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O81192

- BPPS_SALOF

UniProt

O81192 - BPPS_SALOF

Protein

(+)-bornyl diphosphate synthase, chloroplastic

Gene
N/A
Organism
Salvia officinalis (Sage)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

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

    Catalytic activityi

    Geranyl diphosphate = (+)-bornyl diphosphate.1 Publication
    Geranyl diphosphate = (+)-camphene + diphosphate.1 Publication
    Geranyl diphosphate = (+)-alpha-pinene + diphosphate.1 Publication

    Cofactori

    Binds 3 magnesium ions per subunit.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi351 – 3511Magnesium 1
    Metal bindingi351 – 3511Magnesium 2
    Metal bindingi355 – 3551Magnesium 1
    Metal bindingi355 – 3551Magnesium 2
    Metal bindingi496 – 4961Magnesium 3
    Metal bindingi500 – 5001Magnesium 3
    Metal bindingi504 – 5041Magnesium 3

    GO - Molecular functioni

    1. geranyl-diphosphate cyclase activity Source: UniProtKB-EC
    2. magnesium ion binding Source: InterPro
    3. terpene synthase activity Source: InterPro

    GO - Biological processi

    1. (+)-camphor biosynthetic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Isomerase, Lyase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-13764.
    BRENDAi5.5.1.8. 5564.
    UniPathwayiUPA00720.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    (+)-bornyl diphosphate synthase, chloroplastic (EC:5.5.1.8)
    Short name:
    BPPS
    Alternative name(s):
    (+)-alpha-pinene synthase (EC:4.2.3.121)
    (+)-camphene synthase (EC:4.2.3.116)
    SBS
    OrganismiSalvia officinalis (Sage)
    Taxonomic identifieri38868 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsLamialesLamiaceaeNepetoideaeMentheaeSalvia

    Subcellular locationi

    GO - Cellular componenti

    1. chloroplast Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Chloroplast, Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5454ChloroplastCuratedAdd
    BLAST
    Chaini55 – 598544(+)-bornyl diphosphate synthase, chloroplasticPRO_0000033622Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    598
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi67 – 726
    Helixi80 – 9819
    Helixi103 – 11513
    Helixi119 – 1224
    Helixi123 – 13614
    Helixi138 – 1425
    Helixi150 – 16213
    Helixi169 – 1757
    Beta strandi180 – 1834
    Helixi185 – 1895
    Helixi191 – 20111
    Helixi209 – 22517
    Helixi235 – 24612
    Helixi249 – 2513
    Turni254 – 2563
    Helixi258 – 26710
    Helixi273 – 30432
    Helixi306 – 3094
    Helixi317 – 32711
    Helixi334 – 35522
    Helixi360 – 37213
    Helixi377 – 3804
    Helixi383 – 40725
    Helixi412 – 43524
    Helixi441 – 45111
    Helixi454 – 4629
    Helixi472 – 4798
    Helixi483 – 49816
    Helixi513 – 5219
    Helixi525 – 54824
    Helixi555 – 57117
    Turni572 – 5743
    Turni577 – 5815
    Helixi584 – 59310

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliO81192.
    SMRiO81192. Positions 54-598.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO81192.

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi351 – 3555DDXXD motif

    Domaini

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

    Sequence similaritiesi

    Belongs to the terpene synthase family.Curated

    Keywords - Domaini

    Transit peptide

    Family and domain databases

    Gene3Di1.10.600.10. 1 hit.
    1.50.30.10. 1 hit.
    InterProiIPR001906. Terpene_synth_N.
    IPR005630. Terpene_synthase_metal-bd.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    IPR008949. Terpenoid_synth.
    [Graphical view]
    PfamiPF01397. Terpene_synth. 1 hit.
    PF03936. Terpene_synth_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48239. SSF48239. 1 hit.
    SSF48576. SSF48576. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O81192-1 [UniParc]FASTAAdd to Basket

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    MSIISMNVSI LSKPLNCLHN LERRPSKALL VPCTAPTARL RASCSSKLQE    50
    AHQIRRSGNY QPALWDSNYI QSLNTPYTEE RHLDRKAELI VQVRILLKEK 100
    MEPVQQLELI HDLKYLGLSD FFQDEIKEIL GVIYNEHKCF HNNEVEKMDL 150
    YFTALGFRLL RQHGFNISQD VFNCFKNEKG IDFKASLAQD TKGMLQLYEA 200
    SFLLRKGEDT LELAREFATK CLQKKLDEGG NEIDENLLLW IRHSLDLPLH 250
    WRIQSVEARW FIDAYARRPD MNPLIFELAK LNFNIIQATH QQELKDLSRW 300
    WSRLCFPEKL PFVRDRLVES FFWAVGMFEP HQHGYQRKMA ATIIVLATVI 350
    DDIYDVYGTL DELELFTDTF KRWDTESITR LPYYMQLCYW GVHNYISDAA 400
    YDILKEHGFF CLQYLRKSVV DLVEAYFHEA KWYHSGYTPS LDEYLNIAKI 450
    SVASPAIISP TYFTFANASH DTAVIDSLYQ YHDILCLAGI ILRLPDDLGT 500
    SYFELARGDV PKTIQCYMKE TNASEEEAVE HVKFLIREAW KDMNTAIAAG 550
    YPFPDGMVAG AANIGRVAQF IYLHGDGFGV QHSKTYEHIA GLLFEPYA 598
    Length:598
    Mass (Da):69,292
    Last modified:November 1, 1998 - v1
    Checksum:iF2DBDE3AC4C43F67
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051900 mRNA. Translation: AAC26017.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051900 mRNA. Translation: AAC26017.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1N1B X-ray 2.00 A/B 50-598 [» ]
    1N1Z X-ray 2.30 A/B 50-598 [» ]
    1N20 X-ray 2.30 A/B 50-598 [» ]
    1N21 X-ray 3.10 A 50-598 [» ]
    1N22 X-ray 2.40 A/B 50-598 [» ]
    1N23 X-ray 2.40 A/B 50-598 [» ]
    1N24 X-ray 2.30 A/B 50-598 [» ]
    ProteinModelPortali O81192.
    SMRi O81192. Positions 54-598.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00720 .
    BioCyci MetaCyc:MONOMER-13764.
    BRENDAi 5.5.1.8. 5564.

    Miscellaneous databases

    EvolutionaryTracei O81192.

    Family and domain databases

    Gene3Di 1.10.600.10. 1 hit.
    1.50.30.10. 1 hit.
    InterProi IPR001906. Terpene_synth_N.
    IPR005630. Terpene_synthase_metal-bd.
    IPR008930. Terpenoid_cyclase/PrenylTrfase.
    IPR008949. Terpenoid_synth.
    [Graphical view ]
    Pfami PF01397. Terpene_synth. 1 hit.
    PF03936. Terpene_synth_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48239. SSF48239. 1 hit.
    SSF48576. SSF48576. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiBPPS_SALOF
    AccessioniPrimary (citable) accession number: O81192
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2005
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3