TPS4_MATCR
ID TPS4_MATCR Reviewed; 596 AA.
AC I6RE61;
DT 03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=(E)-beta-ocimene synthase, chloroplastic;
DE EC=4.2.3.106;
DE AltName: Full=Terpene synthase 4;
DE Flags: Precursor;
OS Matricaria chamomilla var. recutita (German chamomile) (Chamomilla
OS recutita).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Anthemideae;
OC Matricariinae; Matricaria.
OX NCBI_TaxID=127986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Bodegold;
RX PubMed=22682202; DOI=10.1186/1471-2229-12-84;
RA Irmisch S., Krause S.T., Kunert G., Gershenzon J., Degenhardt J.,
RA Koellner T.G.;
RT "The organ-specific expression of terpene synthase genes contributes to the
RT terpene hydrocarbon composition of chamomile essential oils.";
RL BMC Plant Biol. 12:84-84(2012).
CC -!- FUNCTION: Monoterpene synthase involved in the biosynthesis of (E)-
CC beta-ocimene as the major product and trace amounts of (Z)-beta-
CC ocimene. Can only accept geranyl diphosphate as substrate.
CC {ECO:0000269|PubMed:22682202}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate;
CC Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:64280; EC=4.2.3.106;
CC Evidence={ECO:0000269|PubMed:22682202};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves, stems and disk florets.
CC Detected in roots. {ECO:0000269|PubMed:22682202}.
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}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsb subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQ255378; AFM43737.1; -; mRNA.
DR AlphaFoldDB; I6RE61; -.
DR SMR; I6RE61; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0034768; F:(E)-beta-ocimene synthase activity; IEA:UniProtKB-EC.
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 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 Chloroplast; Lyase; Magnesium; Manganese; Metal-binding; Plastid;
KW Transit peptide.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 36..596
FT /note="(E)-beta-ocimene synthase, chloroplastic"
FT /id="PRO_0000421928"
FT MOTIF 344..348
FT /note="DDXXD motif"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 496
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 596 AA; 69526 MW; 79DD7AA8917313B1 CRC64;
MAITHYQMAS FQSSFHFCML RKTLRQKSSL HFAKRCEATN KIFQTHGSVA IYQKTLWTHD
LIDGLETDFL INRKEKVNEL EVNVARMFMD YENGDISNLE LLELIDNIER LGLGHRFQTN
MKRVLDKIAT VNENSLGLKE EEEEEEEEED NLHALSLKFR ILRQSGYRVS QDFQRKFKES
RGGLTGGLKE LLSIYEASYL SLEGEPDLHE AKLFATEKLL KLTGHENEAM KDHVNHALDI
PLYRRMLRLE ARWYIDAYGK RKDANKQLLE LAILDFNIVQ SAHKRDLQEV SKWWEKTGLV
RKLDFIRDRL MECFFWSVGM VFEPQYYTCR VELTKIATLI TTIDDIYDVY GSLNELKVFT
HAVKRWDINA VENMPEYLQL GFLALYNTIN EMGYETLSAQ GINIIPNLAR VWGELLEAFL
VEAEWTHNNY MPTFKDYLDN AWRSVSGMVL LTHGYFLMNQ DVKDDAIESL ENFHDLFKWS
SMLFRLYNDL AALADEIDKD KSPNAISCYM YEHSVSEEVA REHVKTLIDK AWMKMIEARI
ACSEHMTDPL IDMAINLARV SSCMYQYGDG IKDPEARTKD RVMSIIIKPF DTSEIP
