Top Level Name

  ⌊ Superfamily (core) Isoprenoid Synthase Type I

    ⌊ Subgroup Terpene Cyclase Like 1 C Terminal Domain

     ⌊ Family (+)-bornyl diphosphate synthase

  ⌊ FunctionalDomain bornyl diphosphate synthase, C terminal domain (ID 3644)

Superfamily Assignment Evidence Code(s) ISS
Family Assignment Evidence Code IES
This entry was last updated onJuly 25, 2014

References to Other Databases

Genbank

SpeciesGIAccessionModel
Salvia officinalis 27065865 MB
Salvia officinalis 27065864 MB
Salvia officinalis 27065862 MB
Show All

Uniprot

Protein NameAccessionIdentifierModel
(+)-bornyl diphosphate synthase, chloroplastic O81192 BPPS_SALOF (SwissProt) MB

Sequence

Length of Enzyme (full-length): 549 | Length of Functional Domain: 328

1       10        20        30        40        50        60

EAHQIRRSGNYQPALWDSNYIQSLNTPYTEERHLDRKAELIVQVRILLKEKMEPVQQLEL
IHDLKYLGLSDFFQDEIKEILGVIYNEHKCFHNNEVEKMDLYFTALGFRLLRQHGFNISQ
DVFNCFKNEKGIDFKASLAQDTKGMLQLYEASFLLRKGEDTLELAREFATKCLQKKLDEG
GNEIDENLLLWIRHSLDLPLHWRIQSVEARWFIDAYARRPDMNPLIFELAKLNFNIIQAT
HQQELKDLSRWWSRLCFPEKLPFVRDRLVESFFWAVGMFEPHQHGYQRKMAATIIVLATV
IDDIYDVYGTLDELELFTDTFKRWDTESITRLPYYMQLCYWGVHNYISDAAYDILKEHGF
FCLQYLRKSVVDLVEAYFHEAKWYHSGYTPSLDEYLNIAKISVASPAIISPTYFTFANAS
HDTAVIDSLYQYHDILCLAGIILRLPDDLGTSYFELARGDVPKTIQCYMKETNASEEEAV
EHVKFLIREAWKDMNTAIAAGYPFPDGMVAGAANIGRVAQFIYLHGDGFGVQHSKTYEHI
AGLLFEPYA

FASTA | BLAST | HMM

This shows the full-length sequence of the enzyme. The region of the functional domain is highlighted in black letters, while the residual residues are shown in grey. In many cases the functional domain is the full-length sequence. Conserved catalytic residues (as determined by automated alignment to family, subgroup, or superfamily HMMs) are shown with teal highlighting . Conserved catalytic residues which do not matched the Conserved Alignment Residue are shown with maroon highlighting . Information regarding their function can be found in the Conserved Residues section below.
FASTA formatted full-length sequence.
BLAST this sequence against SFLD.
Scan SFLD-HMMs with this sequence.

Conserved Residues

This EFD conserves 0/0 Family-specific CRs and 6/10 Subgroup-specific CRs.
Position Amino Acid Family/Subgroup CAR Function Evidence Code Reference
302 Asp (D) Subgroup Metal ligand ICS
303 Asp (D) Subgroup None ISS
306 Asp (D) Subgroup Metal ligand ICS
447 Asp (D) Subgroup None ISS
448 Asp (D) Subgroup Metal ligand ICS
455 Glu (E) Subgroup Metal ligand ICS

Catalyzed Reaction(s)

(+)-bornyl diphosphate synthase

Evidence Code: IDA

EC: 5.5.1.8 | IntEnz: 5.5.1.8 | Kegg: 5.5.1.8 | BioCyc: 5.5.1.8 | BRENDA: 5.5.1.8 | MACiE: M0259

Structures

PDB ID Title Molecule Name Number of
EFDs
Resolution (Å) Mutant? Het group Chimera Session Links
1N1Z (+)-Bornyl Diphosphate Synthase: Complex With Mg And Pyrophosphate (+)-Bornyl Diphosphate Synthase 10 2.3 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
1N1B Crystal Structure Of (+)-Bornyl Diphosphate Synthase From Sage (+)-Bornyl Diphosphate Synthase 10 2.0 Magnesium Ion • Mercury (Ii) Ion CSA • PDB • PDBSum
1N23 (+)-Bornyl Diphosphate Synthase: Complex With Mg, Pyrophosphate, And (1R,4S)-2-Azabornane (+)-Bornyl Diphosphate Synthase 10 2.4 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
1N22 (+)-Bornyl Diphosphate Synthase: Complex With Mg, Pyrophosphate, And (4R)-7-Aza-7,8-Dihydrolimonene (+)-Bornyl Diphosphate Synthase 10 2.4 Magnesium Ion
(2 more ⇓)
CSA • PDB • PDBSum
1N21 (+)-Bornyl Diphosphate Synthase: Cocrystal With Mg And 3-Aza-2,3-Dihydrogeranyl Diphosphate (+)-Bornyl Diphosphate Synthase 10 3.1 Magnesium Ion • 2-[Methyl-(4-Methyl-Pent-3-Enyl)-Amino]-Ethyl-Diphosphate CSA • PDB • PDBSum
1N20 (+)-Bornyl Diphosphate Synthase: Complex With Mg And 3-Aza-2,3-Dihydrogeranyl Diphosphate (+)-Bornyl Diphosphate Synthase 10 2.3 Magnesium Ion • 2-[Methyl-(4-Methyl-Pent-3-Enyl)-Amino]-Ethyl-Diphosphate CSA • PDB • PDBSum
1N24 (+)-Bornyl Diphosphate Synthase: Complex With Mg And Product (+)-Bornyl Diphosphate Synthase 10 2.3 Magnesium Ion • (+)-Bornyl Diphosphate CSA • PDB • PDBSum
Percent identity and alignment length from the BLAST match of the Functional Domain sequence to the PDB sequence.
"Yes" indicates that a GI associated with this Functional Domain was mapped to the PDB ID via Uniprot.

Curation History

Time Change Annotation Old Value New Value
April 30, 2014, 11:58 a.m. update curation agent holliday setDomainBoundaries.py
update domain end position 598 549
update domain start position 271 222