TPS1A_CAMHI
ID TPS1A_CAMHI Reviewed; 554 AA.
AC A0A348AUV5;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Valerianol synthase TPS1A {ECO:0000305};
DE EC=4.2.3.204 {ECO:0000269|PubMed:30127518};
DE AltName: Full=Terpene synthase 1 {ECO:0000303|PubMed:30127518};
DE Short=ChTPS1 {ECO:0000303|PubMed:30127518};
DE AltName: Full=Terpene synthase 1a {ECO:0000303|PubMed:30127518};
DE Short=ChTps1a {ECO:0000303|PubMed:30127518};
GN Name=TPS1A {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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
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 -!- TISSUE SPECIFICITY: Expressed in flowers.
CC {ECO:0000269|PubMed:30127518}.
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; LC212976; BBC44636.1; -; mRNA.
DR AlphaFoldDB; A0A348AUV5; -.
DR SMR; A0A348AUV5; -.
DR KEGG; ag:BBC44636; -.
DR BioCyc; MetaCyc:MON-20802; -.
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 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..554
FT /note="Valerianol synthase TPS1A"
FT /id="PRO_0000451719"
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; 64124 MW; E8A9ECFC5BED6E47 CRC64;
MASSQVGDMV NGNAEPTRHL AKFPPSLWGD RFTSFTLDKQ LWDKYGNEIE VLKEQVRSMV
VAGGRKAAEQ INLINVLERL GVSYHFEKEI EEQLEQLFAK FEDNEDYDLF TIALHFRIFR
QHGYKMSCDV FNKFRDSNGE FKETVSNDVQ GMLSLYEATY LKIRGEGFLD EAHAFTIAQL
ESLVGGPHLS SDLSEQVMHA LKQSIHRGFP RLEAKHFISF YEKDASRNET LLRLAKLDFN
QLQLSHREEL CHIFRWWKEL DLISKVPYAR DRAVECFFWS TCAYYEPQHS VGRAVLTKIM
LLLSVTDDTY DAYGTYDELK LYTNAVQRWD VSAMDELPDY MKALYRALLN VYDEVERDLA
KQGRDYGVHH SKEAFKEIVR SYEIEAEWFK EGYVASFEEY MKNALVTSTG RLHTTSCFMG
LEADVATTEA FEWILTKPKM VAASGAIGRL VDDVMSHDEE QERGHVATGL DCYMKQRGVS
KQEAIVELYK MIENAWRDIN EEMLKPTAIS MKLLIRVLNL SRISDVVYKY VDGYTHPEII
KDHVISLFED PIPM
