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O81192

- BPPS_SALOF

UniProt

O81192 - BPPS_SALOF

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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

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

Mg2+1 PublicationNote: Binds 3 Mg(2+) 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
Complete GO annotation...

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-KW
Complete GO annotation...

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 – 726Combined sources
Helixi80 – 9819Combined sources
Helixi103 – 11513Combined sources
Helixi119 – 1224Combined sources
Helixi123 – 13614Combined sources
Helixi138 – 1425Combined sources
Helixi150 – 16213Combined sources
Helixi169 – 1757Combined sources
Beta strandi180 – 1834Combined sources
Helixi185 – 1895Combined sources
Helixi191 – 20111Combined sources
Helixi209 – 22517Combined sources
Helixi235 – 24612Combined sources
Helixi249 – 2513Combined sources
Turni254 – 2563Combined sources
Helixi258 – 26710Combined sources
Helixi273 – 30432Combined sources
Helixi306 – 3094Combined sources
Helixi317 – 32711Combined sources
Helixi334 – 35522Combined sources
Helixi360 – 37213Combined sources
Helixi377 – 3804Combined sources
Helixi383 – 40725Combined sources
Helixi412 – 43524Combined sources
Helixi441 – 45111Combined sources
Helixi454 – 4629Combined sources
Helixi472 – 4798Combined sources
Helixi483 – 49816Combined sources
Helixi513 – 5219Combined sources
Helixi525 – 54824Combined sources
Helixi555 – 57117Combined sources
Turni572 – 5743Combined sources
Turni577 – 5815Combined sources
Helixi584 – 59310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

« Hide

        10         20         30         40         50
MSIISMNVSI LSKPLNCLHN LERRPSKALL VPCTAPTARL RASCSSKLQE
60 70 80 90 100
AHQIRRSGNY QPALWDSNYI QSLNTPYTEE RHLDRKAELI VQVRILLKEK
110 120 130 140 150
MEPVQQLELI HDLKYLGLSD FFQDEIKEIL GVIYNEHKCF HNNEVEKMDL
160 170 180 190 200
YFTALGFRLL RQHGFNISQD VFNCFKNEKG IDFKASLAQD TKGMLQLYEA
210 220 230 240 250
SFLLRKGEDT LELAREFATK CLQKKLDEGG NEIDENLLLW IRHSLDLPLH
260 270 280 290 300
WRIQSVEARW FIDAYARRPD MNPLIFELAK LNFNIIQATH QQELKDLSRW
310 320 330 340 350
WSRLCFPEKL PFVRDRLVES FFWAVGMFEP HQHGYQRKMA ATIIVLATVI
360 370 380 390 400
DDIYDVYGTL DELELFTDTF KRWDTESITR LPYYMQLCYW GVHNYISDAA
410 420 430 440 450
YDILKEHGFF CLQYLRKSVV DLVEAYFHEA KWYHSGYTPS LDEYLNIAKI
460 470 480 490 500
SVASPAIISP TYFTFANASH DTAVIDSLYQ YHDILCLAGI ILRLPDDLGT
510 520 530 540 550
SYFELARGDV PKTIQCYMKE TNASEEEAVE HVKFLIREAW KDMNTAIAAG
560 570 580 590
YPFPDGMVAG AANIGRVAQF IYLHGDGFGV QHSKTYEHIA GLLFEPYA
Length:598
Mass (Da):69,292
Last modified:November 1, 1998 - v1
Checksum:iF2DBDE3AC4C43F67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051900 mRNA. Translation: AAC26017.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF051900 mRNA. Translation: AAC26017.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 74 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