Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O81192 (BPPS_SALOF) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
(+)-bornyl diphosphate synthase, chloroplastic

Short name=BPPS
EC=5.5.1.8
Alternative name(s):
(+)-alpha-pinene synthase
EC=4.2.3.121
(+)-camphene synthase
EC=4.2.3.116
SBS
OrganismSalvia officinalis (Sage)
Taxonomic identifier38868 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsLamialesLamiaceaeNepetoideaeMentheaeSalvia

Protein attributes

Sequence length598 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of the (+)-camphor precursor (+)-bornyl diphosphate from geranyl diphosphate. The enzyme also produces significant amounts of (+)-alpha-pinene, (+)-camphene, and (+-)-limonene. Ref.1

Catalytic activity

Geranyl diphosphate = (+)-bornyl diphosphate. Ref.1

Geranyl diphosphate = (+)-camphene + diphosphate. Ref.1

Geranyl diphosphate = (+)-alpha-pinene + diphosphate. Ref.1

Cofactor

Binds 3 magnesium ions per subunit. Ref.2

Pathway

Terpene metabolism; (R)-camphor biosynthesis.

Subunit structure

Homodimer.

Subcellular location

Plastidchloroplast.

Domain

The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg2+.

Sequence similarities

Belongs to the terpene synthase family.

Ontologies

Keywords
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
Lyase
   Technical term3D-structure
Gene Ontology (GO)
   Biological_process(+)-camphor biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiongeranyl-diphosphate cyclase activity

Inferred from electronic annotation. Source: UniProtKB-EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

terpene synthase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5454Chloroplast Probable
Chain55 – 598544(+)-bornyl diphosphate synthase, chloroplastic
PRO_0000033622

Regions

Motif351 – 3555DDXXD motif

Sites

Metal binding3511Magnesium 1
Metal binding3511Magnesium 2
Metal binding3551Magnesium 1
Metal binding3551Magnesium 2
Metal binding4961Magnesium 3
Metal binding5001Magnesium 3
Metal binding5041Magnesium 3

Secondary structure

................................................................... 598
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O81192 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: F2DBDE3AC4C43F67

FASTA59869,292
        10         20         30         40         50         60 
MSIISMNVSI LSKPLNCLHN LERRPSKALL VPCTAPTARL RASCSSKLQE AHQIRRSGNY 

        70         80         90        100        110        120 
QPALWDSNYI QSLNTPYTEE RHLDRKAELI VQVRILLKEK MEPVQQLELI HDLKYLGLSD 

       130        140        150        160        170        180 
FFQDEIKEIL GVIYNEHKCF HNNEVEKMDL YFTALGFRLL RQHGFNISQD VFNCFKNEKG 

       190        200        210        220        230        240 
IDFKASLAQD TKGMLQLYEA SFLLRKGEDT LELAREFATK CLQKKLDEGG NEIDENLLLW 

       250        260        270        280        290        300 
IRHSLDLPLH WRIQSVEARW FIDAYARRPD MNPLIFELAK LNFNIIQATH QQELKDLSRW 

       310        320        330        340        350        360 
WSRLCFPEKL PFVRDRLVES FFWAVGMFEP HQHGYQRKMA ATIIVLATVI DDIYDVYGTL 

       370        380        390        400        410        420 
DELELFTDTF KRWDTESITR LPYYMQLCYW GVHNYISDAA YDILKEHGFF CLQYLRKSVV 

       430        440        450        460        470        480 
DLVEAYFHEA KWYHSGYTPS LDEYLNIAKI SVASPAIISP TYFTFANASH DTAVIDSLYQ 

       490        500        510        520        530        540 
YHDILCLAGI ILRLPDDLGT SYFELARGDV PKTIQCYMKE TNASEEEAVE HVKFLIREAW 

       550        560        570        580        590 
KDMNTAIAAG YPFPDGMVAG AANIGRVAQF IYLHGDGFGV QHSKTYEHIA GLLFEPYA 

« Hide

References

[1]"Monoterpene synthases from common sage (Salvia officinalis). cDNA isolation, characterization, and functional expression of (+)-sabinene synthase, 1,8-cineole synthase, and (+)-bornyl diphosphate synthase."
Wise M.L., Savage T.J., Katahira E., Croteau R.
J. Biol. Chem. 273:14891-14899(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
[2]"Bornyl diphosphate synthase: structure and strategy for carbocation manipulation by a terpenoid cyclase."
Whittington D.A., Wise M.L., Urbansky M., Coates R.M., Croteau R.B., Christianson D.W.
Proc. Natl. Acad. Sci. U.S.A. 99:15375-15380(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 50-598 IN COMPLEXES WITH MAGNESIUM IONS; GERANYL DIPHOSPHATE AND BORNYL DIPHOSPHATE, COFACTOR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF051900 mRNA. Translation: AAC26017.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N1BX-ray2.00A/B50-598[»]
1N1ZX-ray2.30A/B50-598[»]
1N20X-ray2.30A/B50-598[»]
1N21X-ray3.10A50-598[»]
1N22X-ray2.40A/B50-598[»]
1N23X-ray2.40A/B50-598[»]
1N24X-ray2.30A/B50-598[»]
ProteinModelPortalO81192.
SMRO81192. Positions 54-598.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-13764.
BRENDA5.5.1.8. 5564.
UniPathwayUPA00720.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
1.50.30.10. 1 hit.
InterProIPR001906. Terpene_synth_N.
IPR005630. Terpene_synthase_metal-bd.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF01397. Terpene_synth. 1 hit.
PF03936. Terpene_synth_C. 1 hit.
[Graphical view]
SUPFAMSSF48239. SSF48239. 1 hit.
SSF48576. SSF48576. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO81192.

Entry information

Entry nameBPPS_SALOF
AccessionPrimary (citable) accession number: O81192
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 1, 1998
Last modified: February 19, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways