TPS3_SALSC
ID TPS3_SALSC Reviewed; 774 AA.
AC K4IAL8;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Diterpene synthase 3, chloroplastic {ECO:0000303|PubMed:22834731};
DE Short=SsdiTPS3 {ECO:0000303|PubMed:22834731};
DE Flags: Precursor;
GN Name=TPS3 {ECO:0000303|PubMed:22834731};
OS Salvia sclarea (Clary sage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salviinae;
OC Salvia; Salvia incertae sedis.
OX NCBI_TaxID=38869;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Sepal;
RX PubMed=22834731; DOI=10.1186/1471-2229-12-119;
RA Caniard A., Zerbe P., Legrand S., Cohade A., Valot N., Magnard J.L.,
RA Bohlmann J., Legendre L.;
RT "Discovery and functional characterization of two diterpene synthases for
RT sclareol biosynthesis in Salvia sclarea (L.) and their relevance for
RT perfume manufacture.";
RL BMC Plant Biol. 12:119-119(2012).
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q84ZW8};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q84ZW8};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:Q5GJ60};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000250|UniProtKB:Q84ZW8}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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|UniProtKB:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; JQ478436; AFU61899.1; -; mRNA.
DR AlphaFoldDB; K4IAL8; -.
DR SMR; K4IAL8; -.
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:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
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 SUPFAM; SSF48239; SSF48239; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 2: Evidence at transcript level;
KW Chloroplast; Hydrolase; Lyase; Magnesium; Manganese; Metal-binding;
KW Plastid; Transit peptide.
FT TRANSIT 1..30
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 31..774
FT /note="Diterpene synthase 3, chloroplastic"
FT /id="PRO_0000448860"
FT MOTIF 528..532
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 528
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 528
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 528
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 532
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 669
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 672
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 672
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 676
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 680
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 774 AA; 87531 MW; C0C41B450BA2C58E CRC64;
MISLMLSSSS PFRSSPFSHA SSAALDRLPR ATKLTTELAS VSPWFEERKG RIAKVFDKKE
VGISTYDTAW VAMVPSPLMI SSGEPLPCFP DSLLWLLENQ CHDGSWAQPH HHSLLNKDVL
SSTLACILAL NKWGLGDQHI AKGLHFLEMN FDSAMDPSQI TPIGFDIVFP TMLDHARSLS
LIPTLDQTML KELMNMRDLE LKRCSSSPDM EAYLAYVGEG QDRERVMKYQ RKNGSLFNSP
STTAAAYIAS PNSECLKYLN LVVNKFGGAV PAVYPLDIYS QLHTVDDLER LGISRYFVTE
IESVLDQTYR CWVQGDEEIF LDASTCALAF RLLRINGYNV SSDPVTHCVV GHMNKDVNTA
LEVYKASQLT LYPHETQLEK LNSSLGALLQ DQISSASIQS TQLHAEVQQA LDYPFYAILQ
RMANRKAIEH YNFDPTRILK TSYCLPNSGN KDFLLLSVED FNRLQAMHQE EYKEFERWFV
ENRLDELEVA RQKVEYGYFT AAATISGPEL SDARMSWAKN CVMISVMDDF FDIRGSVQEM
EKIVELVELW DVDISRECCS NDVSIIFSAL KQTISEVGDK GSKLQGRNIT PHIIALWLDL
LYSYMKEVEW SGSCSNPSFD EYMSNASVSF GLGPIVVSTL YVVGPHLSLD MINHSQYHNL
FTLTSTCCRL LHEIRSDERE LKQGKPNALP LYIAENGSMS KEAAISEMIT MSNTLRKQIL
TIVLDNNSVF PKPCKQIFWN MLVANQLFYR KDDGFWSKEL LKVAHQIVHQ PILL
