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Q9UVC3 (CP51_CUNEL) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lanosterol 14-alpha demethylase

EC=1.14.13.70
Alternative name(s):
CYPLI
Cytochrome P450 51
Cytochrome P450-14DM
Cytochrome P450-LIA1
Sterol 14-alpha demethylase
Gene names
Name:CYP51
OrganismCunninghamella elegans
Taxonomic identifier4853 [NCBI]
Taxonomic lineageEukaryotaFungiFungi incertae sedisBasal fungal lineagesMucoromycotinaMucoralesCunninghamellaceaeCunninghamella

Protein attributes

Sequence length512 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes C14-demethylation of lanosterol which is critical for ergosterol biosynthesis. It transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol By similarity.

Catalytic activity

Obtusifoliol + 3 O2 + 3 NADPH = 4-alpha-methyl-5-alpha-ergosta-8,14,24(28)-trien-3-beta-ol + formate + 3 NADP+ + 4 H2O.

Cofactor

Heme group By similarity.

Pathway

Steroid biosynthesis; zymosterol biosynthesis; zymosterol from lanosterol: step 1/6.

Subcellular location

Membrane Potential.

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Biological processLipid synthesis
Steroid biosynthesis
Sterol biosynthesis
   Cellular componentMembrane
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionMonooxygenase
Oxidoreductase
Gene Ontology (GO)
   Biological processsterol biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmembrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionelectron carrier activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

sterol 14-demethylase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 512512Lanosterol 14-alpha demethylase
PRO_0000052006

Sites

Metal binding4581Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9UVC3 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 5E10C9D415CA15B1

FASTA51257,677
        10         20         30         40         50         60 
MAIVSQISRF ITFTIISMGY SVLAVGVALT IHILSQLIVP KNPNEPPNVF SLIPVLGNAV 

        70         80         90        100        110        120 
QFGMNPVAFL QECQKKYGDV FTFTMVGKRV TVCLGADGNQ FVFNSKQNLS SAAEAYNHMT 

       130        140        150        160        170        180 
KYVFGPDVVY DAPHAVFMEQ KKFIKAGLNS DCFRQHVPMI VQETEEFFKK FNKPTGFIEA 

       190        200        210        220        230        240 
YETFGSLIIY TASRCLMGKE IRASLDGNVA KLYYDLDQGF KPINFIFPNL PLPSYRRRDV 

       250        260        270        280        290        300 
ACKKMADLYS SIIQRRKDEK DNNNADLLQA LMDATYKDGT HIPDHHIAGM MIAVLFGGQH 

       310        320        330        340        350        360 
TSATTSAWTI LELANRPDII KALREEQIEK LGSLKADLTF DNLKDLPLLE AAIRETLRLH 

       370        380        390        400        410        420 
PPIFQMMRRV VADKIVYEKN GMEIPKGNFI CAAPGVTQVD PTYFNEPTTY NPYRWIEKTD 

       430        440        450        460        470        480 
PVHQLEQGDD ANIDYGFGAV GISSKSPFLP FGAGRHRCIG EQFGYLQLKT VISTFIRTFD 

       490        500        510 
FDLDGKSVPK SDYTSMVVVP EHTAKVRYTW RE 

« Hide

References

[1]Craft D.L., Loper J.C.
Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 36112 / DSM 8217.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF046863 Genomic DNA. Translation: AAF20263.1.

3D structure databases

ProteinModelPortalQ9UVC3.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002403. Cyt_P450_E_grp-IV.
[Graphical view]
Gene3DG3DSA:1.10.630.10. Cyt_P450. 1 hit.
PfamPF00067. p450. 1 hit.
[Graphical view]
PRINTSPR00465. EP450IV.
PR00385. P450.
SUPFAMSSF48264. Cytochrome_P450. 1 hit.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCP51_CUNEL
AccessionPrimary (citable) accession number: Q9UVC3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: May 1, 2000
Last modified: September 21, 2011
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families