TPS1F_CAMHI
ID TPS1F_CAMHI Reviewed; 554 AA.
AC A0A348AUW0;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Valerianol synthase TPS1F {ECO:0000305};
DE EC=4.2.3.204 {ECO:0000269|PubMed:30127518};
DE AltName: Full=Terpene synthase 1f {ECO:0000303|PubMed:30127518};
DE Short=ChTps1f {ECO:0000303|PubMed:30127518};
GN Name=TPS1F {ECO:0000303|PubMed:30127518};
OS Camellia hiemalis (Camellia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; Ericales; Theaceae; Camellia.
OX NCBI_TaxID=1840584;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=30127518; DOI=10.1038/s41598-018-30653-w;
RA Hattan J., Shindo K., Sasaki T., Ohno F., Tokuda H., Ishikawa K.,
RA Misawa N.;
RT "Identification of novel sesquiterpene synthase genes that mediate the
RT biosynthesis of valerianol, which was an unknown ingredient of tea.";
RL Sci. Rep. 8:12474-12474(2018).
CC -!- FUNCTION: Terpene synthase that catalyzes the biosynthesis of the
CC terpene valerianol, which is a volatile compound of floral scent.
CC {ECO:0000269|PubMed:30127518}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = diphosphate + valerianol;
CC Xref=Rhea:RHEA:60424, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:143779, ChEBI:CHEBI:175763; EC=4.2.3.204;
CC Evidence={ECO:0000269|PubMed:30127518};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60425;
CC Evidence={ECO:0000269|PubMed:30127518};
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:0000305}.
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. {ECO:0000305}.
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DR EMBL; LC212981; BBC44641.1; -; mRNA.
DR AlphaFoldDB; A0A348AUW0; -.
DR SMR; A0A348AUW0; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0016838; F:carbon-oxygen lyase activity, acting on phosphates; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
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 2: Evidence at transcript level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..554
FT /note="Valerianol synthase TPS1F"
FT /id="PRO_0000451723"
FT MOTIF 326..330
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 452
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
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"
SQ SEQUENCE 554 AA; 64122 MW; 5024B1DE152B280C CRC64;
MASSQVGDMV NGNAEPTRHL AKFPPSLWGD RFTSFTLDKQ LWDKYGNEIE VLKEQVRSMV
VAGGRKAAEQ INLINVLERL GVSYHFEKEI EEQLEQLFAK FEDNEDYDLF TIALHFRIFR
QHGYKMSCDV FNKFRDSNCE FKETVSNDVQ GMLSLYEATY LKIRGEGFLD EAHAFTIAQL
ESLVEGPHLS SDLSEQVMHA LKQSIHRGFP RLEAKHFISF YEKDASRNET LLRLAKLDFN
QLQLSHREEL CHIFRWWKEL DLISKVPYAR DRAVECFFWS TCAYYEPQHS VGRAGLTKIM
LLLSVTDDTY DAYGTYNELK LYTNAVQRWD VSAMDELPDY MKALYRALLN VYDEVERDLA
KQGRAYGVHH SKEAFKEIVR SYEIEAEWFK EGYVASFEEY MKNALVTSTG RLHTTSCFMG
LEADVATTEA FEWILTKPKM VAASGAIGRL VDDVMSHDEE QERGHVATGL DCYMKQHGVS
KQEAIVELYK MIENAWRDIN EEMLKPTAIS MKLLIRVLNL SRISDVVYKY VDGYTHPEII
NDHVISLFED PIPM
