A0A852MPM2 · A0A852MPM2_9PASS

  • Protein
    Lanosterol 14-alpha demethylase
  • Gene
    Cyp39a1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

  • 24,25-dihydrolanosterol + 3 reduced [NADPH--hemoprotein reductase] + 3 O2 = 4,4-dimethyl-8,14-cholestadien-3beta-ol + formate + 3 oxidized [NADPH--hemoprotein reductase] + 4 H2O + 4 H+
    This reaction proceeds in the forward direction.
  • 24,25-dihydrolanosterol + reduced [NADPH--hemoprotein reductase] + O2 = 32-hydroxy-24,25-dihydrolanosterol + oxidized [NADPH--hemoprotein reductase] + H2O + H+
    This reaction proceeds in the forward direction.
  • 32-hydroxy-24,25-dihydrolanosterol + reduced [NADPH--hemoprotein reductase] + O2 = 32-oxo-24,25-dihydrolanosterol + oxidized [NADPH--hemoprotein reductase] + 2 H2O + H+
    This reaction proceeds in the forward direction.
  • 32-hydroxylanosterol + reduced [NADPH--hemoprotein reductase] + O2 = 32-oxolanosterol + oxidized [NADPH--hemoprotein reductase] + 2 H2O + H+
    This reaction proceeds in the forward direction.
  • 32-oxo-24,25-dihydrolanosterol + reduced [NADPH--hemoprotein reductase] + O2 = 4,4-dimethyl-8,14-cholestadien-3beta-ol + formate + oxidized [NADPH--hemoprotein reductase] + H2O + 2 H+
    This reaction proceeds in the forward direction.
  • 32-oxolanosterol + reduced [NADPH--hemoprotein reductase] + O2 = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + oxidized [NADPH--hemoprotein reductase] + H2O + 2 H+
    This reaction proceeds in the forward direction.
  • a 14alpha-formyl steroid + reduced [NADPH--hemoprotein reductase] + O2 = a Delta14 steroid + formate + oxidized [NADPH--hemoprotein reductase] + H2O + 2 H+
    This reaction proceeds in the forward direction.
  • a 14alpha-hydroxymethyl steroid + reduced [NADPH--hemoprotein reductase] + O2 = a 14alpha-formyl steroid + oxidized [NADPH--hemoprotein reductase] + 2 H2O + H+
    This reaction proceeds in the forward direction.
  • a 14alpha-methyl steroid + 3 reduced [NADPH--hemoprotein reductase] + 3 O2 = a Delta14 steroid + formate + 3 oxidized [NADPH--hemoprotein reductase] + 4 H2O + 4 H+
    This reaction proceeds in the forward direction.
    EC:1.14.14.154 (UniProtKB | ENZYME | Rhea)
  • a 14alpha-methyl steroid + reduced [NADPH--hemoprotein reductase] + O2 = a 14alpha-hydroxymethyl steroid + oxidized [NADPH--hemoprotein reductase] + H2O + H+
    This reaction proceeds in the forward direction.
  • lanosterol + 3 reduced [NADPH--hemoprotein reductase] + 3 O2 = 4,4-dimethyl-5alpha-cholesta-8,14,24-trien-3beta-ol + formate + 3 oxidized [NADPH--hemoprotein reductase] + 4 H2O + 4 H+
    This reaction proceeds in the forward direction.
    EC:1.14.14.154 (UniProtKB | ENZYME | Rhea)
  • lanosterol + reduced [NADPH--hemoprotein reductase] + O2 = 32-hydroxylanosterol + oxidized [NADPH--hemoprotein reductase] + H2O + H+
    This reaction proceeds in the forward direction.

Cofactor

heme (UniProtKB | Rhea| CHEBI:30413 )

Pathway

Lipid metabolism; bile acid biosynthesis.
Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site256substrate
Binding site393Fe (UniProtKB | ChEBI) of heme (UniProtKB | ChEBI); axial binding residue

GO annotations

AspectTerm
Cellular Componentendoplasmic reticulum membrane
Molecular Functionheme binding
Molecular Functioniron ion binding
Molecular Functionoxysterol 7-alpha-hydroxylase activity
Molecular Functionsteroid 7-alpha-hydroxylase activity
Biological Processbile acid biosynthetic process
Biological Processcholesterol homeostasis
Biological Processcholesterol metabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lanosterol 14-alpha demethylase
  • EC number

Gene names

    • Name
      Cyp39a1
    • ORF names
      PTEMEL_R14458

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • B10K-IZ-033-77
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Archelosauria > Archosauria > Dinosauria > Saurischia > Theropoda > Coelurosauria > Aves > Neognathae > Neoaves > Telluraves > Australaves > Passeriformes > Sylvioidea > Timaliidae > Pteruthius

Accessions

  • Primary accession
    A0A852MPM2

Proteomes

Subcellular Location

Keywords

Family & Domains

Sequence similarities

Belongs to the cytochrome P450 family.

Family and domain databases

Sequence

  • Sequence status
    Fragment
  • Length
    448
  • Mass (Da)
    51,360
  • Last updated
    2021-09-29 v1
  • Checksum
    62E27AC64275EDF1
LLFQLRNPSSPPCIRSWIPWFGAAFQFGKAPLEFIEQARNKHGPVFTIFALGKRFTFVTEEEGTEAFFKSEDLNFEQAVQQAVQNAVSVPAEAFYQNHGNLYSMMKGKMSPSNLHMFSGTLCKELHEHMAHLGTEGTGDLNDLVRHVMYPAVVNTLFGKGICPTSQSEIKEFEEHFQKYDEDFEYASQMPECFLRNWSKSKKWLLKLFEKVVLDAERTNPSEAASKTLLQHLLDNLQGKHLAPNYGLLMLWAAQANAVPVAFWTLAFILSNPAIYKKVMEDLASVFGKAGKDKLEVSEEDLKRMPFIKWCTLEAIRLRSPGAITKKVINPIRIKNFTIPAGDMLMLSPYWLHRNPKYFPDPEMFKPDRWKEANLEKNAFLDSFVAFGGGKHQCPGRWFAIMEIQLFVVLFLYKYEFVLLDAVPKESPLHLVGTQQPMAPLRVRYKCRE

Features

Showing features for non-terminal residue.

TypeIDPosition(s)Description
Non-terminal residue1
Non-terminal residue448

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WEIY01000383
EMBL· GenBank· DDBJ
NXY07382.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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