ID BPPS_SALOF Reviewed; 598 AA. AC O81192; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 103. DE RecName: Full=(+)-bornyl diphosphate synthase, chloroplastic; DE Short=BPPS; DE EC=5.5.1.8; DE AltName: Full=(+)-alpha-pinene synthase; DE EC=4.2.3.121; DE AltName: Full=(+)-camphene synthase; DE EC=4.2.3.116; DE AltName: Full=SBS; DE Flags: Precursor; OS Salvia officinalis (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=38868; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=9614092; DOI=10.1074/jbc.273.24.14891; RA Wise M.L., Savage T.J., Katahira E., Croteau R.; RT "Monoterpene synthases from common sage (Salvia officinalis). cDNA RT isolation, characterization, and functional expression of (+)-sabinene RT synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase."; RL J. Biol. Chem. 273:14891-14899(1998). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 50-598 IN COMPLEXES WITH MAGNESIUM RP IONS; GERANYL DIPHOSPHATE AND BORNYL DIPHOSPHATE, AND COFACTOR. RX PubMed=12432096; DOI=10.1073/pnas.232591099; RA Whittington D.A., Wise M.L., Urbansky M., Coates R.M., Croteau R.B., RA Christianson D.W.; RT "Bornyl diphosphate synthase: structure and strategy for carbocation RT manipulation by a terpenoid cyclase."; RL Proc. Natl. Acad. Sci. U.S.A. 99:15375-15380(2002). CC -!- FUNCTION: Catalyzes the formation of the (+)-camphor precursor (+)- CC bornyl diphosphate from geranyl diphosphate. The enzyme also produces CC significant amounts of (+)-alpha-pinene, (+)-camphene, and (+-)- CC limonene. {ECO:0000269|PubMed:9614092}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-geranyl diphosphate = (2S,4R)-bornyl diphosphate; CC Xref=Rhea:RHEA:18209, ChEBI:CHEBI:57293, ChEBI:CHEBI:58057; CC EC=5.5.1.8; Evidence={ECO:0000269|PubMed:9614092}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-geranyl diphosphate = (1R,4S)-camphene + diphosphate; CC Xref=Rhea:RHEA:32567, ChEBI:CHEBI:20, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58057; EC=4.2.3.116; CC Evidence={ECO:0000269|PubMed:9614092}; CC -!- CATALYTIC ACTIVITY: CC Reaction=(2E)-geranyl diphosphate = (1R,5R)-alpha-pinene + diphosphate; CC Xref=Rhea:RHEA:32575, ChEBI:CHEBI:28261, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:58057; EC=4.2.3.121; CC Evidence={ECO:0000269|PubMed:9614092}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:12432096}; CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:12432096}; CC -!- PATHWAY: Terpene metabolism; (R)-camphor biosynthesis. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. 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:12432096}. CC -!- SIMILARITY: Belongs to the terpene synthase family. {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; AF051900; AAC26017.1; -; mRNA. DR PDB; 1N1B; X-ray; 2.00 A; A/B=50-598. DR PDB; 1N1Z; X-ray; 2.30 A; A/B=50-598. DR PDB; 1N20; X-ray; 2.30 A; A/B=50-598. DR PDB; 1N21; X-ray; 3.10 A; A=50-598. DR PDB; 1N22; X-ray; 2.40 A; A/B=50-598. DR PDB; 1N23; X-ray; 2.40 A; A/B=50-598. DR PDB; 1N24; X-ray; 2.30 A; A/B=50-598. DR PDBsum; 1N1B; -. DR PDBsum; 1N1Z; -. DR PDBsum; 1N20; -. DR PDBsum; 1N21; -. DR PDBsum; 1N22; -. DR PDBsum; 1N23; -. DR PDBsum; 1N24; -. DR AlphaFoldDB; O81192; -. DR SMR; O81192; -. DR KEGG; ag:AAC26017; -. DR BioCyc; MetaCyc:MONOMER-13764; -. DR BRENDA; 5.5.1.8; 5564. DR SABIO-RK; O81192; -. DR UniPathway; UPA00720; -. DR EvolutionaryTrace; O81192; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0102703; F:camphene synthase activity; IDA:UniProtKB. DR GO; GO:0047926; F:geranyl-diphosphate cyclase activity; IDA:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro. DR GO; GO:0046211; P:(+)-camphor biosynthetic process; IDA:UniProtKB. DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro. DR CDD; cd00684; Terpene_cyclase_plant_C1; 1. DR Gene3D; 1.10.600.10; Farnesyl Diphosphate Synthase; 1. DR Gene3D; 1.50.10.130; Terpene synthase, N-terminal domain; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf. 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 PANTHER; PTHR31225; OS04G0344100 PROTEIN-RELATED; 1. DR PANTHER; PTHR31225:SF223; TERPENE SYNTHASE 10-LIKE ISOFORM X1; 1. DR Pfam; PF01397; Terpene_synth; 1. DR Pfam; PF03936; Terpene_synth_C; 1. DR SFLD; SFLDS00005; Isoprenoid_Synthase_Type_I; 1. DR SFLD; SFLDG01604; Terpene_Cyclase_Like_1_C_Termi; 1. DR SFLD; SFLDG01014; Terpene_Cyclase_Like_1_N-term; 1. DR SUPFAM; SSF48239; Terpenoid cyclases/Protein prenyltransferases; 1. DR SUPFAM; SSF48576; Terpenoid synthases; 1. PE 1: Evidence at protein level; KW 3D-structure; Chloroplast; Isomerase; Lyase; Magnesium; Metal-binding; KW Plastid; Transit peptide. FT TRANSIT 1..54 FT /note="Chloroplast" FT /evidence="ECO:0000305" FT CHAIN 55..598 FT /note="(+)-bornyl diphosphate synthase, chloroplastic" FT /id="PRO_0000033622" FT MOTIF 351..355 FT /note="DDXXD motif" FT /evidence="ECO:0000305" FT BINDING 314 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12432096, FT ECO:0007744|PDB:1N1Z" FT BINDING 351 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:12432096, FT ECO:0007744|PDB:1N1Z" FT BINDING 351 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:12432096, FT ECO:0007744|PDB:1N1Z" FT BINDING 355 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:12432096, FT ECO:0007744|PDB:1N1Z" FT BINDING 355 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:12432096, FT ECO:0007744|PDB:1N1Z" FT BINDING 493 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12432096, FT ECO:0007744|PDB:1N1Z" FT BINDING 496 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:12432096, FT ECO:0007744|PDB:1N1Z" FT BINDING 500 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:12432096, FT ECO:0007744|PDB:1N1Z" FT BINDING 500 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12432096, FT ECO:0007744|PDB:1N1Z" FT BINDING 504 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT /evidence="ECO:0000269|PubMed:12432096, FT ECO:0007744|PDB:1N1Z" FT BINDING 512 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:12432096, FT ECO:0007744|PDB:1N1Z" FT HELIX 67..72 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 80..98 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 103..115 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 119..122 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 123..136 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 138..142 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 150..162 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 169..175 FT /evidence="ECO:0007829|PDB:1N1B" FT STRAND 180..183 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 185..189 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 191..201 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 209..225 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 235..246 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 249..251 FT /evidence="ECO:0007829|PDB:1N1B" FT TURN 254..256 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 258..267 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 273..304 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 306..309 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 317..327 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 334..355 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 360..372 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 377..380 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 383..407 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 412..435 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 441..451 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 454..462 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 472..479 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 483..498 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 513..521 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 525..548 FT /evidence="ECO:0007829|PDB:1N1B" FT HELIX 555..571 FT /evidence="ECO:0007829|PDB:1N1B" FT TURN 572..574 FT /evidence="ECO:0007829|PDB:1N1B" FT TURN 577..581 FT /evidence="ECO:0007829|PDB:1N1Z" FT HELIX 584..593 FT /evidence="ECO:0007829|PDB:1N1B" SQ SEQUENCE 598 AA; 69292 MW; F2DBDE3AC4C43F67 CRC64; MSIISMNVSI LSKPLNCLHN LERRPSKALL VPCTAPTARL RASCSSKLQE AHQIRRSGNY QPALWDSNYI QSLNTPYTEE RHLDRKAELI VQVRILLKEK MEPVQQLELI HDLKYLGLSD FFQDEIKEIL GVIYNEHKCF HNNEVEKMDL YFTALGFRLL RQHGFNISQD VFNCFKNEKG IDFKASLAQD TKGMLQLYEA SFLLRKGEDT LELAREFATK CLQKKLDEGG NEIDENLLLW IRHSLDLPLH WRIQSVEARW FIDAYARRPD MNPLIFELAK LNFNIIQATH QQELKDLSRW WSRLCFPEKL PFVRDRLVES FFWAVGMFEP HQHGYQRKMA ATIIVLATVI DDIYDVYGTL DELELFTDTF KRWDTESITR LPYYMQLCYW GVHNYISDAA YDILKEHGFF CLQYLRKSVV DLVEAYFHEA KWYHSGYTPS LDEYLNIAKI SVASPAIISP TYFTFANASH DTAVIDSLYQ YHDILCLAGI ILRLPDDLGT SYFELARGDV PKTIQCYMKE TNASEEEAVE HVKFLIREAW KDMNTAIAAG YPFPDGMVAG AANIGRVAQF IYLHGDGFGV QHSKTYEHIA GLLFEPYA //