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Protein

(+)-bornyl diphosphate synthase, chloroplastic

Gene
N/A
Organism
Salvia officinalis (Sage)
Status
Reviewed-Annotation score: 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 Mg2+ ions per subunit.1 Publication

Pathwayi: (R)-camphor biosynthesis

This protein is involved in the pathway (R)-camphor biosynthesis, which is part of Terpene metabolism.
View all proteins of this organism that are known to be involved in the pathway (R)-camphor biosynthesis and in Terpene metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi351Magnesium 11
Metal bindingi351Magnesium 21
Metal bindingi355Magnesium 11
Metal bindingi355Magnesium 21
Metal bindingi496Magnesium 31
Metal bindingi500Magnesium 31
Metal bindingi504Magnesium 31

GO - Molecular functioni

GO - Biological processi

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

Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 54ChloroplastCuratedAdd BLAST54
ChainiPRO_000003362255 – 598(+)-bornyl diphosphate synthase, chloroplasticAdd BLAST544

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

1598
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi67 – 72Combined sources6
Helixi80 – 98Combined sources19
Helixi103 – 115Combined sources13
Helixi119 – 122Combined sources4
Helixi123 – 136Combined sources14
Helixi138 – 142Combined sources5
Helixi150 – 162Combined sources13
Helixi169 – 175Combined sources7
Beta strandi180 – 183Combined sources4
Helixi185 – 189Combined sources5
Helixi191 – 201Combined sources11
Helixi209 – 225Combined sources17
Helixi235 – 246Combined sources12
Helixi249 – 251Combined sources3
Turni254 – 256Combined sources3
Helixi258 – 267Combined sources10
Helixi273 – 304Combined sources32
Helixi306 – 309Combined sources4
Helixi317 – 327Combined sources11
Helixi334 – 355Combined sources22
Helixi360 – 372Combined sources13
Helixi377 – 380Combined sources4
Helixi383 – 407Combined sources25
Helixi412 – 435Combined sources24
Helixi441 – 451Combined sources11
Helixi454 – 462Combined sources9
Helixi472 – 479Combined sources8
Helixi483 – 498Combined sources16
Helixi513 – 521Combined sources9
Helixi525 – 548Combined sources24
Helixi555 – 571Combined sources17
Turni572 – 574Combined sources3
Turni577 – 581Combined sources5
Helixi584 – 593Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO81192.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi351 – 355DDXXD motif5

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

Phylogenomic databases

KOiK15098.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
1.50.30.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR001906. Terpene_synth_N.
IPR005630. Terpene_synthase_metal-bd.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[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.

Genome annotation databases

KEGGiag:AAC26017.

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

KEGGiag:AAC26017.

Phylogenomic databases

KOiK15098.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiO81192.

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
1.50.30.10. 1 hit.
InterProiIPR008949. Isoprenoid_synthase_dom.
IPR001906. Terpene_synth_N.
IPR005630. Terpene_synthase_metal-bd.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamiPF01397. Terpene_synth. 1 hit.
PF03936. Terpene_synth_C. 1 hit.
[Graphical view]
SUPFAMiSSF48239. SSF48239. 1 hit.
SSF48576. SSF48576. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 81 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.