Top Level Name

  ⌊ Superfamily (core) Isoprenoid Synthase Type II

    ⌊ Subgroup Prenyltransferase Like 2

     ⌊ Family   private

  ⌊ FunctionalDomain Lanosterol (ID 148823)

Superfamily Assignment Evidence Code(s) IEA
Family Assignment Evidence Code IEA
This entry was last updated onJune 10, 2017

References to Other Databases

Genbank: obsolete GI = 114684819

Sequence

Length of Enzyme (full-length): 768 | Length of Functional Domain: 693

1       10        20        30        40        50        60

MTEGTCLRRRGGPYKTEPATDLGRWRLNCERGRQTWTYLQDERAGREQTGLEAYALGLDT
KNYFKDLPKAHTAFEGALNGMTFYVGLQAEDGHWTGDYGGPLFLLPGLLITCHVARIPLP
AGYREEIVRYLRSVQLPDGGWGLHIEDKSTVFGTALNYVSLRILGVGPDDPDLVRARNIL
HKKGGAVAIPSWGKFWLAVLNVYSWEGLNTLFPEMWLFPDWAPAHPSTLWCHCRQVYLPM
SYCYAVRLSAAEDPLVQSLRQELYVEDFASIDWLAQRNNVAPDELYTPHSWLLRVVYALL
NLYEHHHSAHLRQRAVQKLYEHIVADDRFTKSISIGPISKTINMLVRWYVDGPTSTAFQE
HVSRIPDYLWMGLDGMKMQGTNGSQIWDTAFAIQALLEAGGHHRPEFSSCLQKAHEFLRL
SQVPDNPPDYQKYYRQMRKGGFSFSTLDCGWIVSDCTAEALKAVLLLQEKCPHVTEHIPR
ERLCDAVAVLLNMRNPDGGFATYETKRGGHLLELLNPSEVFGDIMIDYTYVECTSAVMQA
LKCFHKHFPEHRAAEIRETLTQGLEFCRRQQRADGSWEGSWGVCFTYGTWFGLEAFACMG
QTYRDGTACAEVSRACDFLLSRQMADGGWGEDFESCEERRYVQSAQSQIHNTCWAMMGLM
AVRHPDIEAQERGVRCLLEKQLPNGDWPQWPSSHRTQRFPALFGVITQAGLQCQYPCLQS
SLEITSVFNPLFRGSVFFLFHEEDFLFTIGSQCRGVCSSPVSFSVLGG
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. The Superfamily domain, when present, is shown using underlining. 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

Subgroup CAR This EFD conserves 4/4 Subgroup-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
387 Trp (W) side chain stabilizes intermediate electrostatic stabiliser -- spectator ICS PubMed:9931258
444 Phe (F) side chain stabilizes intermediate electrostatic stabiliser -- spectator ICS PubMed:9931258
455 Asp (D) side chain initiates catalyzed reaction via protonation of substrate activation -- spectator ICS PubMed:9931258
581 Trp (W) side chain stabilizes intermediate electrostatic stabiliser -- spectator ICS PubMed:9931258
Family CAR This EFD conserves 4/5 Family-specific Conserved Alignment Residues.
Position Amino Acid Location Function Role Evidence Code Reference
387 Trp (W) side chain Stabilizes positive charge on C4 of intermediate electrostatic stabiliser -- spectator ISS
444 Phe (F) side chain Stabilizes positive charge on C8 of intermediate electrostatic stabiliser -- spectator ISS
455 Asp (D) side chain Initiates catalyzed reaction via protonation of substrate proton relay -- reactant ISS
581 Trp (W) side chain Stabilizes positive charge on C10 of intermediate electrostatic stabiliser -- spectator ISS

Structures

PDB ID Title Molecule Name Number of
EFDs		 Resolution (Å) Mutant? Het group Links
1W6K Structure Of Human Osc In Complex With Lanosterol Lanosterol Synthase 32 2.1 B-Octylglucoside • Lanosterol CSA • PDB • PDBSum
1W6J Structure Of Human Osc In Complex With Ro 48-8071 Lanosterol Synthase 32 2.2 B-Octylglucoside
(2 more ⇓) 		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 UniProtKB.

Curation History
Time Change Annotation Old Value New Value
May 2, 2014, 3 a.m. update curation agent updateSuperfamily.py setDomainBoundaries.py
update domain end position 698 693
update domain start position 6 1
EC number assigned by UniProtKB accession ID.