TPS8_COFAR
ID TPS8_COFAR Reviewed; 580 AA.
AC R4YVJ8; A0A6P6SDD0;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-MAY-2022, sequence version 2.
DT 03-AUG-2022, entry version 31.
DE RecName: Full=Putative monoterpene synthase 8 {ECO:0000303|PubMed:23398891};
DE Flags: Precursor;
GN Name=TPS8 {ECO:0000303|PubMed:23398891};
OS Coffea arabica (Arabian coffee).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX NCBI_TaxID=13443;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Catuai Red; TISSUE=Flower, Fruit, and Seed;
RX PubMed=23398891; DOI=10.1016/j.phytochem.2013.01.005;
RA Del Terra L., Lonzarich V., Asquini E., Navarini L., Graziosi G.,
RA Suggi Liverani F., Pallavicini A.;
RT "Functional characterization of three Coffea arabica L. monoterpene
RT synthases: insights into the enzymatic machinery of coffee aroma.";
RL Phytochemistry 89:6-14(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Caturra red;
RA Zimin A.V., Yepes M., Maldonado C.E., Navarro L., Kovaka S., Pertea M.,
RA Gaitan A., Aldwinckle H.;
RT "The Coffea arabica cultivar Caturra genome provides a strong foundation
RT for breeding and functional genomics studies in coffee.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Monoterpene synthase (mono-TPS) involved in the biosynthesis
CC of monoterpenes natural products, constituent of coffee beverage aroma.
CC {ECO:0000250|UniProtKB:A0A6P6W6H5}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000250|UniProtKB:A0A6P6W6H5}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6JD73}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Confined to flowers. {ECO:0000269|PubMed:23398891}.
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. Tpsg subfamily.
CC {ECO:0000305}.
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DR EMBL; HE985295; CCM43930.1; -; mRNA.
DR RefSeq; XP_027063789.1; XM_027207988.1.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000515148; Chromosome 5c.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Chloroplast; Magnesium; Metal-binding; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..44
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 45..580
FT /note="Putative monoterpene synthase 8"
FT /id="PRO_0000455261"
FT MOTIF 333..337
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 333
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 337
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 478
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 482
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 486
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT CONFLICT 420
FT /note="E -> V (in Ref. 1; CCM43930)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="A -> E (in Ref. 1; CCM43930)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 580 AA; 66671 MW; 5D95A183E9C5FB90 CRC64;
MACTSNLSSL SKSWAVLDVP RGAPKATGLW LKRQFIFKTS RICMCMPTPT ATQPIATPLI
RDNESLLKYL RQPSVLPHEV DDSRKELLGR TRRQLRSTSE PLKAMNLIDT LQRLGLAYHF
EDDMNAILSQ LSSSGQSDGD LLTTALRFRL LRHNGHKIVQ KFMDKNGKFK DSLKEDTMGL
LSLYEASHLA ANGEDILLEA MELTEAHLKQ SLPSLPTQLA RKVSSALELP RHRRMARLEA
RRYIQEYSEE IGHDPNLLEL AKLDYNKVQS LHQMELTEIS RWWKQLGLVD KLTFARDRPL
ECFLWTVGIL PEPKYSNCRI ELAKTIAILL VIDDIFDTHG TIDELVLFTN AIRRWDLEAM
EGLPEYMRIC YMALYNTTNE ICYKILKENG WSVLPYLKAT WIDMIEGFML EASWYNNGQE
PNMEEYVANG VTTAGAYMAM VHLFFLIGQG VTEENVKLLM KPYPKLFSCS GRILRLWDDL
GTAKEEQERG DLASSIQLFM RENNITCDEE GRKRILQLID NLWKDLNWEL VSRDAMPLAI
IKAAFNMARS SQVVYQHEEE SYFSSVDNYV ESLFFTPIIN
