BPPS_SALOF
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 03-AUG-2022, entry version 99.
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}.
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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:MON-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; -; 1.
DR Gene3D; 1.50.10.130; -; 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 Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 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
