Top Level Name

  ⌊ Superfamily (core) Isoprenoid Synthase Type II

    ⌊ Subgroup Prenyltransferase Like 2

     ⌊ Family   private

  ⌊ FunctionalDomain Lanosterol Synthase (ID 3851)

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

References to Other Databases

Genbank

SpeciesGIAccessionProteome
Homo sapiens Taxon ID: 9606 984145 PRP URP

Uniprot

Protein NameAccessionEC Number Identifier
Lanosterol synthase P48449 5.4.99.7 ERG7_HUMAN (Swiss-Prot)

Sequence

Length of Enzyme (full-length): 590 | Length of Functional Domain: 590

1       10        20        30        40        50        60

DERAGREQTGLEAYALGLDTKNYFKDLPKAHTAFEGALNGMTFYVGLQAEDGHWTGDYGG
PLFLLPGLLITCHVARIPLPAGYREEIVRYLRSVQLPDGGWGLHIEDKSTVFGTALNYVS
LRILGVGPDDPDLVRARNILHKKGGAVAIPSWGKFWLAVLNVYSWEGLNTLFPEMWLFPD
WAPAHPSTLWCHCRQVYLPMSYCYAVRLSAAEDPLVQSLRQELYVEDFASIDWLAQRNNV
APDELYTPHSWLLRVVYALLNLYEHHHSAHLRQRAVQKLYEHIVADDRFTKSISIGPISK
TINMLVRWYVDGPASTAFQEHVSRIPDYLWMGLDGMKMQGTNGSQIWDTAFAIQALLEAG
GHHRPEFSSCLQKAHEFLRLSQVPDNPPDYQKYYRQMRKGGFSFSTLDCGWIVSDCTAEA
LKAVLLLQEKCPHVTEHIPRERLCDAVAVLLNMRNPDGGFATYETKRGGHLLELLNPSEV
FGDIMIDYTYVECTSAVMQALKYFHKRFPEHRAAEIRETLTQGLEFCRRQQRADGSWEGS
WGVCFTYGTWFGLEAFACMGQTYRDGTACAEVSRACDFLLSRQMADGGWG
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
347 Trp (W) side chain stabilizes intermediate electrostatic stabiliser -- spectator ICS PubMed:9931258
404 Phe (F) side chain stabilizes intermediate electrostatic stabiliser -- spectator ICS PubMed:9931258
415 Asp (D) side chain initiates catalyzed reaction via protonation of substrate activation -- spectator ICS PubMed:9931258
541 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
347 Trp (W) side chain Stabilizes positive charge on C4 of intermediate electrostatic stabiliser -- spectator ISS
404 Phe (F) side chain Stabilizes positive charge on C8 of intermediate electrostatic stabiliser -- spectator ISS
415 Asp (D) side chain Initiates catalyzed reaction via protonation of substrate proton relay -- reactant ISS
541 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.
EC number assigned by UniProtKB accession ID.