind. Crops Prod. 123:546-555(2018).
CC -!- FUNCTION: Involved in the biosynthesis of phenolic sesquiterpenes
CC natural products (Ref.2). Sesquiterpene synthase converting (2E,6E)-
CC farnesyl diphosphate (FPP) to (E)-beta-caryophyllene and alpha-humulene
CC (PubMed:20419468, Ref.2). {ECO:0000269|PubMed:20419468,
CC ECO:0000269|Ref.2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene +
CC diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57;
CC Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295;
CC Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate;
CC Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.104;
CC Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896;
CC Evidence={ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:E2E2P0};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:E2E2P0};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:E2E2P0};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.2}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:A0A0M3Q1Q3}.
CC -!- TISSUE SPECIFICITY: Expressed in peltate glandular trichomes
CC (PubMed:20419468). Present at low levels in flowers, leaves and stems
CC (Ref.4). {ECO:0000269|PubMed:20419468, ECO:0000269|Ref.4}.
CC -!- INDUCTION: Induced by drought. {ECO:0000269|PubMed:27915173}.
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:Q9X839}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; GU385969; ADK73615.1; -; mRNA.
DR SMR; E2E2N4; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0009414; P:response to water deprivation; IEP: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; Manganese; Metal-binding.
FT CHAIN 1..554
FT /note="(E)-beta-caryophyllene synthase"
FT /id="PRO_0000453319"
FT REGION 319..325
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT REGION 391..427
FT /note="Homodimerization"
FT /evidence="ECO:0000250|UniProtKB:A0A0M3Q1Q3"
FT MOTIF 313..317
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9X839"
FT BINDING 313
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 313
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 317
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 317
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 457
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 465
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
SQ SEQUENCE 554 AA; 64662 MW; 7D8D1852432FADC5 CRC64;
MEFPASVASL SANTVGSNDV LRRSVAYHPN IWGDFFLAHT SEFMEISIAE KEEHEWLKEE
IKKLLVQTEY DSILKLELID SIQRLGVSYH FEKEIDRILR YVHQTYPIYE TENKDLRMLA
LRFRLLRQHG FHVPCDVFSE FIDAEGNLME SIAYDIQGIL SLYEASNYGV LGEEILDKAL
DSCSSHLESL ITDTNDDRLS RQVKEALKIP ISKTLTRLGA RKFISMYKED DSHNEKLLKF
AMLDFNMVQR LHQNELSHLT SWWKELDFAN KLPFARDRLV ECYFWIMGVY FEPRHEIARK
ILTKVIYMAS VLDDTYDVYG TLDELILFTS VVRRWDISGI DELPTYMRIY LRALFDVYVE
MEEEMGKIGK SYAVEYAKEE MKRLAEVYFQ EAQWFFSKYK PTMQEYMKVA LLSSGYMMMT
INSLAVIEDP ITKKEFDWVV SEPPILKSSS IITRLMDDLA GYGSEDKYSA VHLYMNEKGV
SEEEAFQELR KQVKNSWKNR NKECLEPRSA SVPILTTVVN FTRVVVVLYT DEDAYGNSKN
KTKDMIKSIL VDPV
