TPS4_CANOD
ID TPS4_CANOD Reviewed; 586 AA.
AC A0A7G5KLV3;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 1.
DT 03-AUG-2022, entry version 6.
DE RecName: Full=Monoterpene synthase TPS4, chloroplastic {ECO:0000305};
DE AltName: Full=Geraniol synthase TPS4 {ECO:0000305};
DE EC=3.1.7.11 {ECO:0000269|PubMed:25956881};
DE AltName: Full=Terpene synthase 4 {ECO:0000303|PubMed:25956881};
DE Short=CoTPS4 {ECO:0000303|PubMed:25956881};
DE Flags: Precursor;
GN Name=TPS4 {ECO:0000303|PubMed:25956881};
OS Cananga odorata (Ylang-ylang tree) (Uvaria odorata).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Magnoliidae; Magnoliales; Annonaceae;
OC Ambavioideae; Cananga.
OX NCBI_TaxID=13393;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND MOTIF.
RX PubMed=25956881; DOI=10.1093/jxb/erv196;
RA Jin J., Kim M.J., Dhandapani S., Tjhang J.G., Yin J.L., Wong L.,
RA Sarojam R., Chua N.H., Jang I.C.;
RT "The floral transcriptome of ylang ylang (Cananga odorata var. fruticosa)
RT uncovers biosynthetic pathways for volatile organic compounds and a
RT multifunctional and novel sesquiterpene synthase.";
RL J. Exp. Bot. 66:3959-3975(2015).
CC -!- FUNCTION: Monoterpene synthase involved in the biosynthesis of volatile
CC organic compounds (PubMed:25956881). Mediates the conversion of (2E)-
CC geranyl diphosphate (GPP) into the acyclic monoterpene, geraniol
CC (PubMed:25956881). Does not use (2E,6E)-farnesyl diphosphate (FPP) as
CC substrate (PubMed:25956881). {ECO:0000269|PubMed:25956881}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + H2O = (2E)-geraniol + diphosphate;
CC Xref=Rhea:RHEA:32679, ChEBI:CHEBI:15377, ChEBI:CHEBI:17447,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057; EC=3.1.7.11;
CC Evidence={ECO:0000269|PubMed:25956881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32680;
CC Evidence={ECO:0000269|PubMed:25956881};
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 -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q40577}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000269|PubMed:25956881}.
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|PubMed:25956881}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsg subfamily.
CC {ECO:0000305}.
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DR EMBL; MN230108; QMW48845.1; -; mRNA.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; Hydrolase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..586
FT /note="Monoterpene synthase TPS4, chloroplastic"
FT /id="PRO_0000455181"
FT MOTIF 340..344
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:25956881"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 340
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 344
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 485
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 586 AA; 67366 MW; A8A2702D91F2356D CRC64;
MAATRNLSLL AQSSQPWAGI YGSHGSPRPI SSWLRRQSIA KTSYICMCTP LSMSQLIATP
LITDIESLLK YLRQPQVLPH EIDDSTKRRE LLERTRRELQ TTLEPLQAMK MIDTLQRLGL
AYHFEDDINS LLTGFSNGQP DEDLLTASLR FRLLRHNGHR INPNIFQKFM DKQGKFIDSL
KEDTRGLFSL YEASYLGANG EDILLQALEF TKAHLKESLP SLAPPLAKKV SQALELPRHR
RMARLEARRY IEEYGGENGH SPDLLELAKL DYNKVQSLHQ LELSEISRWW KQLGLVDKLT
FARDRPLECF LWTVGILPEP KYSSCRIELA KTIAILLVID DIFDTHGTLD ELILFTNAIR
RWDLEAMEDL PEYMRICYMA LYNTTNEICY KILKQNGWSV LPYLKATWID MIEGFMLEAS
WLNTGYVPNM EEYVENGVTT AGAYMALVHL FFLIGQGVTE ENVKLLVKPY PKLFSYSGRI
LRLWDDLGTA KEEQERGDLA SSIDLFMREN NITSDEEGRK CILKIIDNLW KELNGELVSR
HALPLAIIKA AFNMARASQV VYQHEEDSYF SSVDNYVQAL FFTPFN
